R = Retrieve links to Related sequences (neighbors).
Use the 
icon (if present) to retrieve links to the Sequence Retrieval System (SRS).
Use the 
icon (if present) to retrieve links to the Ligand Enzyme and Chemical Compound Database .
Use the 
icon (if present) to retrieve links to the Protein Data Bank database.
WARNING: Descriptions of 105 database sequences were not reported due to the
limiting value of parameter V = 50.
>gi|1706522|sp|P51820|DRTS_SOYBN BIFUNCTIONAL DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE (DHFR-TS) [INCLUDES: DIHYDROFOLATE
REDUCTASE ; THYMIDYLATE SYNTHASE ] >gi|1362048|pir||S55683
dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC
2.1.1.45) - soybean >gi|999190|gb|AAB34317.1| (S78087)
dihydrofolate reductase-thymidylate synthase, DHFR-TS=bifunctional
enzyme {EC 1.5.1.3} [Glycine max, seedling, Peptide, 530 aa]
>gi|1096144|prf||2111237A dihydrofolate reductase-thymidylate
synthase [Glycine max]
Length = 530
Frame 3 hits (HSPs): ___
Frame 2 hits (HSPs): _______________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | 530
0 150 300 450
__________________
Annotated Domains:
BLOCKS BL00075A: Dihydrofolate reductase protei 30..60
BLOCKS BL00075B: Dihydrofolate reductase protei 72..83
BLOCKS BL00075C: Dihydrofolate reductase protei 87..99
BLOCKS BL00075D: Dihydrofolate reductase protei 136..145
BLOCKS BL00091A: Thymidylate synthase proteins. 249..277
BLOCKS BL00091B: Thymidylate synthase proteins. 288..314
BLOCKS BL00091C: Thymidylate synthase proteins. 346..359
BLOCKS BL00091D: Thymidylate synthase proteins. 372..420
BLOCKS BL00091E: Thymidylate synthase proteins. 423..471
BLOCKS BL00091F: Thymidylate synthase proteins. 505..530
DOMO DM00206: DIHYDROFOLATEREDUCTASE 25..202
Entrez Domain: DIHYDROFOLATE REDUCTASE. 1..205
Entrez Domain: THYMIDYLATE SYNTHASE. 206..530
Entrez active site: BY SIMILARITY. 412
PFAM DiHfolate_red: Dihydrofolate reductase 28..173
PFAM thymidylat_synt: Thymidylate synthase 245..530
PRINTS DHFR1: Dihydrofolate reductase motif I - 38..48
PRINTS DHFR2: Dihydrofolate reductase motif II 52..60
PRINTS DHFR3: Dihydrofolate reductase motif III 72..83
PRINTS DHFR4: Dihydrofolate reductase motif IV 135..149
PRINTS THYMDSNTHASE1: Thymidylate synthase moti 288..309
PRINTS THYMDSNTHASE2: Thymidylate synthase moti 381..400
PRINTS THYMDSNTHASE3: Thymidylate synthase moti 407..422
PRINTS THYMDSNTHASE4: Thymidylate synthase moti 425..451
PRINTS THYMDSNTHASE5: Thymidylate synthase moti 463..480
PRODOM PD091247: DRTS_SOYBN 1..28
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 30..200
PRODOM PD203938: DRTS_SOYBN 202..243
PRODOM PD001180: TYSY(21) DRTS(13) TYSA(3) 245..529
PROSITE DHFR: Dihydrofolate reductase signature. 38..60
PROSITE THYMIDYLATE_SYNTHASE: Thymidylate syntha 392..420
__________________
Plus Strand HSPs:
Score = 748 (263.3 bits), Expect = 1.4e-75, Sum P(2) = 1.4e-75
Identities = 147/150 (98%), Positives = 148/150 (98%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL
Sbjct: 90 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 149
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAA 367
NVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAA
Sbjct: 150 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAA 209
Query: 368 ESAGQNIDPLLDNNSESMKFXVQDFSFSPK 457
ESAGQNIDPLLDNNSESMKF V+DFSF PK
Sbjct: 210 ESAGQNIDPLLDNNSESMKFEVKDFSFLPK 239
Score = 42 (14.8 bits), Expect = 1.4e-75, Sum P(2) = 1.4e-75
Identities = 9/13 (69%), Positives = 9/13 (69%), Frame = +3
Query: 441 FPFLXKMISXXHE 479
F FL KMIS HE
Sbjct: 234 FSFLPKMISERHE 246
>gi|1169424|sp|P45350|DRTS_DAUCA BIFUNCTIONAL DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE (DHFR-TS) [INCLUDES: DIHYDROFOLATE
REDUCTASE ; THYMIDYLATE SYNTHASE ] >gi|322727|pir||S32242
dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC
2.1.1.45) - carrot >gi|479740|pir||S35272 dihydrofolate reductase
(EC 1.5.1.3) / thymidylate synthase (EC 2.1.1.45) - carrot
>gi|288615|emb|CAA78954.1| (Z17306) dihydrofolate
reductase-thymidylate synthetase [Daucus carota]
Length = 528
Frame 2 hits (HSPs): _______________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | 528
0 150 300 450
__________________
Annotated Domains:
BLOCKS BL00075A: Dihydrofolate reductase protei 27..57
BLOCKS BL00075B: Dihydrofolate reductase protei 69..80
BLOCKS BL00075C: Dihydrofolate reductase protei 84..96
BLOCKS BL00075D: Dihydrofolate reductase protei 133..142
BLOCKS BL00091A: Thymidylate synthase proteins. 246..274
BLOCKS BL00091B: Thymidylate synthase proteins. 285..311
BLOCKS BL00091C: Thymidylate synthase proteins. 343..356
BLOCKS BL00091D: Thymidylate synthase proteins. 369..417
BLOCKS BL00091E: Thymidylate synthase proteins. 420..468
BLOCKS BL00091F: Thymidylate synthase proteins. 503..528
DOMO DM00206: DIHYDROFOLATEREDUCTASE 22..199
Entrez Domain: DIHYDROFOLATE REDUCTASE. 1..201
Entrez Domain: THYMIDYLATE SYNTHASE. 202..528
Entrez active site: BY SIMILARITY. 409
PFAM DiHfolate_red: Dihydrofolate reductase 25..170
PFAM thymidylat_synt: Thymidylate synthase 242..528
PRINTS DHFR1: Dihydrofolate reductase motif I - 35..45
PRINTS DHFR2: Dihydrofolate reductase motif II 49..57
PRINTS DHFR3: Dihydrofolate reductase motif III 69..80
PRINTS DHFR4: Dihydrofolate reductase motif IV 132..146
PRINTS THYMDSNTHASE1: Thymidylate synthase moti 285..306
PRINTS THYMDSNTHASE2: Thymidylate synthase moti 378..397
PRINTS THYMDSNTHASE3: Thymidylate synthase moti 404..419
PRINTS THYMDSNTHASE4: Thymidylate synthase moti 422..448
PRINTS THYMDSNTHASE5: Thymidylate synthase moti 460..477
PRODOM PD033973: DRTS(1) Q39687(1) 1..25
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 27..197
PRODOM PD190078: DRTS(1) Q39687(1) 199..240
PRODOM PD001180: TYSY(21) DRTS(13) TYSA(3) 242..527
PROSITE DHFR: Dihydrofolate reductase signature. 35..57
PROSITE THYMIDYLATE_SYNTHASE: Thymidylate syntha 389..417
__________________
Plus Strand HSPs:
Score = 552 (194.3 bits), Expect = 2.4e-52, P = 2.4e-52
Identities = 106/152 (69%), Positives = 123/152 (80%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GRLNVVLTRSGSFDIAT ENVVICGSM SALELLA SPY +S+EKVFVIGGGQI+REALN
Sbjct: 88 GRLNVVLTRSGSFDIATVENVVICGSMISALELLAGSPYCVSVEKVFVIGGGQIYREALN 147
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAAE 370
PGC+A+H+TEI+ IECDTF+P +D ++F+PWYSSFP VEN IRY FTTYVRVR+S AE
Sbjct: 148 APGCDAVHITEIEEHIECDTFIPLLDESVFQPWYSSFPLVENKIRYCFTTYVRVRNSVAE 207
Query: 371 SAGQNIDPLLDNNSESMKFXVQDFSFSPKNDF 466
Q D+ S+S F +Q+FSF PK F
Sbjct: 208 LTSQTNGCSSDSKSDSGNFEIQNFSFLPKTVF 239
>gi|7433454|pir||T14315 dihydrofolate reductase (EC 1.5.1.3) / thymidylate
synthase (EC 2.1.1.45) - carrot >gi|3097056|emb|CAA05895.1|
(AJ003139) dihydrofolate reductase-thymidylate synthetase [Daucus
carota]
Length = 577
Frame 2 hits (HSPs): ______________
__________________________________________________
Database sequence: | | | | | 577
0 150 300 450
Plus Strand HSPs:
Score = 552 (194.3 bits), Expect = 2.4e-52, P = 2.4e-52
Identities = 106/152 (69%), Positives = 123/152 (80%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GRLNVVLTRSGSFDIAT ENVVICGSM SALELLA SPY +S+EKVFVIGGGQI+REALN
Sbjct: 137 GRLNVVLTRSGSFDIATVENVVICGSMISALELLAGSPYCVSVEKVFVIGGGQIYREALN 196
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAAE 370
PGC+A+H+TEI+ IECDTF+P +D ++F+PWYSSFP VEN IRY FTTYVRVR+S AE
