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Conserved domains on  [gi|118474888|ref|YP_891524|]
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methyl-accepting chemotaxis protein [Campylobacter fetus subsp. fetus 82-40]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
270-430 2.14e-48

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 165.49  E-value: 2.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 270 ISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:cd11386   17 VAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:cd11386   97 AGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQ 176

                 .
gi 118474888 430 Q 430
Cdd:cd11386  177 E 177
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
154-256 9.33e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 52.64  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 154 SMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSFSNsKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLE 233
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 118474888 234 ASYNPVRNEDGKIYKVIKFATDI 256
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
33-134 2.68e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 51.09  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  33 MAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLPDvvRSMEYDNFWID-LRAGKSKSGLFRRIAKGGKDIYLE 111
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPE--DREELRERLENlLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 118474888 112 ANYIPILDVNGRVYKIIKFANDI 134
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
34-261 8.86e-21

FOG: PAS/PAC domain [Signal transduction mechanisms]


:

Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 89.91  E-value: 8.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  34 AVIEFSTEGIIIDANENFLRTMGYTLDEIkdkhHSMFCLPDVVRSMEYDNFWIDLRAGKSK-SGLFRRIAKGGKDIYLEA 112
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEEL----LGLLLALHPEDRDRLRELLRRLLAGEELlSEELRLVRKDGEERWVEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 113 NYIPILDVNGRVYKIIkFANDITTRHYELMDLKNT-----IYAANRSMAIIEFRPDGTIINANENFLRTMGYTLDE--IK 185
Cdd:COG2202   77 SAAPLRDGEGRVLGLL-GLRDITERKRAEEALRESeerlrALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEelGR 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118474888 186 DKHHSMLCDSSFSNSKEYvGFWTKLRNGEFQSGKYVRYGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDISEQVI 261
Cdd:COG2202  156 GLSDLIHPEDEERRELEL-ARALAEGRGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERKQ 230
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
270-430 2.14e-48

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 165.49  E-value: 2.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 270 ISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:cd11386   17 VAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:cd11386   97 AGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQ 176

                 .
gi 118474888 430 Q 430
Cdd:cd11386  177 E 177
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
154-256 9.33e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 52.64  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 154 SMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSFSNsKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLE 233
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 118474888 234 ASYNPVRNEDGKIYKVIKFATDI 256
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
33-134 2.68e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 51.09  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  33 MAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLPDvvRSMEYDNFWID-LRAGKSKSGLFRRIAKGGKDIYLE 111
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPE--DREELRERLENlLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 118474888 112 ANYIPILDVNGRVYKIIKFANDI 134
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
223-259 1.56e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 36.39  E-value: 1.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 118474888   223 YGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDISEQ 259
Cdd:smart00086   7 RRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
21-74 6.69e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 34.68  E-value: 6.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 118474888    21 ELQDILRAIkhTMAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLPD 74
Cdd:smart00091   2 RLRAILESL--PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPE 53
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
34-261 8.86e-21

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 89.91  E-value: 8.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  34 AVIEFSTEGIIIDANENFLRTMGYTLDEIkdkhHSMFCLPDVVRSMEYDNFWIDLRAGKSK-SGLFRRIAKGGKDIYLEA 112
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEEL----LGLLLALHPEDRDRLRELLRRLLAGEELlSEELRLVRKDGEERWVEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 113 NYIPILDVNGRVYKIIkFANDITTRHYELMDLKNT-----IYAANRSMAIIEFRPDGTIINANENFLRTMGYTLDE--IK 185
Cdd:COG2202   77 SAAPLRDGEGRVLGLL-GLRDITERKRAEEALRESeerlrALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEelGR 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118474888 186 DKHHSMLCDSSFSNSKEYvGFWTKLRNGEFQSGKYVRYGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDISEQVI 261
Cdd:COG2202  156 GLSDLIHPEDEERRELEL-ARALAEGRGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERKQ 230
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
270-430 9.14e-48

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 165.92  E-value: 9.14e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   270 ISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:smart00283  44 IAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGE 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:smart00283 124 AGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQ 203

                   .
gi 118474888   430 Q 430
Cdd:smart00283 204 E 204
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
254-430 8.89e-41

