109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
6e-07 |
52.23 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 771 GVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNKMVDQLN 836
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
1e-06 |
51.46 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 311 GVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 376
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
1e-06 |
51.46 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 403 GVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 468
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
1e-06 |
51.46 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 495 GVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 560
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
1e-06 |
51.07 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 587 GVAGTWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 652
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
1e-06 |
51.07 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 679 GVAGTWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 744
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
2e-06 |
50.69 |
94.29 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113477642 219 GLSGVWKELTDNVNGMADHLTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNQMVDQLN 284
pfam00672 4 VLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
2e-06 |
50.40 |
100.00 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 671 LGGQAKVEGVAGTWKELTDNVNGMAANLTLQ--VRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSS 748
COG2770 1 LHSTAPIFGLLVLALVLILAVLLLAAARRVTrpLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
...
gi 113477642 749 EVT 751
COG2770 81 ALE 83
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
2e-06 |
50.02 |
98.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 579 LGGQAKVEGVAGTWKELTDNVNGMAANLTLQ--VRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSS 656
COG2770 1 LHSTAPIFGLLVLALVLILAVLLLAAARRVTrpLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
..
gi 113477642 657 EV 658
COG2770 81 AL 82
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
3e-06 |
50.02 |
98.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 303 LGGQAKVEGVAGIWKELTDNVNGMAANLTLQ--VRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSS 380
COG2770 1 LHSTAPIFGLLVLALVLILAVLLLAAARRVTrpLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
..
gi 113477642 381 EV 382
COG2770 81 AL 82
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
3e-06 |
50.02 |
98.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 395 LGGQAKVEGVAGIWKELTDNVNGMAANLTLQ--VRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSS 472
COG2770 1 LHSTAPIFGLLVLALVLILAVLLLAAARRVTrpLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
..
gi 113477642 473 EV 474
COG2770 81 AL 82
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
3e-06 |
50.02 |
98.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 487 LGGQAKVEGVAGIWKELTDNVNGMAANLTLQ--VRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSS 564
COG2770 1 LHSTAPIFGLLVLALVLILAVLLLAAARRVTrpLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
..
gi 113477642 565 EV 566
COG2770 81 AL 82
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
3e-06 |
50.02 |
98.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 763 LGGQAKVEGVAGIWKELTDNVNGMAANLTLQ--VRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNKMVDQLNGFSS 840
COG2770 1 LHSTAPIFGLLVLALVLILAVLLLAAARRVTrpLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
..
gi 113477642 841 EV 842
COG2770 81 AL 82
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
3e-05 |
46.55 |
98.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 211 LGVQAKVEGLSGVWKELTDNV--NGMADHLTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNQMVDQLNGFSS 288
COG2770 1 LHSTAPIFGLLVLALVLILAVllLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
|
..
gi 113477642 289 EV 290
COG2770 81 AL 82
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
5e-05 |
45.55 |
88.68 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 238 LTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNQMVDQLN 284
smart00304 3 LLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
7e-05 |
45.32 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 238 LTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNQMVDQLN 284
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
1e-04 |
44.77 |
90.57 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 113477642 789 NLTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNKMVDQLN 836
smart00304 2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
2e-04 |
44.00 |
90.57 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 113477642 329 NLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 376
smart00304 2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
2e-04 |
44.00 |
90.57 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 113477642 421 NLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 468
smart00304 2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
2e-04 |
44.00 |
90.57 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 113477642 513 NLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 560
smart00304 2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
2e-04 |
44.00 |
90.57 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 113477642 605 NLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 652
smart00304 2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47632 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases)... |
false |
false |
false |
53 |
2e-04 |
44.00 |
90.57 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 113477642 697 NLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 744
smart00304 2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
2e-04 |
43.78 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 790 LTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNKMVDQLN 836
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
2e-04 |