Sbjct: 197 APGCDAVHITEIEEHIECDTFIPLLDESVFQPWYSSFPLVENKIRYCFTTYVRVRNSVAE 256
Query: 371 SAGQNIDPLLDNNSESMKFXVQDFSFSPKNDF 466
Q D+ S+S F +Q+FSF PK F
Sbjct: 257 LTSQTNGCSSDSKSDSGNFEIQNFSFLPKTVF 288
>gi|6685381|sp|O81395|DRTS_MAIZE BIFUNCTIONAL DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE (DHFR-TS) [INCLUDES: DIHYDROFOLATE
REDUCTASE ; THYMIDYLATE SYNTHASE ] >gi|7433456|pir||T01684
dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC
2.1.1.45) - maize >gi|3309066|gb|AAC26003.1| (AF073488)
bifunctional dihydrofolate reductase-thymidylate synthase [Zea
mays]
Length = 521
Frame 2 hits (HSPs): _______________
__________________________________________________
Database sequence: | | | | | 521
0 150 300 450
Plus Strand HSPs:
Score = 533 (187.6 bits), Expect = 2.5e-50, P = 2.5e-50
Identities = 101/149 (67%), Positives = 123/149 (82%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GRLNV+LTRSGSFD AT ENVVICGSM SALELLA++PY LSIEKVFVIGGGQ+ RE L
Sbjct: 82 GRLNVILTRSGSFDFATVENVVICGSMESALELLASTPYCLSIEKVFVIGGGQVLREYLK 141
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAAE 370
P CEAIHLT+IQSSIECDTF+PPVDF++F+PWYSSFP +E+NIR+SF ++VRVR S AE
Sbjct: 142 GPACEAIHLTDIQSSIECDTFIPPVDFSVFQPWYSSFPVIESNIRHSFVSFVRVRKSVAE 201
Query: 371 SAGQNIDPLLDNNSESMKFXVQDFSFSPK 457
+ N + ++++ KF ++FSF PK
Sbjct: 202 THESNGKESTEVDTKNDKFETENFSFLPK 230
>gi|4544392|gb|AAD22302.1|AC007047_11 (AC007047) dihydrofolate
reductase-thymidylate synthase [Arabidopsis thaliana]
Length = 519
Frame 2 hits (HSPs): _______________
__________________________________________________
Database sequence: | | | | | 519
0 150 300 450
Plus Strand HSPs:
Score = 475 (167.2 bits), Expect = 3.4e-44, P = 3.4e-44
Identities = 93/153 (60%), Positives = 117/153 (76%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
SGRLNVVLTRSG FDIA ENVV C S+ SAL+LLAA PY LSIE+VFVIGGG I REAL
Sbjct: 85 SGRLNVVLTRSGGFDIANTENVVTCSSVDSALDLLAAPPYCLSIERVFVIGGGDILREAL 144
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAA 367
N P C+AIHLTEI +S++CDTF+P +D ++++PW SSFP EN +R+ FTT+VRV+SSA
Sbjct: 145 NRPSCDAIHLTEIDTSVDCDTFIPAIDTSVYQPWSSSFPVTENGLRFCFTTFVRVKSSAD 204
Query: 368 ESAGQNIDPLLDNNSESMKFXVQDFSFSPKNDF 466
ES+ ++ N S+S++F + F F PK F
Sbjct: 205 ESSDES------NGSQSLQFDGKKFLFLPKMVF 231
>gi|1169422|sp|Q05762|DRT1_ARATH BIFUNCTIONAL DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE 1 (DHFR-TS) [INCLUDES: DIHYDROFOLATE
REDUCTASE ; THYMIDYLATE SYNTHASE ] >gi|289193|gb|AAA32788.1|
(L08593) dihydrofolate reductase-thymidylate synthase [Arabidopsis
thaliana]
Length = 519
Frame 2 hits (HSPs): _______________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | 519
0 150 300 450
__________________
Annotated Domains:
BLOCKS BL00075A: Dihydrofolate reductase protei 25..55
BLOCKS BL00075B: Dihydrofolate reductase protei 67..78
BLOCKS BL00075C: Dihydrofolate reductase protei 82..94
BLOCKS BL00075D: Dihydrofolate reductase protei 131..140
BLOCKS BL00091A: Thymidylate synthase proteins. 238..266
BLOCKS BL00091B: Thymidylate synthase proteins. 277..303
BLOCKS BL00091C: Thymidylate synthase proteins. 335..348
BLOCKS BL00091D: Thymidylate synthase proteins. 361..409
BLOCKS BL00091E: Thymidylate synthase proteins. 412..460
BLOCKS BL00091F: Thymidylate synthase proteins. 494..519
DOMO DM00206: DIHYDROFOLATEREDUCTASE 20..197
DOMO DM00466: THYMIDYLATESYNTHASE 232..518
Entrez Domain: DIHYDROFOLATE REDUCTASE. 1..200
Entrez Domain: HINGE. 201..234
Entrez Domain: THYMIDYLATE SYNTHASE. 235..519
Entrez active site: BY SIMILARITY. 401
PFAM DiHfolate_red: Dihydrofolate reductase 23..168
PFAM thymidylat_synt: Thymidylate synthase 234..519
PRINTS DHFR1: Dihydrofolate reductase motif I - 33..43
PRINTS DHFR2: Dihydrofolate reductase motif II 47..55
PRINTS DHFR3: Dihydrofolate reductase motif III 67..78
PRINTS DHFR4: Dihydrofolate reductase motif IV 130..144
PRINTS THYMDSNTHASE1: Thymidylate synthase moti 277..298
PRINTS THYMDSNTHASE2: Thymidylate synthase moti 370..389
PRINTS THYMDSNTHASE3: Thymidylate synthase moti 396..411
PRINTS THYMDSNTHASE4: Thymidylate synthase moti 414..440
PRINTS THYMDSNTHASE5: Thymidylate synthase moti 452..469
PRODOM PD091242: DRT1_ARATH 1..23
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 25..192
PRODOM PD013664: DRT1(1) DRT2(1) 194..232
PRODOM PD001180: TYSY(21) DRTS(13) TYSA(3) 234..518
PROSITE DHFR: Dihydrofolate reductase signature. 33..55
PROSITE THYMIDYLATE_SYNTHASE: Thymidylate syntha 381..409
__________________
Plus Strand HSPs:
Score = 470 (165.4 bits), Expect = 1.2e-43, P = 1.2e-43
Identities = 92/153 (60%), Positives = 116/153 (75%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
SGRLNVVLTRSG FDIA ENVV C S+ SAL+LL A PY LSIE+VFVIGGG I REAL
Sbjct: 85 SGRLNVVLTRSGGFDIANTENVVTCSSVDSALDLLRAPPYCLSIERVFVIGGGDILREAL 144
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAA 367
N P C+AIHLTEI +S++CDTF+P +D ++++PW SSFP EN +R+ FTT+VRV+SSA
Sbjct: 145 NRPSCDAIHLTEIDTSVDCDTFIPAIDTSVYQPWSSSFPVTENGLRFCFTTFVRVKSSAD 204
Query: 368 ESAGQNIDPLLDNNSESMKFXVQDFSFSPKNDF 466
ES+ ++ N S+S++F + F F PK F
Sbjct: 205 ESSDES------NGSQSLQFDGKKFLFLPKMVF 231
>gi|1169423|sp|Q05763|DRT2_ARATH BIFUNCTIONAL DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE 2 (DHFR-TS) [INCLUDES: DIHYDROFOLATE
REDUCTASE ; THYMIDYLATE SYNTHASE ] >gi|7433457|pir||T05277
dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC
2.1.1.45) - Arabidopsis thaliana >gi|289195|gb|AAA32789.1| (L08594)
dihydrofolate reductase-thymidylate synthase [Arabidopsis thaliana]
>gi|3096926|emb|CAA18836.1| (AL023094) dihydrofolate
reductase-thymidylate synthase [Arabidopsis thaliana]
>gi|7270407|emb|CAB80174.1| (AL161585) dihydrofolate
reductase-thymidylate synthase [Arabidopsis thaliana]
Length = 518
Frame 2 hits (HSPs): ______________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | 518
0 150 300 450
__________________
Annotated Domains:
BLOCKS BL00075A: Dihydrofolate reductase protei 22..52
BLOCKS BL00075B: Dihydrofolate reductase protei 64..75
BLOCKS BL00075C: Dihydrofolate reductase protei 79..91
BLOCKS BL00075D: Dihydrofolate reductase protei 128..137
BLOCKS BL00091A: Thymidylate synthase proteins. 237..265
BLOCKS BL00091B: Thymidylate synthase proteins. 276..302
BLOCKS BL00091C: Thymidylate synthase proteins. 334..347
BLOCKS BL00091D: Thymidylate synthase proteins. 360..408
BLOCKS BL00091E: Thymidylate synthase proteins. 411..459
BLOCKS BL00091F: Thymidylate synthase proteins. 493..518
Entrez Domain: DIHYDROFOLATE REDUCTASE. 1..197
Entrez Domain: HINGE. 198..233
Entrez Domain: THYMIDYLATE SYNTHASE. 234..518
Entrez active site: BY SIMILARITY. 400
PFAM DiHfolate_red: Dihydrofolate reductase 20..165
PFAM thymidylat_synt: Thymidylate synthase 233..518
PRINTS DHFR1: Dihydrofolate reductase motif I - 30..40
PRINTS DHFR2: Dihydrofolate reductase motif II 44..52
PRINTS DHFR3: Dihydrofolate reductase motif III 64..75
PRINTS DHFR4: Dihydrofolate reductase motif IV 127..141
PRINTS THYMDSNTHASE1: Thymidylate synthase moti 276..297
PRINTS THYMDSNTHASE2: Thymidylate synthase moti 369..388
PRINTS THYMDSNTHASE3: Thymidylate synthase moti 395..410
PRINTS THYMDSNTHASE4: Thymidylate synthase moti 413..439
PRINTS THYMDSNTHASE5: Thymidylate synthase moti 451..468
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 22..189
PRODOM PD013664: DRT1(1) DRT2(1) 191..231
PRODOM PD001180: TYSY(21) DRTS(13) TYSA(3) 233..517
