| 109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
true |
false |
false |
70 |
5e-09 |
58.39 |
100.00 |
2,193,0,39,233,39,31 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94968801 194 SAFVALIAVLAGLFIARRTAKSIVDPIDALNKMAGEIGEsGDLEHTVEIERDDEVGDLAKTFNSMVTYLTE 264
pfam00672 1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIAS-GDLDDRVPVSGPDEIGELARAFNQMADRLRE 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 |
| 34875 |
COG5278 |
COG5278 |
Predicted periplasmic ligand-binding sensor domain [Signal transduction mechanisms] |
Predicted periplasmic ligand-binding sensor domain [Signal transduction mechanisms] |
true |
false |
false |
207 |
1e-06 |
49.92 |
97.58 |
4,0,0,141,148,141,6,156,147,10,166,159,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 1 MTGRNTIRKRLMISFGAIIALVVVLFIASFLSVMRERSAKAAAQTAIDMQSAIEKLRMQMMENRVALAGYVLTGGPAPLA 80
COG5278 1 MTKRMPIRKKIILSFVIGVLLLLLASGASYWSIQKSNQSTREVIETQQVLAAALDLLSAVSDAESGQRGYLLTGNDEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 81 KFNSGVEEFDHLLSDARSKAYSEGQRTALKELEDRNRNWKEKFALPLIQVGKSVEMGNATAtdvqlkyITVSNEwaGQPQ 160
COG5278 81 PYEEATEELDQKLEELRALTADDPELLESLDDLEPLIQWKLAEADETIPLRRDGKLEAAVQ-------IISSDQ--GKVL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 94968801 161 PDEALD--NAERDNAQELTQRRERDSTSSLVTLVASAFVALIAVLAGLFIA 209
COG5278 152 MDAIRQylQEIEEEENERLTQALAEQQNAARTLRIALIIGGIVILLVAVML 202
|
|
cl05000 |
123601 |
CHASE3 |
CHASE3 domain |
CHASE3 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 |
6e-05 |
44.55 |
100.00 |
2,215,0,16,232,16,32 |
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 94968801 216 IVDPIDALNKMAGEIGeSGDLEHTVEIERDDEVGDLAKTFNSMVTYLTE 264
cd06225 1 ILRPLRRLAEAAQRIA-AGDLDVRLPVTGRDEIGELARAFNQMAERLRE 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 |
| 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 |
2e-04 |
43.01 |
100.00 |
2,213,0,19,233,19,34 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 94968801 214 KSIVDPIDALNKMAGEIGEsGDLEHTVEIERDDEVGDLAKTFNSMVTYLTEMAS 267
smart00304 1 RRILRPLRRLAEAAQRIAD-GDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 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 |
| 128579 |
smart00283 |
MA |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). |
true |
true |
false |
262 |
2e-40 |
162.46 |
99.24 |
2,341,0,70,418,70,190 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 342 EVTSTMHEMSVNVQNMVKNTQMQASNVSETSASIDQMVASIQRVADTAKVLLDISNKSREEVHSGITTMTkatdglgRIN 421
smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMD-------QIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 422 TAIQSSSDIIDALGQRADDIGKIIEVIDDLAEQTNLLALNAAIEAARAGEHGLGFAVVADEVRKLAEKSAQSTKEISDLI 501
smart00283 74 EVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 502 QSIQKEARKAVENMEKSTTIVNEGLMLGNELSVALKKISTVVTEVYKFAQEIGAATNEQSHGSSQIARATTRLNEITHEI 581
smart00283 154 KEIQEETNEAVAAMEESSSEVEEGVELVEETGEALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQET 233
|
250 260
....*....|....*....|....*..
