| 109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
2e-09 |
59.93 |
100.00 |
1,192,0,70 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 193 IVGFMVFGVFAAIALGWFLTRLIVGPVRELQATATKLAAGDVEVDIKANTNDELGKLAQSIAALAATIKD 262
pfam00672 1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
|
|
cl01054 |
141075 |
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 |
| 128599 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain |
false |
false |
false |
53 |
6e-05 |
45.32 |
100.00 |
1,212,0,53 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 94968699 213 RLIVGPVRELQATATKLAAGDVEVDIKANTNDELGKLAQSIAALAATIKDRAQ 265
smart00304 1 RRILRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
|
|
cl01054 |
141075 |
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 |
1e-04 |
43.78 |
100.00 |
1,214,0,48 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 94968699 215 IVGPVRELQATATKLAAGDVEVDIKANTNDELGKLAQSIAALAATIKD 262
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
|
|
cl01054 |
141075 |
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 |
0.003 |
39.23 |
85.54 |
2,187,1,19,206,21,51 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94968699 188 SATQQIVGFMVFGVFAAIA-LGWFLTRLIVGPVRELQATATKLAAGDVEVDIKANTNDELGKLAQSIAALA 257
COG2770 2 HSTAPIFGLLVLALVLILAvLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMR 72
|
|
cl01054 |
141075 |
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 |
| 128579 |
smart00283 |
MA |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). |
true |
true |
false |
262 |
3e-45 |
179.02 |
98.85 |
3,626,3,176,802,180,4,806,190,72 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 627 EAATMLNNVSQQMTASADETATQANVVSAASEQVSRNVQTVASGADQMGASIKEIAKNTAEATRVANSAVQTAEATNQNI 706
smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 707 GKLGQSSAEIGQVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKETAKATEDIGRKIEAIQTDTTGA 786
smart00283 84 EELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 787 VSAIAEIGAVINQISD-IQTT------IASAVEEQSVTSNEISRNLAEAAKGNVDITRNVTGVAEAARVTTTGAAETQKS 859
smart00283 164 VAAMEESSSEVEEGVElVEETgealeeIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAA 243
|
250
....*....|....*....
gi 94968699 860 AKSLERMAVELKKLVSRFK 878
smart00283 244 AEELSGLAEELKELVEQFK 262
|
|
|
|
|
|
|
-1 |
| 109084 |
pfam00015 |
MCPsignal |
Methyl-accepting chemotaxis protein (MCP) signaling domain |
Methyl-accepting chemotaxis protein (MCP) signaling domain |
false |
true |
false |
241 |
3e-34 |
142.56 |
99.17 |
3,657,0,51,708,62,96,804,165,74 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 658 EQVSRNVQTVASGADQMGASIKEIAKNTAEATRVANSAVQTAEATNQNIGK-----------LGQSSAEIGQVIKVITSI 726
pfam00015 1 EEQASAIEQVAASMEQLTATVRDIASNAAQASDLAKQASEEALEEMSQIGQevdnavqvmeeLATSSKNISDIISVIDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 727 AQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKETAKATEDIGRKIEAIQTDTTGAVSAIAEIGAVINQISDIQ-- 804
pfam00015 81 AFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEQLIEEIQKESNDAVESMQQTRTQVEVGSTIVek 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94968699 805 -----TTIASAVEEQSVTSNEISRNLAEAAKGNVDITRNVTGVAEAARVTTTGAAETQKSAKSLERMAVELKKLVSRFK 878
pfam00015 161 tgealKEIVEAIGEIADEVQEIAAASEEQSAGIEQINQAVERIDQVTQQNAALVEESSAASESLSEQAEELTALVAQFK 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 |
1e-30 |
130.10 |
78.92 |
4,559,85,29,596,114,102,698,220,98,796,325,82 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 560 RQAQKLSDALKELAQGNLNALMVTDASDAdtdearktYEVISDAFAKSAAAFRGAMMDIGRTTEALLEAATMLNNVSQQM 639
COG0840 86 EPISDLLEVVERIAAGDLTKRIDESSNDE--------FGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATEL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 640 TASADETATQANVVSAASEQVSRNVQTVASGADQMGASIKEIAKNTAEATRVANSAVQT----AEATNQNIGKLGQSSAE 715
COG0840 158 SARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQmqeiAEELAEVVKKLSESSQE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 716 IGQVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKETAKATEDIGRKIEAIQTDTTGAVSAIAEIGA 795
COG0840 238 IEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESAS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 796 V-------INQISDIQTTIASAVEEQSVTSNEISRNLAEAAKGNVDITRNVTGVAEAARVTTTGAAETQKSAKSLERMAV 868
