NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|33596249|ref|NP_883892|]
View 

methyl-accepting chemotaxis protein [Bordetella parapertussis 12822]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
302-501 1.30e-54

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: 184.75  E-value: 1.30e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 302 EAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQT 381
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 382 NILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSVGRMSTGSAQAGRAGETMRELVQSVERVTAL 461
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33596249 462 MAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELT 501
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
24-114 4.97e-13

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: 65.73  E-value: 4.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAMPV- 102
Cdd:cd00130   8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIr 87
                        90
                ....*....|..
gi 33596249 103 IEAGNVTGYASV 114
Cdd:cd00130  88 DEGGEVIGLLGV 99
HAMP pfam00672
HAMP domain;
203-269 9.72e-05

HAMP domain;


:

Pssm-ID: 250044  Cd Length: 70  Bit Score: 40.68  E-value: 9.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33596249   203 WGAYALGALGAVLAAMALGGRFGRQLRNAEEVARQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSL 269
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRL 68
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
279-522 4.34e-64

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: 212.15  E-value: 4.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    279 KTSEHVHTIS----RLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELV 354
Cdd:smart00283   1 DVSEAVEEIAagaeEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    355 ATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLI------- 427
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    428 -------DDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGEL 500
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 33596249    501 THVAEHLGQESGSLVEAIGVFR 522
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
30-115 6.17e-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: 59.32  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    30 ITYCNPAFIAISGFSREELLGQPHNIVR--HPDMPEDVFADMW-ATLQARKPWLAVVKNRHKSGGFYWVLANAMPVI-EA 105
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELKSSYEGWLDlvHPEDRERVRRALQeLLLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRdEN 80
                          90
                  ....*....|
gi 33596249   106 GNVTGYASVR 115
Cdd:pfam08447  81 GKPVRVIGVA 90
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
302-501 1.30e-54

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: 184.75  E-value: 1.30e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 302 EAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQT 381
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 382 NILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSVGRMSTGSAQAGRAGETMRELVQSVERVTAL 461
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33596249 462 MAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELT 501
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
24-114 4.97e-13

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: 65.73  E-value: 4.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAMPV- 102
Cdd:cd00130   8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIr 87
                        90
                ....*....|..
gi 33596249 103 IEAGNVTGYASV 114
Cdd:cd00130  88 DEGGEVIGLLGV 99
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
24-74 9.53e-07

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: 46.62  E-value: 9.53e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 33596249     24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQ 74
Cdd:smart00091  17 LDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
HAMP pfam00672
HAMP domain;
203-269 9.72e-05

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 40.68  E-value: 9.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33596249   203 WGAYALGALGAVLAAMALGGRFGRQLRNAEEVARQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSL 269
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRL 68
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
409-533 5.24e-03

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from Escherichia coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 250719  Cd Length: 201  Bit Score: 36.98  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   409 VRSLAQRTAqaAKEVK-VLIDDSVG----------RMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVA 477
Cdd:pfam01580  59 ILSLAARHS--PEEVRlYLIDPKGGelaaledlphLLSPVATDPEDALSALRALVAEMERRYALLKQLGVRSIEEYNGEI 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 33596249   478 QISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEaiGVFRTPGAGARAIGM 533
Cdd:pfam01580 137 AEDILGGGWLEELPPIVVIVDERAELMLAAPKDSEMRVE--GALARLARMGRAAGI 190
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
279-522 4.34e-64

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: 212.15  E-value: 4.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    279 KTSEHVHTIS----RLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELV 354
Cdd:smart00283   1 DVSEAVEEIAagaeEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    355 ATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLI------- 427
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    428 -------DDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGEL 500
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 33596249    501 THVAEHLGQESGSLVEAIGVFR 522
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
30-115 6.17e-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: 59.32  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    30 ITYCNPAFIAISGFSREELLGQPHNIVR--HPDMPEDVFADMW-ATLQARKPWLAVVKNRHKSGGFYWVLANAMPVI-EA 105
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELKSSYEGWLDlvHPEDRERVRRALQeLLLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRdEN 80
                          90
                  ....*....|
gi 33596249   106 GNVTGYASVR 115
Cdd:pfam08447  81 GKPVRVIGVA 90
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
198-543 3.59e-84