PROSITE DHFR: Dihydrofolate reductase signature. 30..52
PROSITE THYMIDYLATE_SYNTHASE: Thymidylate syntha 380..408
__________________
Plus Strand HSPs:
Score = 445 (156.6 bits), Expect = 5.2e-41, P = 5.2e-41
Identities = 86/128 (67%), Positives = 102/128 (79%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
SGRLNVVL+RS FDIA ENVV C S+ SAL+LLAA P+SLSIEKVFVIGGG I REAL
Sbjct: 82 SGRLNVVLSRSSGFDIANTENVVTCSSIDSALDLLAAPPFSLSIEKVFVIGGGDILREAL 141
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAA 367
N P CEAIH+TEI +SI+CDTF+P VD + ++PW SSFP EN +R+SFTT+VRV+SS+A
Sbjct: 142 NKPSCEAIHITEIDTSIDCDTFIPTVDTSAYQPWCSSFPICENGLRFSFTTHVRVKSSSA 201
Query: 368 ESAGQNID 391
A D
Sbjct: 202 GEASDESD 209
>gi|4567234|gb|AAD23649.1|AC007119_15 (AC007119) putative dihydrofolate
reductase-thymidylate synthase [Arabidopsis thaliana]
Length = 492
Frame 2 hits (HSPs): ________________
__________________________________________________
Database sequence: | | | | | 492
0 150 300 450
Plus Strand HSPs:
Score = 398 (140.1 bits), Expect = 5.0e-36, P = 5.0e-36
Identities = 84/152 (55%), Positives = 105/152 (69%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GRLN+VLT+S +IA ENV++ SM SALELLA PYSLSIEKVFVIGGG++ R +N
Sbjct: 88 GRLNIVLTKSSCHNIAIDENVLVSSSMESALELLATEPYSLSIEKVFVIGGGELLRNYMN 147
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAAE 370
C+AIHLTEI S+ CD F P VD +++RPWYSSFP VEN IRYSF TYVR R A
Sbjct: 148 ASICDAIHLTEIDISVPCDAFAPRVDTSLYRPWYSSFPVVENGIRYSFNTYVR-RKDAIV 206
Query: 371 SAGQNIDPLLDNNSESMKFXVQDFSFSPKNDF 466
+G+ + +ES ++++SF PK F
Sbjct: 207 GSGEK-----KSVAES---DLKEYSFLPKMVF 230
>gi|118980|sp|P28019|DYR_AEDAL DIHYDROFOLATE REDUCTASE >gi|103013|pir||S17984
dihydrofolate reductase (EC 1.5.1.3) - forest day mosquito
>gi|5556|emb|CAA42748.1| (X60192) dihydrofolate reductase [Aedes
albopictus]
Length = 186
Frame 2 hits (HSPs): ________________________________
Annotated Domains: _________________________________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 2..182
PFAM DiHfolate_red: Dihydrofolate reductase 5..149
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 29..37
PRINTS DHFR3: Dihydrofolate reductase motif III 49..60
PRINTS DHFR4: Dihydrofolate reductase motif IV 111..125
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..182
PROSITE DHFR: Dihydrofolate reductase signature. 15..37
__________________
Plus Strand HSPs:
Score = 193 (67.9 bits), Expect = 2.6e-14, P = 2.6e-14
Identities = 43/116 (37%), Positives = 68/116 (58%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
RLN++LTR S + +E V++C SM AL+ L +P IE V+++GG +++EA+
Sbjct: 69 RLNIILTRDPSANAYPSE-VMVCTSMQEALKKLDEAPLVNEIENVWIVGGNAVYKEAMQS 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPV--DFTIFRPWYSSFPK---VENNIRYSFTTYVRV 352
C I+LTEI+ + ECD F P + DF + + P+ EN I+Y + Y +V
Sbjct: 128 DRCHRIYLTEIKETFECDAFFPEITSDFQLVKN-DDDVPEDIQEENGIQYQYRIYEKV 184
>gi|6164599|gb|AAF04459.1|AF104106_1 (AF104106) dihydrofolate reductase
[Heliothis virescens]
Length = 185
Frame 2 hits (HSPs): ________________________________
__________________________________________________
Database sequence: | | | | | 185
0 50 100 150
Plus Strand HSPs:
Score = 163 (57.4 bits), Expect = 4.0e-11, P = 4.0e-11
Identities = 42/115 (36%), Positives = 60/115 (52%), Frame = +2
Query: 14 RLNVVLTRS-GSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
R+N+VLT + S E V++ + A++ + IE +VIGG I+R A+
Sbjct: 71 RVNIVLTHNVDSVKENVPEGVMVFPGLDEAIKYIEGRE---DIESTWVIGGSSIYRAAMT 127
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPW-YSSFP---KVENNIRYSFTTYVRV 352
P C I+LTEIQ S +CDTF P +D F P +VE NI Y F Y ++
Sbjct: 128 HPNCGKIYLTEIQKSFDCDTFFPNIDKQQFHLVDEEQIPGEKQVEGNISYYFRVYKKL 185
>gi|118982|sp|P00376|DYR_BOVIN DIHYDROFOLATE REDUCTASE >gi|66092|pir||RDBOD
dihydrofolate reductase (EC 1.5.1.3) - bovine
Length = 186
Frame 2 hits (HSPs): _______________________________
Annotated Domains: _________________________________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 2..183
PFAM DiHfolate_red: Dihydrofolate reductase 5..149
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 30..38
PRINTS DHFR3: Dihydrofolate reductase motif III 50..61
PRINTS DHFR4: Dihydrofolate reductase motif IV 111..125
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..183
PROSITE DHFR: Dihydrofolate reductase signature. 15..38
__________________
Plus Strand HSPs:
Score = 151 (53.2 bits), Expect = 7.4e-10, P = 7.4e-10
Identities = 35/113 (30%), Positives = 58/113 (51%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ ALEL+ + ++ V+++GG +++EA+N
Sbjct: 70 RINIVLSRELKEPPKGAH--FLAKSLDDALELIQDPELTNKVDVVWIVGGSSVYKEAMNK 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYSSFP---KVENNIRYSFTTY 343
PG + +T I E D F P +DF ++ P Y P + E I+Y F Y
Sbjct: 128 PGHVRLFVTRIMQEFESDAFFPEIDFEKYKLLPEYPGVPLDVQEEKGIKYKFEVY 182
>gi|118998|sp|P16184|DYR_PNECA DIHYDROFOLATE REDUCTASE >gi|100983|pir||A36177
dihydrofolate reductase (EC 1.5.1.3) [validated] - Pneumocystis
carinii >gi|7546368|pdb|2CD2|A Chain A, Ligand Induced
Conformational Changes In The Crystal Structures Of Pneumocystis
Carinii Dihydrofolate Reductase Complexes With Folate And Nadp+
>gi|7245416|pdb|1CD2|A Chain A, Ligand Induced Conformational
Changes In The Crystal Structures Of Pneumocystis Carinii
Dihydrofolate Reductase Complexes With Folate And Nadp+
>gi|2780979|pdb|1DAJ| Comparison Of Ternary Complexes Of
Pneumocystis Carinii And Wild Type Human Dihydrofolate Reductase
With Coenzyme Nadph And A Novel Classical Antitumor
Furo[2,3d]pyrimidine Antifolate >gi|7546369|pdb|3CD2|A Chain A,
Ligand Induced Conformational Changes In The Crystal Structures Of
Pneumocystis Carinii Dihydrofolate Reductase Complexes With Folate
And Nadp+ >gi|1311367|pdb|1DYR| The Structure Of Pneumocystis
Carinii Dihydrofolate Reductase To 1.9 Angstroms Resolution
>gi|7546370|pdb|4CD2|A Chain A, Ligand Induced Conformational
Changes In The Crystal Structures Of Pneumocystis Carinii
Dihydrofolate Reductase Complexes With Folate And Nadp+
>gi|169408|gb|AAA33787.1| (M26495) dihydrofolate reductase
[Pneumocystis carinii] >gi|169410|gb|AAA33788.1| (M26496)
dihydrofolate reductase [Pneumocystis carinii]
Length = 206
Frame 2 hits (HSPs): __________________________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | | 206
0 50 100 150 200
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 5..203
PFAM DiHfolate_red: Dihydrofolate reductase 8..157
PRINTS DHFR1: Dihydrofolate reductase motif I - 18..28
PRINTS DHFR2: Dihydrofolate reductase motif II 32..40
PRINTS DHFR3: Dihydrofolate reductase motif III 55..66
PRINTS DHFR4: Dihydrofolate reductase motif IV 119..133
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 10..167
PRODOM PD091252: DYR_PNECA 169..205
PROSITE DHFR: Dihydrofolate reductase signature. 18..40
__________________
Plus Strand HSPs:
Score = 147 (51.7 bits), Expect = 2.0e-09, P = 2.0e-09
Identities = 38/103 (36%), Positives = 59/103 (57%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLA---ASPYSLSIEKVFVIGGGQIFRE 181
GR+NVV+TR+ S D+ + S+ ALELL S S+ I ++FVIGG Q+++
Sbjct: 74 GRINVVITRNESLDLGNG--IHSAKSLDHALELLYRTYGSESSVQINRIFVIGGAQLYKA 131
Query: 182 ALNVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENN 319
A++ P + I T I I CD F P + F + W S + K +++
Sbjct: 132 AMDHPKLDRIMATIIYKDIHCDVFFP-LKFRD-KEWSSVWKKEKHS 175
>gi|11514295|pdb|1D8R|A Chain A, Structural Studies On Bio-Active Compounds.