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 150.53  E-value: 8.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 254 TDISEQVIKDQEKLKLISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSstlVASLNQQSDEIKSIIQTISDIADQT 333
Cdd:COG0840  176 EELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEV---VKKLSESSQEIEEITSVINSIAEQT 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 334 NLLALNAAIEAARAGDHGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDC 413
Cdd:COG0840  253 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSS 332
                        170
                 ....*....|....*..
gi 118474888 414 MQKIRASSAEVANAMSQ 430
Cdd:COG0840  333 LGEIAAAIEEVSQLISE 349
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
270-429 1.31e-35

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 131.41  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  270 ISDLADKNDNLTQDGDRVIENTVSNVQNIadmmsqsstlVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:pfam00015   3 ASDLAQLASEEALDEMSQIGQVVDDAVET----------MEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:pfam00015  73 QGRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQ 152
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
271-430 4.58e-24

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 103.16  E-value: 4.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 271 SDLADKNDNLTQDGDRVIENTVSNVQNIADmmsqsstlvaslnqQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGDH 350
Cdd:PRK15048 325 SQLAQSASDTAQHGGKVVDGVVKTMHEIAD--------------SSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 351 GRGFAVVADEVRSLAERTEHSVSEISTTIS---SIRDVTSQVVQSIKDGLEDVnqsVELAKEAKDCMQKIRASSAEVANA 427
Cdd:PRK15048 391 GRGFAVVAGEVRNLASRSAQAAKEIKALIEdsvSRVDTGSVLVESAGETMNNI---VNAVTRVTDIMGEIASASDEQSRG 467

                 ...
gi 118474888 428 MSQ 430
Cdd:PRK15048 468 IDQ 470
PAS_9 pfam13426
PAS domain;
154-258 1.55e-17

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 77.81  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  154 SMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSfSNSKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLE 233
Cdd:pfam13426   1 PDGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDLFGPG-TDEEAVARLREALRNGGEVEVELELRRKDGEPFPVL 79
                          90       100
                  ....*....|....*....|....*
gi 118474888  234 ASYNPVRNEDGKIYKVIKFATDISE 258
Cdd:pfam13426  80 VSASPVRDEDGEVVGIVGILRDITE 104
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
23-138 3.60e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator [Regulatory functions, Small molecule interactions].


Pssm-ID: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 51.13  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   23 QDILRAIKHTMAV--IEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLP-DVVRSMEYdnFWIDLRAGKS-KSGLF 98
Cdd:TIGR00229   2 EERYRAIFESSPDaiIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEeDREEVRER--IERRLEGEREpVSEER 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 118474888   99 RRIAKGGKDIYLEANYIPILDVNGRVYkIIKFANDITTRH 138
Cdd:TIGR00229  80 RVRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITERK 118
PRK13558 PRK13558
bacterio-opsin activator; Provisional
161-283 2.64e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 41.75  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 161 RPDGTIINANENFLRTMGYTLDEIKDKHHSMLcDSSFSNSKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLEASYNPVR 240
Cdd:PRK13558 168 LPDEPLIYINDAFERITGYSPDEVLGRNCRFL-QGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIR 246
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 118474888 241 NEDGKIYKVIKFATDISEQ------VIKDQEKLKlisDLADKNDNLTQD 283
Cdd:PRK13558 247 DEDGTVTHYVGFQTDVTERkeaelaLQRERRKLQ---RLLERVEGLVND 292
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
270-430 2.14e-48

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 165.49  E-value: 2.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 270 ISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:cd11386   17 VAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:cd11386   97 AGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQ 176

                 .
gi 118474888 430 Q 430
Cdd:cd11386  177 E 177
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
154-256 9.33e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 52.64  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 154 SMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSFSNsKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLE 233
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 118474888 234 ASYNPVRNEDGKIYKVIKFATDI 256
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
33-134 2.68e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 51.09  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  33 MAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLPDvvRSMEYDNFWID-LRAGKSKSGLFRRIAKGGKDIYLE 111
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPE--DREELRERLENlLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 118474888 112 ANYIPILDVNGRVYKIIKFANDI 134
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
223-259 1.56e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 36.39  E-value: 1.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 118474888   223 YGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDISEQ 259
Cdd:smart00086   7 RRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
21-74 6.69e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 34.68  E-value: 6.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 118474888    21 ELQDILRAIkhTMAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLPD 74
Cdd:smart00091   2 RLRAILESL--PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPE 53
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
253-334 9.68e-03