COG0840 318 EvsegvklVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAE 397
|
330
....*....|
gi 94968699 869 ELKKLVSRFK 878
COG0840 398 KLLELVAKFK 407
|
|
|
|
|
|
|
-1 |
| 137524 |
PRK09793 |
PRK09793 |
methyl-accepting protein IV; Provisional |
methyl-accepting protein IV; Provisional |
false |
true |
false |
533 |
6e-23 |
104.77 |
51.97 |
7,622,256,89,711,352,67,778,423,5,783,431,31,821,462,9,840,471,38,878,510,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 623 EALLEAATMLNNVSQQMTASADETATQANVVSAASEQVSRNVQTVASGADQMGASIKEIAKNTAEATRVANSAVQTAEAT 702
PRK09793 257 QALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 703 NQNIGKLGQ-------SSAEIGQVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKETAKATEDIGRK 775
PRK09793 337 GVQVSTMTHtmqeiatSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 776 IEA----IQTDT---TGAVSAIAEIGAVINQISDIQTTIASAVEEQsvtsneiSRNLAEAAKgnvditrnvtGVAEAARV 848
PRK09793 417 IEEsvnrVQQGSklvNNAAATMTDIVSSVTRVNDIMGEIASASEEQ-------RRGIEQVAQ----------AVSQMDQV 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 94968699 849 TTTGAAETQKSAKSLERMAVELKKLVSRFK-YDGEQNSRSLAVSSRADRMPATS 901
PRK09793 480 TQQNASLVEEAAVATEQLANQADHLSSRVAvFTLEEHEVARHESAQLQIAPVVS 533
|
|
|
|
|
|
|
-1 |
| 117025 |
pfam08448 |
PAS_4 |
PAS fold |
PAS fold |
true |
true |
false |
110 |
4e-07 |
52.42 |
100.00 |
3,438,0,72,510,74,30,545,104,6 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 439 FDAIPKPIQFIDSQFKVQYMNKAGLELMGKSAESAIGSRCSYNTSACGTEKCTCAQAMKIDGLTRIETQARI--QGKQYD 516
pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELllNGEERH 80
|
90 100 110
....*....|....*....|....*....|....*
gi 94968699 517 FTCCAVPLKDGNGRTIGAFELMDDeslikTTMRKA 551
pfam08448 81 YELRLTPLRDPDGEVIGVLVISRD-----ITERRR 110
|
|
|
|
|
|
|
-1 |
| 137977 |
PRK10549 |
PRK10549 |
signal transduction histidine-protein kinase BaeS; Provisional |
signal transduction histidine-protein kinase BaeS; Provisional |
false |
true |
false |
467 |
1e-06 |
50.88 |
14.99 |
3,192,169,6,200,175,7,208,182,57 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94968699 193 IVGFMVfgVFAAIALgWFLTRLIVGPVRELQATATKLAAGDVEVDIKANTNDELGKLAQSIAALAATIKDRAQ 265
PRK10549 170 IVALST--LLAALAT-FLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLEKNQQ 239
|
|
|
|
|
|
|
-1 |
| 132001 |
TIGR02956 |
TMAO_torS |
TMAO reductase sytem sensor TorS |
TMAO reductase sytem sensor TorS |
false |
true |
false |
968 |
3e-04 |
42.46 |
11.88 |
3,194,331,25,219,358,7,226,367,79 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 195 GFMVFGVFAAIALGWFLTRLIVGPV--RELQATA--TKLAAGDVEVDIKANTNDELGKLAQSIAALAATIKDRAQAAQHI 270
TIGR02956 332 GLLITGMLGLVILVFIMWRVVYRSVilRLNQHTQalLRLALGDLDISLDARGDDELAHMGRAIEAFRDTAAHNLKLQADE 411
|
90 100 110
....*....|....*....|....*....|....*
gi 94968699 271 AQGDLQLQIKPASDKDVLAKSLQSLVDTLNGLMQE 305
TIGR02956 412 RQVAQELQEHKESLEQLVAQRTQELAETNERLNAE 446
|
|
|
|
|
|
|
-1 |
| 31700 |
COG1511 |
COG1511 |
Predicted membrane protein [Function unknown] |
Predicted membrane protein [Function unknown] |
false |
true |
false |
780 |
8e-04 |
41.23 |
30.51 |
1,624,203,238 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 625 LLEAATMLNNVSQQMTASADETATQANVVSAASEQVSRNVQTVASGADQMGASIKEIAKNTAEATRVANSAVQTAEATNQ 704
COG1511 204 LSDLLNTLNNSSATFSDGLNALTSGLTTLTDGLNQLDSGLGTLAAGIGELKQGAEQLNEGIGEFSSGLSELNSGVQDLAA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968699 705 NIGKLGQSSAEIGQVIKVITSIAQQTNLLALNATIEAARAGEAGKGFAVVANEVKELAKETAKATEDIGRKIEAIQTDTT 784
COG1511 284 GVPQLNQGISALAAGLSLPDSLGDQFSSLQEALTQIAQGLKQKTSSSLEAAQGSLSSLQSMLALSKSLDLTAEGATVDAL 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94968699 785 GAVSAIAEIGAVINQISDIQTTIASAVEEQSVTSNEISRNLAEAAKGNVDITRNVTGVAEAARVTTTGAAETQKSAKS 862
COG1511 364 GAPDGVQWLDESQKTLATLSELLSTGIDGVSEGLDALEQASAQLAKSLAKLKTAVAQIAASIAQLLPGASEVLKTLKS 441
|
|
|
|
|
|
|
-1 |
| 34605 |
COG5000 |
NtrY |
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms] |
Signal transduction histidine kinase involved in nitrogen fixation and metabolism... |
false |
true |
false |
712 |
0.001 |
40.71 |
9.41 |
2,176,268,22,200,290,45 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94968699 177 KREKENSALAASATQQIVGFMVfgVFAAIALGWFLTRLIVGPVRELQATATKLAAGDVEVDIKANTNDE 245
COG5000 269 EAGRDGLQIAFALLYLSTALLV--LLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDE 335
|
|
|
|
|
|
|
-1 |
|