gi 94968801 582 NSAVEEQAGGAQQVVRAMERMRELIQQ 608
smart00283 234 AAMSEEISAAAEELSGLAEELKELVEQ 260
|
|
|
|
|
|
|
-1 |
| 109084 |
pfam00015 |
MCPsignal |
Methyl-accepting chemotaxis protein (MCP) signaling domain |
Methyl-accepting chemotaxis protein (MCP) signaling domain |
false |
true |
false |
241 |
8e-33 |
137.17 |
97.51 |
2,363,2,39,412,41,196 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 364 QASNVSETSASIDQMVASIQRVADTAKVLLDISNKSREEvhsgittmtkATDGLGRINTAIQSSSDIIDALGQRADDIGK 443
pfam00015 3 QASAIEQVAASMEQLTATVRDIASNAAQASDLAKQASEE----------ALEEMSQIGQEVDNAVQVMEELATSSKNISD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 444 IIEVIDDLAEQTNLLALNAAIEAARAGEHGLGFAVVADEVRKLAEKSAQSTKEISDLIQSIQKEARKAVENMEKSTTIVN 523
pfam00015 73 IISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEQLIEEIQKESNDAVESMQQTRTQVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 524 EGLMLGNELSVALKKISTVVTEVYKFAQEIGAATNEQSHGSSQIARATTRLNEITHEINSAVEEQAGGAQQVVRAMERMR 603
pfam00015 153 VGSTIVEKTGEALKEIVEAIGEIADEVQEIAAASEEQSAGIEQINQAVERIDQVTQQNAALVEESSAASESLSEQAEELT 232
|
....*
gi 94968801 604 ELIQQ 608
pfam00015 233 ALVAQ 237
|
|
|
|
|
|
|
-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 |
6e-29 |
124.33 |
79.41 |
4,255,81,33,288,116,47,363,163,63,429,226,179 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 256 NSMVTYLTEMASTSEAIAGGDLTVDVRPRSSRD--TLGNAFLGMTEGLRMLVGRVRDSAAQVAAGSNQVADASDESAKIS 333
COG0840 82 RAILEPISDLLEVVERIAAGDLTKRIDESSNDEfgQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 334 VQassaidevtstmhemsvnvqnmvkntqmQASNVSETSASIDQMVASIQRVADTAKVLLDISNKSREEVHSGITTMTKA 413
COG0840 162 DQ----------------------------QAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 414 TDGLGRINTAIQSssdIIDALGQRADDIGKIIEVIDDLAEQTNLLALNAAIEAARAGEHGLGFAVVADEVRKLAEKSAQS 493
COG0840 214 VEQMQEIAEELAE---VVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 494 TKEISDLIQSIQKEARKAVENMEKSTTIVNEGLMLGNELSVALKKISTVVTEVYKFAQEIGAATNEQSHGSSQIARATTR 573
COG0840 291 AKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEE 370
|
330 340 350
....*....|....*....|....*....|....*
gi 94968801 574 LNEITHEINSAVEEQAGGAQQVVRAMERMRELIQQ 608
COG0840 371 LDDVTQENAAAVEELAAASEELKELAEKLLELVAK 405
|
|
|
|
|
|
|
-1 |
| 137524 |
PRK09793 |
PRK09793 |
methyl-accepting protein IV; Provisional |
methyl-accepting protein IV; Provisional |
false |
true |
false |
533 |
4e-21 |
98.61 |
43.15 |
4,348,278,42,397,320,29,433,349,68,515,417,91 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 349 EMSVNVQNMVKNTQMQASNVSETSASIDQMVASIQRVADTAKvlldisnKSREEVHSGITTMTKATDGLGRINTAIQSss 428
PRK09793 279 EIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNAR-------QASELAKNAATTAQAGGVQVSTMTHTMQE-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 429 diidaLGQRADDIGKIIEVIDDLAEQTNLLALNAAIEAARAGEHGLGFAVVADEVRKLAEKSAQSTKEISDLIqsiqkea 508
PRK09793 350 -----IATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLI------- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 509 rkavenmEKSTTIVNEGLMLGNELSVALKKISTVVTEVYKFAQEIGAATNEQSHGSSQIARATTRLNEITHEINSAVEEQ 588
PRK09793 418 -------EESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEA 490
|
250
....*....|....*...