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 36.06  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 253 ATDISEQVIKDQEKLKLISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQ 332
Cdd:cd11386  119 AKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198

                 ..
gi 118474888 333 TN 334
Cdd:cd11386  199 IA 200
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
34-261 8.86e-21

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 89.91  E-value: 8.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  34 AVIEFSTEGIIIDANENFLRTMGYTLDEIkdkhHSMFCLPDVVRSMEYDNFWIDLRAGKSK-SGLFRRIAKGGKDIYLEA 112
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEEL----LGLLLALHPEDRDRLRELLRRLLAGEELlSEELRLVRKDGEERWVEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 113 NYIPILDVNGRVYKIIkFANDITTRHYELMDLKNT-----IYAANRSMAIIEFRPDGTIINANENFLRTMGYTLDE--IK 185
Cdd:COG2202   77 SAAPLRDGEGRVLGLL-GLRDITERKRAEEALRESeerlrALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEelGR 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118474888 186 DKHHSMLCDSSFSNSKEYvGFWTKLRNGEFQSGKYVRYGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDISEQVI 261
Cdd:COG2202  156 GLSDLIHPEDEERRELEL-ARALAEGRGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERKQ 230
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
270-430 9.14e-48

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 165.92  E-value: 9.14e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   270 ISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:smart00283  44 IAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGE 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:smart00283 124 AGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQ 203

                   .
gi 118474888   430 Q 430
Cdd:smart00283 204 E 204
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
254-430 8.89e-41

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 150.53  E-value: 8.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 254 TDISEQVIKDQEKLKLISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSstlVASLNQQSDEIKSIIQTISDIADQT 333
Cdd:COG0840  176 EELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEV---VKKLSESSQEIEEITSVINSIAEQT 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 334 NLLALNAAIEAARAGDHGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDC 413
Cdd:COG0840  253 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSS 332
                        170
                 ....*....|....*..
gi 118474888 414 MQKIRASSAEVANAMSQ 430
Cdd:COG0840  333 LGEIAAAIEEVSQLISE 349
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
270-429 1.31e-35

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 131.41  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  270 ISDLADKNDNLTQDGDRVIENTVSNVQNIadmmsqsstlVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGD 349
Cdd:pfam00015   3 ASDLAQLASEEALDEMSQIGQVVDDAVET----------MEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  350 HGRGFAVVADEVRSLAERTEHSVSEISTTISSIRDVTSQVVQSIKDGLEDVNQSVELAKEAKDCMQKIRASSAEVANAMS 429
Cdd:pfam00015  73 QGRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQ 152
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
271-430 4.58e-24

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 103.16  E-value: 4.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 271 SDLADKNDNLTQDGDRVIENTVSNVQNIADmmsqsstlvaslnqQSDEIKSIIQTISDIADQTNLLALNAAIEAARAGDH 350
Cdd:PRK15048 325 SQLAQSASDTAQHGGKVVDGVVKTMHEIAD--------------SSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 351 GRGFAVVADEVRSLAERTEHSVSEISTTIS---SIRDVTSQVVQSIKDGLEDVnqsVELAKEAKDCMQKIRASSAEVANA 427
Cdd:PRK15048 391 GRGFAVVAGEVRNLASRSAQAAKEIKALIEdsvSRVDTGSVLVESAGETMNNI---VNAVTRVTDIMGEIASASDEQSRG 467

                 ...
gi 118474888 428 MSQ 430
Cdd:PRK15048 468 IDQ 470
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
256-430 1.34e-22

