NCBI Conserved Domain Search

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Conserved domains on [gi\|6980533\|pdb\|2STA\|E]
Chain E, Anionic Salmon Trypsin In Complex With Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I)

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List of domain hits		?

References:

Marchler-Bauer A et al. (2007), "CDD: a conserved domain database for interactive domain family analysis.", Nucleic Acids Res.35(D)237-240.

Marchler-Bauer A et al. (2005), "CDD: a Conserved Domain Database for protein classification.", Nucleic Acids Res.33(D)192-196.

Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.

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of the residues that compose this conserved feature have been mapped to the query sequence.

Click on the triangle to view details about the feature, including a multiple sequence alignment of your query sequence and the protein sequences used to curate the domain model, where hash marks (#) above the aligned sequences show the location of the conserved feature residues.

The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions. Click on the triangle for interactive 3D structure viewing options.

This image shows a graphical summary of conserved domains identified on the query sequence. The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits (labeled illustration) or all hits (labeled illustration).
Domains are color coded according to superfamilies to which they have been assigned. Hits with scores that pass a domain-specific threshold (specific hits) are drawn in bright colors. Others (non-specific hits) and superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features), they are mapped to the query sequence and indicated through sets of triangles with the same color and shade of the domain or superfamily that provides the annotation.
Mouse over the colored bars or triangles to see descriptions of the domains and features. click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.

The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores. Click on the PssmId to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.

To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page, or click on the triangles, if present, that represent functional sites (conserved features) mapped to the query sequence.

Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence. (labeled illustration)
Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance. (labeled illustration)
Four types of hits can be shown, as available, for each region on the query sequence:

specific hits meet or exceed a domain-specific e-value threshold (illustrated example) and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains

The CD-Search help document provides more detail about the tool and its features.

Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool (CDART).

29152

cd00190

Tryp_SPc

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.

Trypsin-like serine protease; Many of these are synthesized as inactive precursor...

true

false

true

232

9e-77

281.44

100.00

                    10        20        30        40        50        60        70        80
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E    1 IVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 74
cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                    90       100       110       120       130       140       150       160
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E   75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 151
cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160

                   170       180       190       200       210       220       230
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2STA_E  152 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 218
cd00190 161 yGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232

cl00149

119569

Tryp_SPc

Trypsin-like serine protease; Many of these are synthesized as inactive precursor...

109157

pfam00089

Trypsin

false

216

4e-71

262.37

100.00

                      10        20        30        40        50        60        70        80
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E      1 IVGGYECKPYSQPHQVSL-NSGYHFCGGSLVNENWVVSAAHCYKSR--VEVRLGEHNIKVTEGSEQFISSSRVIRHPNYS 77
pfam00089   1 IVGGDEAQPGSFPWQVSLqVSSGHFCGGSLISENWVLTAAHCVSNAssVRVVLGAHNIVLREGGEQKFDVKKIIVHPNYN 80

                      90       100       110       120       130       140       150       160
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E     78 SynIDNDIMLIKLSKPATLNTYVQPVALPTSCA--PAGTMCTVSGWGNTmSSTADSNKLQCLNIPILSYSDCNNSYPGMI 155
pfam00089  81 P--DTNDIALLKLKSPVTLGDTVRPICLPTASSdlPVGTTCTVSGWGNT-KTLGTPDTLQEVTVPVVSRETCRSAYGGTV 157

                     170       180       190       200       210       220
              ....*....|....*....|....*....|....*....|....*....|....*....|.
2STA_E    156 TNAMFCAGYleGGKDSCQGDSGGPVVC-NGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWL 215
pfam00089 158 TDNMICAGA--GGKDACQGDSGGPLVCsDGELVGIVSWGYGCASGNYPGVYTPVSSYLDWI 216

cl00149

119569

Tryp_SPc

Trypsin-like serine protease; Many of these are synthesized as inactive precursor...

-1

47370

smart00020

Tryp_SPc

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.