Crystal Structure And Molecular Modeling Studies On The
Pneumocystis Carinii Dihydrofolate Reductase Cofactor Complex With
Tab, A Highly Selective Antifolate
Length = 205
Frame 2 hits (HSPs): __________________________
__________________________________________________
Database sequence: | | | | | | 205
0 50 100 150 200
Plus Strand HSPs:
Score = 147 (51.7 bits), Expect = 2.0e-09, P = 2.0e-09
Identities = 38/103 (36%), Positives = 59/103 (57%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLA---ASPYSLSIEKVFVIGGGQIFRE 181
GR+NVV+TR+ S D+ + S+ ALELL S S+ I ++FVIGG Q+++
Sbjct: 73 GRINVVITRNESLDLGNG--IHSAKSLDHALELLYRTYGSESSVQINRIFVIGGAQLYKA 130
Query: 182 ALNVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENN 319
A++ P + I T I I CD F P + F + W S + K +++
Sbjct: 131 AMDHPKLDRIMATIIYKDIHCDVFFP-LKFRD-KEWSSVWKKEKHS 174
>gi|631622|pir||S42446 dihydrofolate reductase (EC 1.5.1.3) - Chinese hamster
>gi|304504|gb|AAA36976.1| (K01165) dihydrofolate reductase 97
[Cricetulus griseus]
Length = 187
Frame 2 hits (HSPs): _______________________________
Annotated Domains: __________________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
__________________
Annotated Domains:
Entrez domain: type I dihydrofolate reductase h 4..126
PROSITE DHFR: Dihydrofolate reductase signature. 16..39
__________________
Plus Strand HSPs:
Score = 146 (51.4 bits), Expect = 2.5e-09, P = 2.5e-09
Identities = 35/113 (30%), Positives = 60/113 (53%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ +AL+L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPQGAH--FLAKSLDNALKLIEQPELADKVDMVWIVGGSSVYKEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYSS-FPKV--ENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y P+V E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFETDTFFPEIDLEKYKLLPEYPRVLPEVQEEKGIKYKFEVY 183
>gi|631621|pir||S42445 dihydrofolate reductase (EC 1.5.1.3) (clone A3-35) -
Chinese hamster >gi|304503|gb|AAA36974.1| (K01164) dihydrofolate
reductase 35 [Cricetulus griseus]
Length = 187
Frame 2 hits (HSPs): _______________________________
Annotated Domains: __________________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
__________________
Annotated Domains:
Entrez domain: type I dihydrofolate reductase h 4..126
PROSITE DHFR: Dihydrofolate reductase signature. 16..39
__________________
Plus Strand HSPs:
Score = 145 (51.0 bits), Expect = 3.2e-09, P = 3.2e-09
Identities = 35/113 (30%), Positives = 59/113 (52%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL+L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPQGAH--FLAKSLDDALKLIEQPELADKVDMVWIVGGSSVYKEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYSS-FPKV--ENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y P+V E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFETDTFFPEIDLEKYKLLPEYPRVLPEVQEEKGIKYKFEVY 183
>gi|1718261|gb|AAC57090.1| (U75698) ORF 2; dihydrofolate reductase DHFR homolog
[Kaposi's sarcoma-associated herpesvirus]
>gi|1778598|gb|AAC56947.1| (U83347) dihydrofolate reductase homolog
[Kaposi's sarcoma-associated herpesvirus]
>gi|3551757|gb|AAC34938.1| (U71365) dihydrofolate reductase
[Kaposi's sarcoma-associated herpesvirus]
Length = 210
Frame 2 hits (HSPs): ______________________________
__________________________________________________
Database sequence: | | | | | | 210
0 50 100 150 200
Plus Strand HSPs:
Score = 142 (50.0 bits), Expect = 6.7e-09, P = 6.7e-09
Identities = 40/122 (32%), Positives = 61/122 (50%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
+GR+NVVL+R+ A + S+ +AL L + + I+KV+VIGGG ++REAL
Sbjct: 68 AGRINVVLSRTLETPPPGAH--FLASSLDAALGLARSPELAQQIDKVWVIGGGDLYREAL 125
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIF---RPWYSSFPKV--ENNIRYSFTTYVRV 352
P + LT + CD F+ + P +V E I Y F TY++V
Sbjct: 126 TGPWPVRLFLTRVLHDFACDVFLSHDSLAAYARVNPKPGEQERVFQERGIFYMFETYIKV 185
Query: 353 RSSA 364
S+
Sbjct: 186 TQSS 189
>gi|2246550|gb|AAB62675.1| (U93872) ORF 02, dihydrofolate reductase (DHFR)
homolog [Kaposi's sarcoma-associated herpesvirus]
Length = 210
Frame 2 hits (HSPs): ______________________________
__________________________________________________
Database sequence: | | | | | | 210
0 50 100 150 200
Plus Strand HSPs:
Score = 142 (50.0 bits), Expect = 6.7e-09, P = 6.7e-09
Identities = 40/122 (32%), Positives = 61/122 (50%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
+GR+NVVL+R+ A + S+ +AL L + + I+KV+VIGGG ++REAL
Sbjct: 68 AGRINVVLSRTLETPPPGAH--FLASSLDAALGLARSPELAQQIDKVWVIGGGNLYREAL 125
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFTIF---RPWYSSFPKV--ENNIRYSFTTYVRV 352
P + LT + CD F+ + P +V E I Y F TY++V
Sbjct: 126 TGPWPVRLFLTRVLHDFACDVFLSHDSLAAYARVNPKPGEQERVFQERGIFYMFETYIKV 185
Query: 353 RSSA 364
S+
Sbjct: 186 TQSS 189
>gi|289982|gb|AAA36972.1| (L15311) dihydrofolate reductase [Cricetulus sp.]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 140 (49.3 bits), Expect = 1.1e-08, P = 1.1e-08
Identities = 34/113 (30%), Positives = 59/113 (52%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ +AL+L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPQGAH--FLAKSLDNALKLIEQPELADKVDMVWIVGGSSVYKEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLEKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|729385|sp|P17719|DYR_DROME DIHYDROFOLATE REDUCTASE >gi|1079065|pir||A53803
dihydrofolate reductase (EC 1.5.1.3) - fruit fly (Drosophila
melanogaster) >gi|500630|gb|AAA19051.1| (U06861) dihydrofolate
reductase [Drosophila melanogaster]
Length = 182
Frame 2 hits (HSPs): ______________________________
Annotated Domains: _________________________________________________
__________________________________________________
Database sequence: | | | | | 182
0 50 100 150
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 2..179
PFAM DiHfolate_red: Dihydrofolate reductase 5..146
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 29..37
PRINTS DHFR3: Dihydrofolate reductase motif III 49..60
PRINTS DHFR4: Dihydrofolate reductase motif IV 108..122
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..179
PROSITE DHFR: Dihydrofolate reductase signature. 15..37
__________________
Plus Strand HSPs:
Score = 140 (49.3 bits), Expect = 1.1e-08, P = 1.1e-08
Identities = 33/107 (30%), Positives = 61/107 (57%), Frame = +2
Query: 14 RLNVVL-TRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
RLN+VL T D+ + V++C ++ +A+++L +E ++++GG ++ EA+
Sbjct: 69 RLNIVLSTTLQESDLP--KGVLLCPNLETAMKILEEQN---EVENIWIVGGSGVYEEAMA 123
Query: 191 VPGCEAIHLTEIQSSIECDTFMP--PVDFTIFRPWYSSFP---KVENNIRYSF 334
P C +++T+I +CDTF P P F P S P + EN I++ +
Sbjct: 124 SPRCHRLYITQIMQKFDCDTFFPAIPDSFREVAP-DSDMPLGVQEENGIKFEY 175
>gi|4503323 ref|NP_000782.1| dihydrofolate reductase [Homo sapiens]
>gi|118992|sp|P00374|DYR_HUMAN DIHYDROFOLATE REDUCTASE
>gi|1070440|pir||RDHUD dihydrofolate reductase (EC 1.5.1.3)
[validated] - human >gi|30775|emb|CAA23765.1| (V00507) coding
sequence of DHFR (1 is 1st base in codon) (561 is 3rd base in
codon) [Homo sapiens] >gi|182717|gb|AAA58484.1| (J00139)
dihydrofolate reductase (EC 1.5.1.3) [Homo sapiens]
>gi|182724|gb|AAA58485.1| (J00140) dihydrofolate reductase [Homo
sapiens] >gi|1617080|emb|CAA25409.1| (X00855) dihydrofolate
reductase [Homo sapiens] >gi|12652875|gb|AAH00192.1|AAH00192
(BC000192) dihydrofolate reductase [Homo sapiens]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 70 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 127
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 128 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 183