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 274.19  E-value: 3.59e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  198 AAPYGWGAYALGALGAVLAAMALGGRFG--RQLRN--AEEVA--RQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSLIG 271
Cdd:PRK15048 184 ADDYRFAQWQLAVIALVVVLILLVAWYGirRMLLTplAKIIAhiREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTD 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  272 ISTEVIGKTSEHVHTISRLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVG 351
Cdd:PRK15048 264 TVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVD 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  352 ELVATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSV 431
Cdd:PRK15048 344 GVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSV 423
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  432 GRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQES 511
Cdd:PRK15048 424 SRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQA 503
                        330       340       350
                 ....*....|....*....|....*....|..
gi 33596249  512 GSLVEAIGVFRTPGAGARAIGMPEQAPRRAPA 543
Cdd:PRK15048 504 SRLTQAVSAFRLAASPLTNKPQTPSRPASEQP 535
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
207-523 1.74e-66

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 223.33  E-value: 1.74e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 207 ALGALGAVLAAMALGGRFGRQLRNAEEVARQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSLIGISTEVIGKTSEHVHT 286
Cdd:COG0840  67 LVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGA 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 287 ISRLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQG------- 359
Cdd:COG0840 147 SEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEiaeelae 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 360 ----LDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLI-------- 427
Cdd:COG0840 227 vvkkLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIeeiqneaa 306
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 428 ------DDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELT 501
Cdd:COG0840 307 davehmEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELA 386
                       330       340
                ....*....|....*....|..
gi 33596249 502 HVAEHLGQESGSLVEAIGVFRT 523
Cdd:COG0840 387 AASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
331-522 3.43e-55

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: 186.88  E-value: 3.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   331 VAARLTQESSEVAA----QGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVA 406
Cdd:pfam00015   2 QASDLAQLASEEALdemsQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   407 AEVRSLAQRTAQAAKEVKVLIDDSVGRM--------------STGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQ 472
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVKQTndstasiqqtrtevEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 33596249   473 STGVAQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEAIGVFR 522
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
24-121 2.56e-14

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: 70.00  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKN-RHKSGGFYWVLANAMPV 102
Cdd:TIGR00229  19 IDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEREPVSEERRvRRKDGSEIWVEVSVSPI 98
                          90       100
                  ....*....|....*....|....*
gi 33596249   103 IEAGNVTGYASV------RVKATQA 121
Cdd:TIGR00229  99 RTNGGELGVVGIvrditeRKQAEEA 123
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
10-120 3.80e-09

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 56.01  E-value: 3.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  10 HEFVLQDDQYLISKTDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQA--RKPWLAVVKNRH 87
Cdd:COG2202 114 LRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEgrGGPLEIEYRVRR 193
                        90       100       110
                ....*....|....*....|....*....|....
gi 33596249  88 KSGG-FYWVLANAMPVIEAGNVTGYASVRVKATQ 120
Cdd:COG2202 194 KDGErVRWILSRISPVRDDGEIVGVVGIARDITE 227
PRK13558 PRK13558
bacterio-opsin activator; Provisional
30-111 1.12e-05

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 46.75  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   30 ITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAMPV-IEAGNV 108
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIrDEDGTV 252

                 ...
gi 33596249  109 TGY 111
Cdd:PRK13558 253 THY 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
287-522 1.11e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 40.42  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    287 ISRLREDSQGLAARTEAQSAALQDTASSVEQLAETV----------------------TRNAESAGVAARLTQ---ESSE 341
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleelsrqisalrkdlaRLEAEVEQLEERIAQlskELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    342 VAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEgiAFQTNILALNAAVEAARA--GEQGKGFAVVAAEVRSLAQRTAQA 419
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIE--QLKEELKALREALDELRAelTLLNEEAANLRERLESLERRIAAT 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    420 AKEVKVLiddsvgrmstgSAQAGRAGETMRELVQSVERVTALMAEISTA----SGEQSTGVAQISSAVHRMEEVVQQNVS 495
Cdd:TIGR02168  837 ERRLEDL-----------EEQIEELSEDIESLAAEIEELEELIEELESElealLNERASLEEALALLRSELEELSEELRE 905
                          250       260       270
                   ....*....|....*....|....*....|
gi 33596249    496 M---VGELTHVAEHLGQESGSLVEAIGVFR 522
Cdd:TIGR02168  906 LeskRSELRRELEELREKLAQLELRLEGLE 935
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
302-501 1.30e-54

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: 184.75  E-value: 1.30e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 302 EAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQT 381
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 382 NILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSVGRMSTGSAQAGRAGETMRELVQSVERVTAL 461
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33596249 462 MAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELT 501
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
24-114 4.97e-13

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: 65.73  E-value: 4.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAMPV- 102
Cdd:cd00130   8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIr 87
                        90
                ....*....|..
gi 33596249 103 IEAGNVTGYASV 114
Cdd:cd00130  88 DEGGEVIGLLGV 99
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
24-74 9.53e-07

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: 46.62  E-value: 9.53e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 33596249     24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQ 74
Cdd:smart00091  17 LDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
HAMP pfam00672
HAMP domain;
203-269 9.72e-05