43.39 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 330 LTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 376
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
2e-04 |
43.39 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 422 LTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 468
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
2e-04 |
43.39 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 514 LTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 560
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
2e-04 |
43.39 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 606 LTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 652
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
false |
false |
false |
48 |
2e-04 |
43.39 |
97.92 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113477642 698 LTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 744
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
|
|
cl01054 |
120347 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
47612 |
smart00283 |
MA |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis. |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). Thought to... |
true |
true |
false |
262 |
2e-28 |
123.87 |
68.70 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 977 IGKLGVSSAEIGNVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKQTASATEDISQKIEAIQGDTRG 1056
smart00283 83 VEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 1057 AVEAIGQITTIISQINDIQG-------TIASAVEEQTATTNEIARNVNQAAERSSGIALNITSVAKTAQSTSNGAAKTQK 1129
smart00283 163 AVAAMEESSSEVEEGVELVEetgealeEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISA 242
|
170 180
....*....|....*....|
gi 113477642 1130 SATELSKTAGDLHELVNQFK 1149
smart00283 243 AAEELSGLAEELDELVERFK 262
|
|
|
|
|
|
|
-1 |
109084 |
pfam00015 |
MCPsignal |
Methyl-accepting chemotaxis protein (MCP) signaling domain |
Methyl-accepting chemotaxis protein (MCP) signaling domain |
false |
true |
false |
241 |
4e-27 |
119.45 |
74.69 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 977 IGKLGVSSAEIGNVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKQTASATEDISQKIEAIQGDTRG 1056
pfam00015 60 MEELATSSKNISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEQLIEEIQKESND 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 1057 AVEAIGQI-------TTIISQINDIQGTIASAVEEQTATTNEIARNVNQAAERSSGIALNITSVAKTAQSTSNGAAKTQK 1129
pfam00015 140 AVESMQQTrtqvevgSTIVEKTGEALKEIVEAIGEIADEVQEIAAASEEQSAGIEQINQAVERIDQVTQQNAALVEESSA 219
|
170 180
....*....|....*....|
gi 113477642 1130 SATELSKTAGDLHELVNQFK 1149
pfam00015 220 ASESLSEQAEELTALVAQFK 239
|
|
|
|
|
|
|
-1 |
31182 |
COG0840 |
Tar |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms] |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction... |
false |
true |
false |
408 |
9e-25 |
111.23 |
99.26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 710 TAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSSEVTRVAKEVGTEGTLGGQAKVEGVAGIWKELTDNVNGMAAN 789
COG0840 4 EAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 790 LTLQVRNIAEVATAVAQGDLTQKITVDAQGEILELKTTLNKMVDQLNGFSSEVSRVAKEVGTegtlggqaKVEGVAGTWK 869
COG0840 84 ILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSG--------ASEEIAASAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 870 ELTDNVNGMAANLTEqvkkiakaaiaVAKSSEEMMAESQTMSQASQETSTQAESVSSNAAQVSANVQSVATGVEEMTTSI 949
COG0840 156 ELSARADQQAESLEE-----------VASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 950 QEIaknatnaaqvattavktaettnetIGKLGVSSAEIGNVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEV 1029
COG0840 225 AEV------------------------VKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 1030 KELAKQTASATEDISQKIEAIQGDTRGAVEAIGQITTIIS-------QINDIQGTIASAVEEQTATTNEIARNVNQAAER 1102
COG0840 281 RKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSegvklveETGSSLGEIAAAIEEVSQLISEIAAATEEQTAV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 113477642 1103 SSGIALNITSVAKTAQSTSNGAAKTQKSATELSKTAGDLHELVNQFKF 1150
COG0840 361 LEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
|
|
|
|
|
|
|
-1 |
104157 |
PRK09793 |
PRK09793 |
methyl-accepting protein IV; Provisional |
methyl-accepting protein IV; Provisional |
false |
true |
false |
533 |
6e-19 |
92.06 |
28.52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 980 LGVSSAEIGNVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKQTASATEDISQKIE-----AIQGD- 1053
PRK09793 350 IATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEesvnrVQQGSk 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113477642 1054 -TRGAVEAIGQITTIISQINDIQGTIASAVEEQTATTNEIARNVNQAAERSSGIALNITSVAKTAQSTSNGA 1124
PRK09793 430 lVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQA 501
|
|
|
|
|
|
|
-1 |
31182 |
COG0840 |
Tar |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms] |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction... |
true |
true |
false |
408 |
7e-06 |
48.44 |
97.30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 434 TAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSSEVSRVAKEVGTEGILGGQAKVEGVAGIWKELTDNVNGMAAN 513
COG0840 4 EAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 514 LTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSSEVSRVAKEV--GTEGILGGQAKVEGVAGT 591
COG0840 84 ILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALsgASEEIAASATELSARADQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 592 WKELTDNVNGMAANLTLQVRNIAEVATAVAQgdltqkITVDVQGEILELKTTLNKMVDQLNGFSSEVSRVAKEVGTEGil 671
COG0840 164 QAESLEEVASAIEELSETVKEVAFNAKEAAA------LASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKKLSESS-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 672 ggqAKVEGVAGTWKELTDNVNGMAANLTL-------QVRNIAEVATAVAQ-GDLTQKITVDVQGEILELKTTLNKMVDQL 743
COG0840 236 ---QEIEEITSVINSIAEQTNLLALNAAIeaarageAGRGFAVVADEVRKlAERSADSAKEIGLLIEEIQNEAADAVEHM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 744 NGFSSEVTRVAKEVGTEGtlggqAKVEGVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDAQGEILE 823
COG0840 313 EESASEVSEGVKLVEETG-----SSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAA 387
|
410
....*....|...