>gi|118989|sp|P27421|DYR_HSVS7 DIHYDROFOLATE REDUCTASE (DHFR)
>gi|93182|pir||S14840 dihydrofolate reductase (EC 1.5.1.3) -
saimiriine herpesvirus 1 (strain 484-77) >gi|60413|emb|CAA41575.1|
(X58774) ORF - has homology to dihydrofolate reductase [Saimiriine
herpesvirus 2]
Length = 186
Frame 2 hits (HSPs): _______________________________
Annotated Domains: _________________________________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 3..183
PFAM DiHfolate_red: Dihydrofolate reductase 6..149
PRINTS DHFR1: Dihydrofolate reductase motif I - 16..26
PRINTS DHFR2: Dihydrofolate reductase motif II 31..39
PRINTS DHFR3: Dihydrofolate reductase motif III 50..61
PRINTS DHFR4: Dihydrofolate reductase motif IV 111..125
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 8..183
PROSITE DHFR: Dihydrofolate reductase signature. 16..39
__________________
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 33/113 (29%), Positives = 60/113 (53%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL++ +I + + S++ AL+L+ + ++ V++IGG ++++A+N
Sbjct: 70 RINLVLSKKLK-EIPHGAHF-LARSLNDALKLIEQPEFVNKVDMVWIIGGSSVYKDAMNY 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFRPW--YSSFP---KVENNIRYSFTTY 343
+ +T I S E DTF P +D ++P Y P + E IRY F Y
Sbjct: 128 SSHLKLFVTRIMQSFETDTFFPEIDLKKYKPLIEYPGVPSNTQEEKGIRYKFEVY 182
>gi|66091|pir||RDHY75 dihydrofolate reductase (EC 1.5.1.3)
(antifolate-resistant variant) - Chinese hamster
Length = 186
Frame 2 hits (HSPs): _______________________________
Annotated Domains: __________________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
__________________
Annotated Domains:
Entrez domain: type I dihydrofolate reductase h 3..125
Entrez binding site: substrate (Glu, Phe, Asn, 30
Entrez binding site: substrate (Glu, Phe, Asn, 34
Entrez binding site: substrate (Glu, Phe, Asn, 64
Entrez binding site: substrate (Glu, Phe, Asn, 70
PROSITE DHFR: Dihydrofolate reductase signature. 15..38
__________________
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 34/113 (30%), Positives = 58/113 (51%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL+L+ + ++ V+++GG +++EA+N
Sbjct: 70 RINIVLSRELKEPPQGAH--FLAKSLDDALKLIEQPELADKVDMVWIVGGSSVYKEAMNQ 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 128 PGHLRLFVTRIMQEFESDTFFPEIDLEKYKLLPEYPGVLSEVQEEKGIKYKFEVY 182
>gi|1352324|sp|P04753|DYR_MESAU DIHYDROFOLATE REDUCTASE
>gi|191046|gb|AAA36971.1| (M37124) dihydrofolate reductase
[Cricetulus sp.]
Length = 187
Frame 2 hits (HSPs): _______________________________
Annotated Domains: ________________________________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
__________________
Annotated Domains:
Entrez other site: INVOLVED IN MTX BINDING (BY 8..10
Entrez other site: INVOLVED IN MTX BINDING (BY 23
Entrez other site: INVOLVED IN MTX BINDING (BY 31..32
Entrez other site: INVOLVED IN MTX BINDING (BY 35
Entrez other site: INVOLVED IN MTX BINDING (BY 37
Entrez other site: INVOLVED IN MTX BINDING (BY 60..70
Entrez other site: INVOLVED IN MTX BINDING (BY 116
Entrez other site: INVOLVED IN MTX BINDING (BY 137
PFAM DiHfolate_red: Dihydrofolate reductase 5..149
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 30..38
PRINTS DHFR3: Dihydrofolate reductase motif III 50..61
PRINTS DHFR4: Dihydrofolate reductase motif IV 111..125
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..183
PROSITE DHFR: Dihydrofolate reductase signature. 16..39
__________________
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 34/113 (30%), Positives = 58/113 (51%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL+L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPQGAH--FLAKSLDDALKLIEQPELADKVDMVWIVGGSSVYKEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLEKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|2914338|pdb|1HFR| Comparison Of Ternary Crystal Complexes Of Human
Dihydrofolate Reductase With Nadph And A Classical Antitumor
Furopyrimdine >gi|3212581|pdb|1OHJ| Human Dihydrofolate Reductase,
Monoclinic (P21) Crystal Form >gi|3212582|pdb|1OHK| Human
Dihydrofolate Reductase, Orthorhombic (P21 21 21) Crystal Form
>gi|229890|pdb|1DRF| Dihydrofolate Reductase (E.C.1.5.1.3) Complex
With Folate >gi|229860|pdb|1DHF|A Chain A, Dihydrofolate Reductase
(E.C.1.5.1.3) (DHFR) Complex With Folate >gi|229861|pdb|1DHF|B
Chain B, Dihydrofolate Reductase (E.C.1.5.1.3) (DHFR) Complex With
Folate >gi|230481|pdb|2DHF|A Chain A, Dihydrofolate Reductase
(E.C.1.5.1.3) (DHFR) Complex With 5-Deazafolate
>gi|230482|pdb|2DHF|B Chain B, Dihydrofolate Reductase
(E.C.1.5.1.3) (DHFR) Complex With 5-Deazafolate
>gi|223651|prf||0905195A reductase,dihydrofolate [Homo sapiens]
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 69 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 126
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 127 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 182
>gi|223661|prf||0906214A reductase,dihydrofolate [Homo sapiens]
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 69 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTQQPELANKVDMVWIVGGSSVYKEAMN 126
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 127 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 182
>gi|304502|gb|AAA36970.1| (M19869) dihydrofolate reductase (EC 1.5.1.3)
[Cricetulus sp.]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 34/113 (30%), Positives = 58/113 (51%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL+L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPQGAH--FLAKSLDDALKLIEQPELADKVDMVWIVGGSSVYKEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLEKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|1065363|pdb|1DLR| Dihydrofolate Reductase (E.C.1.5.1.3) (Dhfr) Mutant
With Leu 22 Replaced By Phe (L22f) Complexed With Nadph And
Piritrexim (Ptx)
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 69 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 126
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 127 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 182
>gi|1065364|pdb|1DLS| Dihydrofolate Reductase (E.C.1.5.1.3) (Dhfr) Mutant
With Leu 22 Replaced By Tyr (L22y) Complexed With Nadph And
Methotrexate
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 69 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 126
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 127 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 182
>gi|3660048|pdb|1BOZ|A Chain A, Structure-Based Design And Synthesis Of
Lipophilic 2,4- Diamino-6-Substituted Quinazolines And Their
Evaluation As Inhibitors Of Dihydrofolate Reductase And Potential
Antitumor Agents >gi|2914336|pdb|1HFP| Comparison Of Ternary
Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A
Classical Antitumor Furopyrimdine
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 69 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 126
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 127 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 182
>gi|2914337|pdb|1HFQ| Comparison Of Ternary Crystal Complexes Of Human
Dihydrofolate Reductase With Nadph And A Classical Antitumor
Furopyrimdine
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 69 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 126
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 127 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 182
>gi|7300157|gb|AAF55324.1| (AE003713) Dhfr gene product [Drosophila
melanogaster]
Length = 182
Frame 2 hits (HSPs): ______________________________