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 98.87  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 256 ISEQVIKDQEKLKLISDLADKNDNLTQDGDRVIENTVSNVQNIAdmmsqsstlvaslnQQSDEIKSIIQTISDIADQTNL 335
Cdd:PRK15041 312 LTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIS--------------TSSQKIADIISVIDGIAFQTNI 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 336 LALNAAIEAARAGDHGRGFAVVADEVRSLAERTEHSVSEISTTIS---SIRDVTSQVVQSIKDGLEDVNQSVelaKEAKD 412
Cdd:PRK15041 378 LALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEdsvGKVDVGSTLVESAGETMAEIVSAV---TRVTD 454
                        170
                 ....*....|....*...
gi 118474888 413 CMQKIRASSAEVANAMSQ 430
Cdd:PRK15041 455 IMGEIASASDEQSRGIDQ 472
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
268-430 1.50e-21

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 95.52  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 268 KLISDLADKNDNLTQDGDrVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQTNLLALNAAIEAARA 347
Cdd:PRK09793 307 QLTATVGQNADNARQASE-LAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARA 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 348 GDHGRGFAVVADEVRSLAERTEHSVSEISTTI-SSIRDVT--SQVVQSIKDGLEDVNQSVelaKEAKDCMQKIRASSAE- 423
Cdd:PRK09793 386 GEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIeESVNRVQqgSKLVNNAAATMTDIVSSV---TRVNDIMGEIASASEEq 462
                        170
                 ....*....|...
gi 118474888 424 ------VANAMSQ 430
Cdd:PRK09793 463 rrgieqVAQAVSQ 475
PAS_9 pfam13426
PAS domain;
154-258 1.55e-17

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 77.81  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  154 SMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSfSNSKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLE 233
Cdd:pfam13426   1 PDGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDLFGPG-TDEEAVARLREALRNGGEVEVELELRRKDGEPFPVL 79
                          90       100
                  ....*....|....*....|....*
gi 118474888  234 ASYNPVRNEDGKIYKVIKFATDISE 258
Cdd:pfam13426  80 VSASPVRDEDGEVVGIVGILRDITE 104
PAS_9 pfam13426
PAS domain;
33-135 7.97e-16

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 72.80  E-value: 7.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   33 MAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFcLPDVVRSMEYDNFWIDLRAGKSKSGLFRRIAKGGKDIYLEA 112
Cdd:pfam13426   2 DGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDL-FGPGTDEEAVARLREALRNGGEVEVELELRRKDGEPFPVLV 80
                          90       100
                  ....*....|....*....|...
gi 118474888  113 NYIPILDVNGRVYKIIKFANDIT 135
Cdd:pfam13426  81 SASPVRDEDGEVVGIVGILRDIT 103
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
166-253 6.12e-11

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 58.55  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  166 IINANENFLRTMGYTLDEIK----DKHHSMLCDSSFSNSKEYVGFWtkLRNGEFQSGKYVRYGKGGKVVYLEASYNPVRN 241
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELKssyeGWLDLVHPEDRERVRRALQELL--LKKGEPYSGEYRIRRKDGSYRWVEARGRPIRD 78
                          90
                  ....*....|..
gi 118474888  242 EDGKIYKVIKFA 253
Cdd:pfam08447  79 ENGKPVRVIGVA 90
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
44-131 1.18e-10

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 57.78  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   44 IIDANENFLRTMGYTLDEIK----DKHHSMFClPDVVR-SMEYDNFWidLRAGKSKSGLFRRIAKGGKDIYLEANYIPIL 118
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELKssyeGWLDLVHP-EDRERvRRALQELL--LKKGEPYSGEYRIRRKDGSYRWVEARGRPIR 77
                          90
                  ....*....|...
gi 118474888  119 DVNGRVYKIIKFA 131
Cdd:pfam08447  78 DENGKPVRVIGVA 90
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
11-138 2.96e-09

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 56.01  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  11 QIQQTDTHCTELQDILRAI--KHTMAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLPDvVRSMEYDNFWIDL 88
Cdd:COG2202   99 ERKRAEEALRESEERLRALleASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPE-DEERRELELARAL 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 118474888  89 RAGKSKS--GLFRRIAKGGKDIYLEANYIPILDVNGRVYKIIKFANDITTRH 138
Cdd:COG2202  178 AEGRGGPleIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERK 229
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
23-138 3.60e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator [Regulatory functions, Small molecule interactions].