Trypsin-like serine protease; Many of these are synthesised as inactive precursor...

false

231

6e-71

262.20

99.57

                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E       1 IVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGSeQFISSSRVIRHP 74
smart00020   2 IVGGSEANIGSFPWQVSLqyRGGRHFCGGSLISPRWVLTAAHCVygsaPSSIRVRLGSHDLSSGEET-QTVKVSKVIVHP 80

                       90       100       110       120       130       140       150       160
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E      75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTM-SSTADSNKLQCLNIPILSYSDCNNSY 151
smart00020  81 NYNPSTYDNDIALLKLSEPVTLSDTVRPICLPSSgyNVPAGTTCTVSGWGRTSeSSGSLPDTLQEVNVPIVSNATCRRAY 160

                      170       180       190       200       210       220       230
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2STA_E     152 PG--MITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWG-YGCAEPGNPGVYAKVCIFNDWL 215
smart00020 161 SGgpAITDNMLCAGGLEGGKDACQGDSGGPLVCNdpgrWVLVGIVSWGsYGCARPNKPGVYTRVSSYLDWI 231

cl00149

119569

Tryp_SPc

Trypsin-like serine protease; Many of these are synthesized as inactive precursor...

-1

33391

COG3591

V8-like Glu-specific endopeptidase [Amino acid transport and metabolism]

false

251

0.009

35.28

61.35

                    10        20        30        40        50        60        70        80
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E    9 PYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKS--RVEVRLGEHNIKVTEGSEQFIS-SSRVIRHPNYSSYNIDNDI 85
COG3591  50 PYSAVVQFEAATGRLCTAATLIGPNTVLTAGHCIYSpdYGEDDIAAAPPGVNSDGGPFYGiTKIEIRVYPGELYKEDGAS 129

                    90       100       110       120       130       140       150
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2STA_E   86 M---LIKLSKPATLNTYVQPVALPT-SCAPAGTMCTVSGW----GNTMSSTADSNKLQCLNIPILSYSdcNNSYPG 153
COG3591 130 YdvgEAALESGINIGDVVNYLKRNTaSEAKANDRITVIGYpgdkPNIGTMWESTGKVNSIKGNKLFYD--ADTLPG 203

cl00149

119569

Tryp_SPc

Trypsin-like serine protease; Many of these are synthesized as inactive precursor...

-1

35199

COG5640

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover,..

false

true

false

413

3e-20

93.17

60.05

                    10        20        30        40        50        60        70        80
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E    1 IVGGYECKPYSQPHQVSL------NSGYHFCGGSLVNENWVVSAAHCYKSRVEVRlGEHNIKVTEGSE----QFISSSRV 70
COG5640  33 IIGGSNANAGEYPSLVALvdrisdYVSGTFCGGSKLGGRYVLTAAHCADASSPIS-SDVNRVVVDLNDssqaERGHVRTI 111

                    90       100       110       120       130       140       150       160
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E   71 IRHPNYSSYNIDNDIMLIKLSKPATL----NTYVQPVALPTSCAPAGTMCTVSGWGNTM-----SSTADSNKLQCLNIPI 141
COG5640 112 YVHEFYSPGNLGNDIAVLELARAASLprvkITSFDASDTFLNSVTTVSPMTNGTFGVTTpsdvpRSSPKGTILHEVAVLF 191

                   170       180       190       200       210       220       230       240
            ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2STA_E  142 LS------YSDCNNSYPGMITNAMFCAGYLegGKDSCQGDSGGPVVCNGE----LQGVVSWGYG-CAEPGNPGVYAKVCI 210
COG5640 192 VPlstcaqYKGCANASDGATGLTGFCAGRP--PKDACQGDSGGPIFHKGEegrvQRGVVSWGDGgCGGTLIPGVYTNVSN 269

                   250
            ....*....|.
2STA_E  211 FNDWLTSTMAS 221
COG5640 270 YQDWIAAMTNG 280

-1

active site	0	3	3	true	29152	cd00190	Tryp_SPc
cleavage site	1	1	1	true	29152	cd00190	Tryp_SPc
substrate binding sites	2	3	3	true	29152	cd00190	Tryp_SPc