__________________________________________________
Database sequence: | | | | | 182
0 50 100 150
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 1.4e-08, P = 1.4e-08
Identities = 33/107 (30%), Positives = 61/107 (57%), Frame = +2
Query: 14 RLNVVL-TRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
RLN+VL T D+ + V++C ++ +A+++L +E ++++GG ++ EA+
Sbjct: 69 RLNIVLSTTLQESDLP--KGVLLCPNLETAMKILEEQN---EVENIWIVGGSGVYEEAMA 123
Query: 191 VPGCEAIHLTEIQSSIECDTFMP--PVDFTIFRPWYSSFP---KVENNIRYSF 334
P C +++T+I +CDTF P P F P S P + EN I++ +
Sbjct: 124 SPRCHRLYITKIMQKFDCDTFFPAIPDSFREVAP-DSDMPLGVQEENGIKFEY 175
>gi|50700|emb|CAA24112.1| (V00734) DHF reductase [Mus musculus]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 138 (48.6 bits), Expect = 1.8e-08, P = 1.8e-08
Identities = 34/113 (30%), Positives = 57/113 (50%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPRGAH--FLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|50711|emb|CAA39544.1| (X56066) dihydrofolate reductase [Mus musculus]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 138 (48.6 bits), Expect = 1.8e-08, P = 1.8e-08
Identities = 34/113 (30%), Positives = 57/113 (50%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPRGAH--FLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|7106289 ref|NP_034179.1| dihydrofolate reductase [Mus musculus]
>gi|1706542|sp|P00375|DYR_MOUSE DIHYDROFOLATE REDUCTASE
>gi|387160|gb|AAA37638.1| (J00388) dihydrofolate reductase ( [Mus
musculus] >gi|439209|gb|AAA37523.1| (L26316) dihydrofolate
reductase [Mus musculus]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 138 (48.6 bits), Expect = 1.8e-08, P = 1.8e-08
Identities = 34/113 (30%), Positives = 57/113 (50%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPRGAH--FLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|2144346|pir||RDMSD dihydrofolate reductase (EC 1.5.1.3),
methotrexate-resistant - mouse
Length = 187
Frame 2 hits (HSPs): _______________________________
Annotated Domains: __________________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
__________________
Annotated Domains:
Entrez domain: type I dihydrofolate reductase h 4..126
Entrez binding site: substrate (Glu, Phe, Asn, 31
Entrez binding site: substrate (Glu, Phe, Asn, 35
Entrez binding site: substrate (Glu, Phe, Asn, 65
Entrez binding site: substrate (Glu, Phe, Asn, 71
PROSITE DHFR: Dihydrofolate reductase signature. 16..39
__________________
Plus Strand HSPs:
Score = 138 (48.6 bits), Expect = 1.8e-08, P = 1.8e-08
Identities = 34/113 (30%), Positives = 57/113 (50%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPRGAH--FLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVY 183
>gi|2842720|sp|Q93341|DYR_CAEEL PUTATIVE DIHYDROFOLATE REDUCTASE
>gi|7497109|pir||T19778 hypothetical protein C36B1.7 -
Caenorhabditis elegans >gi|3874779|emb|CAB02272.1| (Z80215)
contains similarity to Pfam domain: PF00186 (Dihydrofolate
reductase), Score=208.5, E-value=3.3e-60, N=1~cDNA EST yk104e11.3
comes from this gene~cDNA EST yk104e11.5 comes from this gene~cDNA
EST yk369e10.5 comes from this gene [Caenorhabditis>
Length = 189
Frame 2 hits (HSPs): ________________________
Annotated Domains: ________________________________________________
__________________________________________________
Database sequence: | | | | | 189
0 50 100 150
__________________
Annotated Domains:
PFAM DiHfolate_red: Dihydrofolate reductase 5..148
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 29..37
PRINTS DHFR3: Dihydrofolate reductase motif III 49..60
PRINTS DHFR4: Dihydrofolate reductase motif IV 110..124
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..183
PROSITE DHFR: Dihydrofolate reductase signature. 15..37
__________________
Plus Strand HSPs:
Score = 137 (48.2 bits), Expect = 2.3e-08, P = 2.3e-08
Identities = 30/89 (33%), Positives = 53/89 (59%), Frame = +2
Query: 8 SGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREAL 187
+GRLN+VL+R +++ ++ S+ +A++LL+ P+ SIE ++ IGG +I+ AL
Sbjct: 67 AGRLNIVLSRQ--LPAQKSDDYIVVNSLEAAMKLLSEPPFVDSIETIWNIGGAEIYDLAL 124
Query: 188 NVPGCEAIHLTEIQSSIECDTFMPPVDFT 274
+ IHLT I + E D + +DF+
Sbjct: 125 RENLVDEIHLTRIFKNFEADVHLKSLDFS 153
>gi|12731598 ref|XP_003991.2| dihydrofolate reductase [Homo sapiens]
Length = 262
Frame 2 hits (HSPs): _______________________
__________________________________________________
Database sequence: | | | | | | | 262
0 50 100 150 200 250
Plus Strand HSPs:
Score = 139 (48.9 bits), Expect = 3.0e-08, P = 3.0e-08
Identities = 35/114 (30%), Positives = 58/114 (50%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+N+VL+R A + S+ AL+L + ++ V+++GG +++EA+N
Sbjct: 145 GRINLVLSRELKEPPQGAH--FLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMN 202
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E I+Y F Y
Sbjct: 203 HPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVY 258
>gi|9625957 ref|NP_040203.1| dihydrofolate reductase [Saimiriine herpesvirus 2]
>gi|118990|sp|P09503|DYR_HSVSA DIHYDROFOLATE REDUCTASE (DHFR)
>gi|66094|pir||RDBE11 dihydrofolate reductase (EC 1.5.1.3) -
saimiriine herpesvirus 1 (strain 11) >gi|60322|emb|CAA45624.1|
(X64346) dihydrofolate reductase [Saimiriine herpesvirus 2]
>gi|331032|gb|AAA46154.1| (M19237) DHFR (dihydrofolate reductase)
(EC 1.5.1.3) [Saimiriine herpesvirus 2] >gi|609446|gb|AAA58726.1|
(M28071) dihydrofolate reductase [Saimiriine herpesvirus 2]
Length = 187
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 187
0 50 100 150
Plus Strand HSPs:
Score = 135 (47.5 bits), Expect = 3.7e-08, P = 3.7e-08
Identities = 34/114 (29%), Positives = 61/114 (53%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR+NVVL++ ++ + + S+ AL+L + ++ V++IGG +++EA++
Sbjct: 70 GRINVVLSKELK-ELPHRAHF-LAKSLDDALKLTEQPELANKVDMVWIIGGSSVYKEAMS 127
Query: 191 VPGCEA-IHLTEIQSSIECDTFMPPVDFTIFR-----PWYSSFPKVENNIRYSFTTY 343
P C+ + +T I ECDTF P D ++ P S + E +I+Y F Y
Sbjct: 128 YP-CDLKLFVTRIMQDFECDTFFPEFDLEKYKLLIEYPSVLSNVQEEKSIKYKFEVY 183
>gi|229623|prf||770500A reductase,dihydrofolate [Mus musculus]
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 135 (47.5 bits), Expect = 3.7e-08, P = 3.7e-08
Identities = 33/113 (29%), Positives = 57/113 (50%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL L+ + ++ V+++GG ++ +A+N
Sbjct: 70 RINIVLSRELKEPPRGAH--FLAKSLDDALRLIQEPELASKVDMVWIVGGSSVYEQAMNE 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYS---SFPKVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ P Y S + E+ I+Y F Y
Sbjct: 128 PGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEDGIKYKFEVY 182
>gi|118991|sp|P22573|DYR_HSVSC DIHYDROFOLATE REDUCTASE >gi|66095|pir||RDBEHS
dihydrofolate reductase (EC 1.5.1.3) - saimiriine herpesvirus 1
(strain 488) >gi|331010|gb|AAA72932.1| (M55264) dihydrofolate
reductase [Saimiriine herpesvirus 2]
Length = 213
Frame 2 hits (HSPs): ____________________________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | | 213
0 50 100 150 200
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 3..183
PFAM DiHfolate_red: Dihydrofolate reductase 6..149
PRINTS DHFR1: Dihydrofolate reductase motif I - 16..26
PRINTS DHFR2: Dihydrofolate reductase motif II 31..39
PRINTS DHFR3: Dihydrofolate reductase motif III 50..61
PRINTS DHFR4: Dihydrofolate reductase motif IV 111..125
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 8..183
PRODOM PD091248: DYR_HSVSC 185..212
PROSITE DHFR: Dihydrofolate reductase signature. 16..39
__________________
Plus Strand HSPs:
Score = 131 (46.1 bits), Expect = 1.0e-07, P = 1.0e-07