Pssm-ID: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 51.13  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   23 QDILRAIKHTMAV--IEFSTEGIIIDANENFLRTMGYTLDEIKDKHHSMFCLP-DVVRSMEYdnFWIDLRAGKS-KSGLF 98
Cdd:TIGR00229   2 EERYRAIFESSPDaiIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEeDREEVRER--IERRLEGEREpVSEER 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 118474888   99 RRIAKGGKDIYLEANYIPILDVNGRVYkIIKFANDITTRH 138
Cdd:TIGR00229  80 RVRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITERK 118
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
152-260 5.85e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 50.49  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  152 NRSMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKH-HSMLCDSSFSnskEYVGFWTK-LRNGEFQSGKYVrYGKGGKV 229
Cdd:pfam08448   3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTlAELLPPEDAA---RLERALRRaLEGEEPIDFLEE-LLLNGEE 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 118474888  230 VYLEASYNPVRNEDGKIYKVIKFATDISEQV 260
Cdd:pfam08448  79 RHYELRLTPLRDPDGEVIGVLVISRDITERR 109
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
33-138 8.16e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 49.72  E-value: 8.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   33 MAVIEFSTEGIIIDANENFLRTMGYTLDEIKDKH-HSMFCLPDVVRSMEYDNFWidLRAGKSKSGLFRRIAkGGKDIYLE 111
Cdd:pfam08448   6 DALAVLDPDGRVRYANAAAAELFGLPPEELLGKTlAELLPPEDAARLERALRRA--LEGEEPIDFLEELLL-NGEERHYE 82
                          90       100
                  ....*....|....*....|....*..
gi 118474888  112 ANYIPILDVNGRVYKIIKFANDITTRH 138
Cdd:pfam08448  83 LRLTPLRDPDGEVIGVLVISRDITERR 109
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
156-258 9.00e-07

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator [Regulatory functions, Small molecule interactions].


Pssm-ID: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 46.89  E-value: 9.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  156 AIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSFSN-SKEYvgFWTKLRNG-EFQSGKYVRYGKGGKVVYLE 233
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREeVRER--IERRLEGErEPVSEERRVRRKDGSEIWVE 92
                          90       100
                  ....*....|....*....|....*
gi 118474888  234 ASYNPVRNEDGKIYkVIKFATDISE 258
Cdd:TIGR00229  93 VSVSPIRTNGGELG-VVGIVRDITE 116
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
166-267 1.48e-04

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions].


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 42.58  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  166 IINANENFLRTMGYTLDEIKDKHHSMLCDSSfSNSKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLEASYNPVRNEDGK 245
Cdd:TIGR02938  26 ILYANDAFTRITGYTKEEIIGKNESVLSNHT-TPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVAPVLNEAGE 104
                          90       100
                  ....*....|....*....|....*..
gi 118474888  246 IYKVIKFATDISE-----QVIKDQEKL 267
Cdd:TIGR02938 105 TTHFLGMHRDITElhrleQVVANQKLL 131
PRK13558 PRK13558
bacterio-opsin activator; Provisional
161-283 2.64e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 41.75  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 161 RPDGTIINANENFLRTMGYTLDEIKDKHHSMLcDSSFSNSKEYVGFWTKLRNGEFQSGKYVRYGKGGKVVYLEASYNPVR 240
Cdd:PRK13558 168 LPDEPLIYINDAFERITGYSPDEVLGRNCRFL-QGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIR 246
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 118474888 241 NEDGKIYKVIKFATDISEQ------VIKDQEKLKlisDLADKNDNLTQD 283
Cdd:PRK13558 247 DEDGTVTHYVGFQTDVTERkeaelaLQRERRKLQ---RLLERVEGLVND 292
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
141-260 7.22e-04

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 40.34  E-value: 7.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 141 LMDLK--NTIYAANRSMAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLcdssFSNSKEYVGFWTK-LRNGEFQS 217
Cdd:PRK11360 257 LRETRslNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSEL----FPPNTPFASPLLDtLEHGTEHV 332
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 118474888 218 GKYVRYGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDISEQV 260
Cdd:PRK11360 333 DLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERK 375
Ttg2C COG1463
ABC-type transport system involved in resistance to organic solvents, periplasmic component ...
254-412 9.82e-04