gi 113477642 824 LKTTLNKMVDQLN 836
COG0840 388 ASEELKELAEKLL 400
|
|
|
|
|
|
|
-1 |
31182 |
COG0840 |
Tar |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms] |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction... |
true |
true |
false |
408 |
8e-06 |
48.44 |
94.12 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 171 KPLNEEFYRIGSIVNQIVDKLNSFSSEVTRVAQEVGTEGKLGVQAKVEGLSGVWKELTDNVNGMADHLTLQVRNIAEVAT 250
COG0840 17 GEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 251 AVAQGDLTQKITVDAQGEILELKTTLNQMVDQLNGFSSEVSRVAKEVGT------EGILGGQAKVEGVAGIWKELTDNVN 324
COG0840 97 RIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGaseeiaASATELSARADQQAESLEEVASAIE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 325 GMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLNGFSSEVSRVAKEVGTegilggqaKVEGV 404
COG0840 177 ELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKKLSESSQEIEEITS--------VINSI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 405 AGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQ-GDLTQKITVDVQGEILELKTTLNKMVDQLNGFSSEVSRVAKEVGT 483
COG0840 249 AEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKlAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEE 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113477642 484 EGilggqAKVEGVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGEILELKTTLNKMVDQLN 560
COG0840 329 TG-----SSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLL 400
|
|
|
|
|
|
|
-1 |
31182 |
COG0840 |
Tar |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms] |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction... |
false |
true |
false |
408 |
0.005 |
39.20 |
96.57 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 58 LLVAMKAARDGDFTVRIPENNGLGEVAIVFNQMIAINQNFAEEIGRISREVWQEGELTTRKSFTEVkgswksSIDSLNEL 137
COG0840 7 LNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIV------VLVLAILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 138 INNWTKPSREVSLVLEAVANGDLSKKINFQFegkplNEEFYRIGSIVNQIVDKLNSFSSEVTRVAQEV--GTEGKLGVQA 215
COG0840 81 LRAILEPISDLLEVVERIAAGDLTKRIDESS-----NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALsgASEEIAASAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 216 KVEGLSGVWKELTDNVNGMADHLTLQVRNIAEVATAVAQgdltqkITVDAQGEILELKTTLNQMVDQLNGFSSEVSRVAK 295
COG0840 156 ELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAA------LASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 296 EVGTEG--ILGGQAKVEGVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQ-GDLTQKITVDVQGEILELKTTLNKMV 372
COG0840 230 KLSESSqeIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKlAERSADSAKEIGLLIEEIQNEAADAV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113477642 373 DQLNGFSSEVSRVAKEVGTEGilggqAKVEGVAGIWKELTDNVNGMAANLTLQVRNIAEVATAVAQGDLTQKITVDVQGE 452
COG0840 310 EHMEESASEVSEGVKLVEETG-----SSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEE 384
|
410
....*....|....*.
gi 113477642 453 ILELKTTLNKMVDQLN 468
COG0840 385 LAAASEELKELAEKLL 400
|
|
|
|
|
|
|
-1 |