Identities = 31/116 (26%), Positives = 61/116 (52%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL++ +I + + S++ AL+L+ +++V++IGG ++++A+N
Sbjct: 70 RINLVLSKKLK-EIPHGAHF-LARSLNDALKLIEQPELVNKVDRVWIIGGSSVYKDAMNY 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR-----PWYSSFPKVENNIRYSFTTYVRV 352
+ +T I S E DTF P +D ++ P S + E I+Y F Y ++
Sbjct: 128 SSHLKLFVTRIMQSFETDTFFPEIDLKNYKLLIEYPGVPSNTQEEKGIKYKFEVYEKI 185
>gi|118997|sp|P00377|DYR_PIG DIHYDROFOLATE REDUCTASE >gi|66093|pir||RDPGD
dihydrofolate reductase (EC 1.5.1.3) - pig
Length = 186
Frame 2 hits (HSPs): _______________________________
__________________________________________________
Database sequence: | | | | | 186
0 50 100 150
Plus Strand HSPs:
Score = 130 (45.8 bits), Expect = 1.2e-07, P = 1.2e-07
Identities = 33/113 (29%), Positives = 55/113 (48%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL+L ++ V+++GG +++EA+N
Sbjct: 70 RINIVLSRELKEPPQGAH--FLAKSLDDALKLTEQPELKDKVDMVWIVGGSSVYKEAMNK 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYSSFP---KVENNIRYSFTTY 343
PG + +T I E DTF P +D ++ S P + E I+Y F Y
Sbjct: 128 PGHIRLFVTRIMKEFESDTFFPEIDLEKYKLLSECSGVPSDVQEEKGIKYKFEVY 182
>gi|11252926|pir||G81214 dihydrofolate reductase NMB0308 [imported] - Neisseria
meningitidis (group B strain MD58) >gi|7225528|gb|AAF40754.1|
(AE002387) dihydrofolate reductase [Neisseria meningitidis MC58]
Length = 162
Frame 2 hits (HSPs): _________________________________
__________________________________________________
Database sequence: | | | | | 162
0 50 100 150
Plus Strand HSPs:
Score = 127 (44.7 bits), Expect = 2.6e-07, P = 2.6e-07
Identities = 35/113 (30%), Positives = 60/113 (53%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR N+V++R + A AE S+ +AL L A + E+ ++GG QI+ +A+
Sbjct: 59 GRRNIVISRQADYCAAGAETAA---SLEAALALCAGA------EEAVIMGGAQIYGQAM- 108
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENN-IRYSFTTYVR 349
P + +TE+ S+E D F P +D T ++ + +V + RY+F Y+R
Sbjct: 109 -PLATDLRITEVDLSVEGDAFFPAIDRTHWKEAERTERRVSSKGTRYAFVHYLR 161
>gi|118996|sp|P04174|DYR_NEIGO DIHYDROFOLATE REDUCTASE >gi|66103|pir||RDNHD
dihydrofolate reductase (EC 1.5.1.3) - Neisseria gonorrhoeae
Length = 162
Frame 2 hits (HSPs): _________________________________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | 162
0 50 100 150
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 2..160
PFAM DiHfolate_red: Dihydrofolate reductase 5..130
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 29..37
PRINTS DHFR3: Dihydrofolate reductase motif III 42..53
PRINTS DHFR4: Dihydrofolate reductase motif IV 94..108
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..132
PRODOM PD091243: DYR_NEIGO 134..161
PROSITE DHFR: Dihydrofolate reductase signature. 15..37
__________________
Plus Strand HSPs:
Score = 124 (43.7 bits), Expect = 5.4e-07, P = 5.4e-07
Identities = 35/112 (31%), Positives = 59/112 (52%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR N+V++R + A AE V S+ AL L A + E+ ++GG QI+ +A+
Sbjct: 59 GRRNIVISRQADYCAAGAETVA---SLEVALALCAGA------EEAVIMGGAQIYGQAM- 108
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENN-IRYSFTTYV 346
P + +TE+ S+E D F P +D T +R + +V + + Y+F Y+
Sbjct: 109 -PLATDLRITEVDLSVEGDAFFPEIDRTHWREAERTERRVSSKGVAYTFVHYL 160
>gi|1619305|emb|CAA24113.1| (V00735) dihydrofolate reductase [Mus musculus]
Length = 162
Frame 2 hits (HSPs): __________________________
__________________________________________________
Database sequence: | | | | | 162
0 50 100 150
Plus Strand HSPs:
Score = 124 (43.7 bits), Expect = 5.4e-07, P = 5.4e-07
Identities = 26/85 (30%), Positives = 45/85 (52%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL L+ + ++ V+++GG +++EA+N
Sbjct: 71 RINIVLSRELKEPPRGAH--FLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQ 128
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVD 268
PG + +T I E DTF P +D
Sbjct: 129 PGHLRLFVTRIMQEFESDTFFPEID 153
>gi|118985|sp|P00378|DYR_CHICK DIHYDROFOLATE REDUCTASE >gi|66096|pir||RDCHD
dihydrofolate reductase (EC 1.5.1.3) - chicken >gi|231296|pdb|8DFR|
Dihydrofolate Reductase (E.C.1.5.1.3) >gi|442841|pdb|1DR6|
Dihydrofolate Reductase (E.C.1.5.1.3) With Cys 11 Covalently Bound
To Mercuribenzoate Complex With Nicotinamide Adenine Dinucleotide
Phosphate And Biopterin >gi|442836|pdb|1DR1| Dihydrofolate
Reductase (E.C.1.5.1.3) Complex With Nadp+ And Biopterin
>gi|442838|pdb|1DR3| Dihydrofolate Reductase (E.C.1.5.1.3) Complex
With Oxidized Thionicotinamide Adenine Dinucleotide Phosphate And
Biopterin >gi|442839|pdb|1DR4| Dihydrofolate Reductase
(E.C.1.5.1.3) With Cys 11 Modified With Methyl Mercury Complex With
Nicotinamide Adenine Dinucleotide Phosphate And Biopterin
>gi|442837|pdb|1DR2| Dihydrofolate Reductase (E.C.1.5.1.3) Complex
With Oxidized Thionicotinamide Adenine Dinucleotide Phosphate
>gi|442840|pdb|1DR5| Dihydrofolate Reductase (E.C.1.5.1.3) With
Cys 11 Modified With Methyl Mercury Complex With Nicotinamide
Adenine Dinucleotide Phosphate >gi|442842|pdb|1DR7| Dihydrofolate
Reductase (E.C.1.5.1.3) With Cys 11 Covalently Bound To
Mercuribenzoate Complex With Nicotinamide Adenine Dinucleotide
Phosphate
Length = 189
Frame 2 hits (HSPs): ______________________________
Annotated Domains: _________________________________________________
__________________________________________________
Database sequence: | | | | | 189
0 50 100 150
__________________
Annotated Domains:
DOMO DM00206: DIHYDROFOLATEREDUCTASE 2..183
PFAM DiHfolate_red: Dihydrofolate reductase 5..149
PRINTS DHFR1: Dihydrofolate reductase motif I - 15..25
PRINTS DHFR2: Dihydrofolate reductase motif II 30..38
PRINTS DHFR3: Dihydrofolate reductase motif III 50..61
PRINTS DHFR4: Dihydrofolate reductase motif IV 111..125
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 7..183
PROSITE DHFR: Dihydrofolate reductase signature. 15..38
__________________
Plus Strand HSPs:
Score = 121 (42.6 bits), Expect = 1.1e-06, P = 1.1e-06
Identities = 32/113 (28%), Positives = 55/113 (48%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+N+VL+R A + S+ AL LL + ++ V+++GG +++ A+
Sbjct: 70 RINIVLSRE--LKEAPKGAHYLSKSLDDALALLDSPELKSKVDMVWIVGGTAVYKAAMEK 127
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFR--PWYSSFP---KVENNIRYSFTTY 343
P + +T I E DTF P +D+ F+ Y P + E+ I+Y F Y
Sbjct: 128 PINHRLFVTRILHEFESDTFFPEIDYKDFKLLTEYPGVPADIQEEDGIQYKFEVY 182
>gi|11252924|pir||H81790 dihydrofolate reductase (EC 1.5.1.3) NMA2179
[imported] - Neisseria meningitidis (group A strain Z2491)
>gi|7380800|emb|CAB85391.1| (AL162758) dihydrofolate reductase
[Neisseria meningitidis Z2491]
Length = 162
Frame 2 hits (HSPs): _________________________________
__________________________________________________
Database sequence: | | | | | 162
0 50 100 150
Plus Strand HSPs:
Score = 121 (42.6 bits), Expect = 1.1e-06, P = 1.1e-06
Identities = 34/113 (30%), Positives = 59/113 (52%), Frame = +2
Query: 11 GRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALN 190
GR N+V++R + A AE S+ +AL L A + E+ ++GG QI+ +A+
Sbjct: 59 GRRNIVISRQADYCAAGAETAA---SLEAALALCAGA------EEAVIMGGAQIYGQAM- 108
Query: 191 VPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENN-IRYSFTTYVR 349
P + +TE+ S+E D F P +D T ++ + +V + Y+F Y+R
Sbjct: 109 -PLATDLRITEVDLSVEGDAFFPAIDRTHWKEAERTERRVSSKGTSYAFVHYLR 161
>gi|1480451|gb|AAC47230.1| (U41366) bifunctional dihydrofolate
reductase-thymidylate synthase [Cryptosporidium parvum]
Length = 521
Frame 2 hits (HSPs): ____________
__________________________________________________
Database sequence: | | | | | 521