ABC-type transport system involved in resistance to organic solvents, periplasmic component [Secondary metabolites biosynthesis, transport, and catabolism]


Pssm-ID: 224380 [Multi-domain]  Cd Length: 359  Bit Score: 39.75  E-value: 9.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 254 TDISEQVIKDQEKLkLISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLVASLNQQSDEIKSIIQTISDIADQT 333
Cdd:COG1463  149 LLLLGGLDPDRLNA-ILNEAAAALAGTGPQLNALLDNLAQFTDALNARDGDIGALIANLNQLLDSLAAASDQLDRLLDNL 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 334 NLL---------ALNAAIEAARAgdhgrgfavVADEVRSLAERTEHSVseiSTTISSIRDVTsQVVQSIKDGLEDVNQSV 404
Cdd:COG1463  228 ATLtaalaarrdALDDALAALSA---------LAATVNDLLAENRPNL---NQALANLRPLA-TLLVDYLPGLEQLLHGL 294

                 ....*...
gi 118474888 405 ELAKEAKD 412
Cdd:COG1463  295 PTYAANLV 302
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
156-256 1.33e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 36.99  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  156 AIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSML---CDSSFsnskeYVGFWTKLRNGEFQSGKYVRY-GKGGKVVY 231
Cdd:pfam00989  13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLipeEDDAV-----AELLRQALLQGEESRGFEVSFrVRDGRPRH 87
                          90       100
                  ....*....|....*....|....*
gi 118474888  232 LEASYNPVRNEDGKIYkVIKFATDI 256
Cdd:pfam00989  88 VEVRASPVRDAGGEIG-FLGVLRDI 111
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
26-134 1.63e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 36.99  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   26 LRAIKHTM--AVIEFSTEGIIIDANENFLRTMGYTLDEIKDKHhsmfcLPDVVR---SMEYDNFWIDLRAG-KSKSGLFR 99
Cdd:pfam00989   3 LRAILESLpdGIFVVDEDGRILYVNAAAEELLGLSREEVIGKS-----LLDLIPeedDAVAELLRQALLQGeESRGFEVS 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 118474888  100 RIAKGGKDIYLEANYIPILDVNGRVYkIIKFANDI 134
Cdd:pfam00989  78 FRVRDGRPRHVEVRASPVRDAGGEIG-FLGVLRDI 111
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
253-388 2.27e-03

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 38.04  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   253 ATDISEQVIKDQEKLKLISDLADKNDNLTQDGDRVIENTVSNVQNIADMMSQSSTLV----ASLNQQSDEIKSIIQTISD 328
Cdd:smart00283 146 AKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVqeiaAATDEQAAGSEEVNAAIDE 225
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888   329 IADqtnllalnaaieaaragdhgrgfavVADEVRSLAERTEHSVSEISTTISSIRDVTSQ 388
Cdd:smart00283 226 IAQ-------------------------VTQETAAMSEEISAAAEELSGLAEELDELVER 260
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
56-266 7.76e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 37.06  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888  56 GYTLDEIKDKHHSMFcLPDVVRSMEYDNFWIDLRAGKSK-SGLFRRIA---KGGKDIYLEANYIPIlDVNGRVYKIIkFA 131
Cdd:PRK11359  46 GYKREEVIGNNIDML-IPRDLRPAHPEYIRHNREGGKARvEGMSRELQlekKDGSKIWTRFALSKV-SAEGKVYYLA-LV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118474888 132 NDITTRHYELMDLKNTIYAANRS-MAIIEFRPDGTIINANENFLRTMGYTLDEIKDKHHSMLCDSSFSNSKEYVGFWTKL 210
Cdd:PRK11359 123 RDASVEMAQKEQTRQLIIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLL 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118474888 211 RNGEFQSGKYVRYGKGGKVVYLEASYNPVRNEDGKIYKVIKFATDIS-EQVIKDQEK 266
Cdd:PRK11359 203 WKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITeERQIRQLEG 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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