gi 94968801 589 AGGAQQVVRAMERMRELI 606
PRK09793 491 AVATEQLANQADHLSSRV 508
|
|
|
|
|
|
|
-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 |
4e-07 |
51.88 |
19.52 |
6,156,243,17,173,265,19,195,284,37,233,321,10,243,332,16,262,348,34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 157 GQPQPDEALDNAERDNA-----QELTQRRERDSTSSLVTLVasaFVALIAVLAGLFIARRTAKSIVDPIDALNKMAGEIG 231
COG5000 244 VRPVDPKVAEHADLTEGaaaeyRELEAGRDGLQIAFALLYL---STALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVA 320
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94968801 232 EsGDLEHTVEIE-RDDEVGDLAKTFNSMVtylTEMASTSEAIAGGDLTVDVRPRSSRDTLGNAFLG 296
COG5000 321 D-GDLDVQVPVRrVDEDVGRLSKAFNKMT---EQLSSQQEALERAKDALEQRRRFLEAVLSGLTAG 382
|
|
|
|
|
|
|
-1 |
| 138290 |
PRK10935 |
PRK10935 |
nitrate/nitrite sensor protein NarQ; Provisional |
nitrate/nitrite sensor protein NarQ; Provisional |
false |
true |
false |
568 |
1e-04 |
43.71 |
13.20 |
3,187,146,17,204,164,26,231,190,31 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94968801 188 LVTLVASAFVALIAVLA-GLFIARRTAKSIVDPIDALNKMAGEIgESGDLEHTVEIERDDEVGDLAKTFNSMVTYL 262
PRK10935 147 LILLVAISLLGLILILTlVFFTVRFTRRQVVAPLNQLVTASQQI-QKGQFDIPLDTTLPNELGLLAKAFNQMASEL 221
|
|
|
|
|
|
|
-1 |
| 33640 |
COG3850 |
NarQ |
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] |
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction... |
false |
true |
false |
574 |
3e-04 |
42.58 |
16.38 |
4,173,135,12,187,147,17,205,164,27,233,191,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 174 QELTQRRERDSTssLVTLVASAFVALIAVLAgLFIARRTAKSIVDPIDALNKMAGEIGEsGDLEHTVEIERDDEVGDLAK 253
COG3850 136 LALQRFAERKTI--LLVLVQLAGMLLILLLV-VFTIYWLRRRVVRPLNQLTSAAQRIGR-RQFDQRPTDTGRNELGLLGR 211
|
90
....*....|....*...
gi 94968801 254 TFNSMVTYLTEMASTSEA 271
COG3850 212 AFNQMSGELKKLYADLEQ 229
|
|
|
|
|
|
|
-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 |
5e-04 |
41.51 |
77.70 |
4,363,89,61,424,151,110,534,268,25,559,328,78 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 364 QASNVSETSASIDQMVASIQRVADTAKVLLDISNKSREEVHSGITTMTKATDGLGRINTAI-QSSSDIIDALGQRADDIG 442
COG0840 90 DLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIaASATELSARADQQAESLE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 443 KIIEVIDDLAEQTNLLALNAAIEAARAGEHGLGFAVVADEVRKLAEKSAQSTKEISDLIQSIQKEARKAVENMEKSTTIV 522
COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKKLSESSQEIEEITSVINSIA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968801 523 NEGLMLGNELSV-------ALKKISTVVTEVYKFAQEIGAATNE-----------------------------------Q 560
COG0840 250 EQTNLLALNAAIeaarageAGRGFAVVADEVRKLAERSADSAKEigllieeiqneaadavehmeesasevsegvklveeT 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94968801 561 SHGSSQIARATTRLNEITHEINSAVEEQAGGAQQVVRAMERMRELIQQSTSGSTELAASAEQMSKMSRQLLDAMDRF 637
COG0840 330 GSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKF 406
|
|
|
|
|
|
|
-1 |
|