0 150 300 450
Plus Strand HSPs:
Score = 130 (45.8 bits), Expect = 1.3e-06, P = 1.3e-06
Identities = 43/127 (33%), Positives = 61/127 (48%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+ VV++ S D A NVV+ ++ ++E L SIE +FV GG I+R+AL
Sbjct: 70 RIIVVISSSLPQDEADP-NVVVFRNLEDSIENLMNDD---SIENIFVCGGESIYRDALKD 125
Query: 194 PGCEAIHLTEIQ-SSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAAE 370
+ I+LT + IE DT+ P + T F P Y S NI Y F + +
Sbjct: 126 NFVDRIYLTRVALEDIEFDTYFPEIPET-FLPVYMSQTFCTKNISYDFMIFEKQEKKTL- 183
Query: 371 SAGQNIDP 394
QN DP
Sbjct: 184 ---QNCDP 188
>gi|2833339|sp|Q27828|DRTS_PARTE BIFUNCTIONAL DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE (DHFR-TS) [INCLUDES: DIHYDROFOLATE
REDUCTASE ; THYMIDYLATE SYNTHASE ] >gi|2133432|pir||S65570
dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC
2.1.1.45) - Paramecium tetraurelia >gi|434592|gb|AAC47025.1|
(U03885) dihydrofolate reductase-thymidylate synthase [Paramecium
tetraurelia]
Length = 462
Frame 2 hits (HSPs): _____________
Annotated Domains: __________________________________________________
__________________________________________________
Database sequence: | | | | | 462
0 150 300 450
__________________
Annotated Domains:
BLOCKS BL00075A: Dihydrofolate reductase protei 10..40
BLOCKS BL00075B: Dihydrofolate reductase protei 45..56
BLOCKS BL00075C: Dihydrofolate reductase protei 58..70
BLOCKS BL00075D: Dihydrofolate reductase protei 98..107
BLOCKS BL00091A: Thymidylate synthase proteins. 182..210
BLOCKS BL00091B: Thymidylate synthase proteins. 221..247
BLOCKS BL00091C: Thymidylate synthase proteins. 279..292
BLOCKS BL00091D: Thymidylate synthase proteins. 305..353
BLOCKS BL00091E: Thymidylate synthase proteins. 356..404
BLOCKS BL00091F: Thymidylate synthase proteins. 437..462
Entrez Domain: DIHYDROFOLATE REDUCTASE. 1..179
Entrez Domain: THYMIDYLATE SYNTHASE. 180..462
Entrez active site: BY SIMILARITY. 345
PFAM DiHfolate_red: Dihydrofolate reductase 8..140
PFAM thymidylat_synt: Thymidylate synthase 178..462
PRINTS DHFR1: Dihydrofolate reductase motif I - 18..28
PRINTS DHFR2: Dihydrofolate reductase motif II 32..40
PRINTS DHFR3: Dihydrofolate reductase motif III 45..56
PRINTS DHFR4: Dihydrofolate reductase motif IV 97..111
PRINTS THYMDSNTHASE1: Thymidylate synthase moti 221..242
PRINTS THYMDSNTHASE2: Thymidylate synthase moti 314..333
PRINTS THYMDSNTHASE3: Thymidylate synthase moti 340..355
PRINTS THYMDSNTHASE4: Thymidylate synthase moti 358..384
PRINTS THYMDSNTHASE5: Thymidylate synthase moti 396..413
PRODOM PD000692: DYR(35) DRTS(14) DYRA(2) 10..160
PRODOM PD001180: TYSY(21) DRTS(13) TYSA(3) 178..461
PROSITE DHFR: Dihydrofolate reductase signature. 18..40
PROSITE THYMIDYLATE_SYNTHASE: Thymidylate syntha 325..353
__________________
Plus Strand HSPs:
Score = 129 (45.4 bits), Expect = 1.4e-06, P = 1.4e-06
Identities = 33/115 (28%), Positives = 59/115 (51%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R+NVV++++ + ++ V + + AL+ Y+ S +K+++IGG +IF E L
Sbjct: 63 RVNVVISKN----MKSSNEVQVFPRIEDALQF-----YNTSHQKLYLIGGKRIFEEGLAT 113
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRS 358
C +HLT I +CD ++ F+ F+ +S K EN I Y + + S
Sbjct: 114 DKCSDVHLTRIGVETKCDVYLNKNIFSTFQVNKTSQTKSENGINYDYQHLINKNS 168
>gi|1073998|pir||S52336 dihydrofolate reductase (EC 1.5.1.3) - Haemophilus
influenzae (clinical isolate R1042) >gi|665643|emb|CAA58993.1|
(X84207) dihydrofolate reductase [Haemophilus influenzae]
Length = 160
Frame 2 hits (HSPs): _________________________________
Annotated Domains: _________________________________
__________________________________________________
Database sequence: | | | | | 160
0 50 100 150
__________________
Annotated Domains:
Entrez domain: type I dihydrofolate reductase h 2..105
PROSITE DHFR: Dihydrofolate reductase signature. 14..36
__________________
Plus Strand HSPs:
Score = 118 (41.5 bits), Expect = 2.3e-06, P = 2.3e-06
Identities = 31/114 (27%), Positives = 61/114 (53%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
R N+VL+R F E VV S+ SA+ + +++ +IGGG++F++ L
Sbjct: 58 RTNIVLSRQ-PFK---HEGVVWKNSLESAVNFVR------DFDEIMLIGGGELFKQYL-- 105
Query: 194 PGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVR 355
P + ++LT+IQ+ ++ DTF P +++ ++ + + K + RY + + R
Sbjct: 106 PKADKLYLTQIQTELDGDTFFPQLNWEEWKIEFDEYHKADEQNRYDCRSLILTR 159
>gi|2624564|pdb|1AI9|A Chain A, Candida Albicans Dihydrofolate Reductase
>gi|2624565|pdb|1AI9|B Chain B, Candida Albicans Dihydrofolate
Reductase >gi|2780860|pdb|1AOE|B Chain B, Candida Albicans
Dihydrofolate Reductase Complexed With
Dihydro-Nicotinamide-Adenine-Dinucleotide Phosphate (Nadph) And
1,3-Diamino-7-(1-Ethyepropye)-7h-Pyrralo- [3,2-F]quinazoline
(Gw345) >gi|2780859|pdb|1AOE|A Chain A, Candida Albicans
Dihydrofolate Reductase Complexed With
Dihydro-Nicotinamide-Adenine-Dinucleotide Phosphate (Nadph) And
1,3-Diamino-7-(1-Ethyepropye)-7h-Pyrralo- [3,2-F]quinazoline
(Gw345) >gi|2959580|gb|AAC05610.1| (U84588) dihydrofolate reductase
[Candida albicans]
Length = 192
Frame 2 hits (HSPs): _____________________
__________________________________________________
Database sequence: | | | | | 192
0 50 100 150
Plus Strand HSPs:
Score = 118 (41.5 bits), Expect = 2.3e-06, P = 2.3e-06
Identities = 30/81 (37%), Positives = 51/81 (62%), Frame = +2
Query: 14 RLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNV 193
RLN++L+RS +I +N++ S+ S+L L++ +E+VF+IGG +I+ E +N
Sbjct: 72 RLNIILSRSYENEIID-DNIIHASSIESSLNLVS------DVERVFIIGGAEIYNELINN 124
Query: 194 PGCEAIHLTEIQ----SSIECDTFM 256
+ +TEI+ SIE DTF+
Sbjct: 125 SLVSHLLITEIEHPSPESIEMDTFL 149
WARNING: HSPs involving 105 database sequences were not reported due to the
limiting value of parameter B = 50.
Parameters:
filter=none
matrix=BLOSUM62
V=50
B=50
E=10
gi
H=1
sort_by_pvalue
echofilter
ctxfactor=5.94
Query ----- As Used ----- ----- Computed ----
Frame MatID Matrix name Lambda K H Lambda K H
Std. 0 BLOSUM62 0.318 0.135 0.401
+3 0 BLOSUM62 0.318 0.135 0.401 0.349 0.155 0.501
Q=9,R=2 0.244 0.0300 0.180 n/a n/a n/a
+2 0 BLOSUM62 0.318 0.135 0.401 0.326 0.139 0.412
Q=9,R=2 0.244 0.0300 0.180 n/a n/a n/a
+1 0 BLOSUM62 0.318 0.135 0.401 0.379 0.168 0.761
Q=9,R=2 0.244 0.0300 0.180 n/a n/a n/a
-1 0 BLOSUM62 0.318 0.135 0.401 0.346 0.149 0.514
Q=9,R=2 0.244 0.0300 0.180 n/a n/a n/a
-2 0 BLOSUM62 0.318 0.135 0.401 0.337 0.144 0.446
Q=9,R=2 0.244 0.0300 0.180 n/a n/a n/a
-3 0 BLOSUM62 0.318 0.135 0.401 0.360 0.157 0.584
Q=9,R=2 0.244 0.0300 0.180 n/a n/a n/a
Query
Frame MatID Length Eff.Length E S W T X E2 S2
+3 0 159 155 10. 74 3 12 22 0.096 34
30 0.12 36
+2 0 160 158 10. 74 3 12 22 0.098 34
30 0.097 37
+1 0 160 156 10. 74 3 12 22 0.097 34
30 0.12 36
-1 0 160 157 10. 74 3 12 22 0.098 34
30 0.12 36
-2 0 160 158 10. 74 3 12 22 0.098 34
30 0.097 37
-3 0 159 155 10. 74 3 12 22 0.096 34
30 0.12 36
Statistics:
Database: /usr/local/dot5/sl_home/beauty/seqdb/blast/nr
Title: nr
Release date: unknown
Posted date: 4:06 PM CST Feb 28, 2001
Format: BLAST
# of letters in database: 197,782,623
# of sequences in database: 625,274
# of database sequences satisfying E: 155
No. of states in DFA: 594 (59 KB)
Total size of DFA: 191 KB (192 KB)
Time to generate neighborhood: 0.01u 0.00s 0.01t Elapsed: 00:00:00
No. of threads or processors used: 6
Search cpu time: 147.22u 1.39s 148.61t Elapsed: 00:00:25
Total cpu time: 147.28u 1.42s 148.70t Elapsed: 00:00:25
Start: Mon Oct 1 20:56:57 2001 End: Mon Oct 1 20:57:22 2001
WARNINGS ISSUED: 2
Annotated Domains Database: March 14, 2000
Release Date: March 14, 2000