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 40.68  E-value: 9.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33596249   203 WGAYALGALGAVLAAMALGGRFGRQLRNAEEVARQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSL 269
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRL 68
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
409-533 5.24e-03

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from Escherichia coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 250719  Cd Length: 201  Bit Score: 36.98  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   409 VRSLAQRTAqaAKEVK-VLIDDSVG----------RMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVA 477
Cdd:pfam01580  59 ILSLAARHS--PEEVRlYLIDPKGGelaaledlphLLSPVATDPEDALSALRALVAEMERRYALLKQLGVRSIEEYNGEI 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 33596249   478 QISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEaiGVFRTPGAGARAIGM 533
Cdd:pfam01580 137 AEDILGGGWLEELPPIVVIVDERAELMLAAPKDSEMRVE--GALARLARMGRAAGI 190
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
279-522 4.34e-64

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: 212.15  E-value: 4.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    279 KTSEHVHTIS----RLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELV 354
Cdd:smart00283   1 DVSEAVEEIAagaeEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    355 ATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLI------- 427
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    428 -------DDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGEL 500
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 33596249    501 THVAEHLGQESGSLVEAIGVFR 522
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
30-115 6.17e-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: 59.32  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    30 ITYCNPAFIAISGFSREELLGQPHNIVR--HPDMPEDVFADMW-ATLQARKPWLAVVKNRHKSGGFYWVLANAMPVI-EA 105
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELKSSYEGWLDlvHPEDRERVRRALQeLLLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRdEN 80
                          90
                  ....*....|
gi 33596249   106 GNVTGYASVR 115
Cdd:pfam08447  81 GKPVRVIGVA 90
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
198-543 3.59e-84

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 274.19  E-value: 3.59e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  198 AAPYGWGAYALGALGAVLAAMALGGRFG--RQLRN--AEEVA--RQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSLIG 271
Cdd:PRK15048 184 ADDYRFAQWQLAVIALVVVLILLVAWYGirRMLLTplAKIIAhiREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTD 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  272 ISTEVIGKTSEHVHTISRLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVG 351
Cdd:PRK15048 264 TVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVD 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  352 ELVATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSV 431
Cdd:PRK15048 344 GVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSV 423
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  432 GRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQES 511
Cdd:PRK15048 424 SRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQA 503
                        330       340       350
                 ....*....|....*....|....*....|..
gi 33596249  512 GSLVEAIGVFRTPGAGARAIGMPEQAPRRAPA 543
Cdd:PRK15048 504 SRLTQAVSAFRLAASPLTNKPQTPSRPASEQP 535
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
236-545 9.90e-82

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 267.98  E-value: 9.90e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  236 RQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSLIGISTEVIGKTSEHVHTISRLREDSQGLAARTEAQSAALQDTASSV 315
Cdd:PRK15041 230 RHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASM 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  316 EQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARA 395
Cdd:PRK15041 310 EQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARA 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  396 GEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTG 475
Cdd:PRK15041 390 GEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRG 469
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  476 VAQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEAIGVFRTPGAGARAIGMPEQAPRRAPART 545
Cdd:PRK15041 470 IDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPATP 539
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
238-522 1.16e-73

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 245.75  E-value: 1.16e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  238 IAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSLIGISTEViGKTSEHVHT-ISRLREDSQGLAARTEAQSAALQDTASSVE 316
Cdd:PRK09793 228 IAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDV-RKGSQEMHIgIAEIVAGNNDLSSRTEQQAASLAQTAASME 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  317 QLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAG 396
Cdd:PRK09793 307 QLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAG 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  397 EQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGV 476
Cdd:PRK09793 387 EQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGI 466
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 33596249  477 AQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEAIGVFR 522
Cdd:PRK09793 467 EQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
207-523 1.74e-66

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 223.33  E-value: 1.74e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 207 ALGALGAVLAAMALGGRFGRQLRNAEEVARQIAAGNLVNEVDSGVGGEMRNLYFYLDIMRKSLIGISTEVIGKTSEHVHT 286
Cdd:COG0840  67 LVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGA 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 287 ISRLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATMQG------- 359
Cdd:COG0840 147 SEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEiaeelae 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 360 ----LDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLI-------- 427
Cdd:COG0840 227 vvkkLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIeeiqneaa 306
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249 428 ------DDSVGRMSTGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELT 501
Cdd:COG0840 307 davehmEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELA 386
                       330       340
                ....*....|....*....|..
gi 33596249 502 HVAEHLGQESGSLVEAIGVFRT 523
Cdd:COG0840 387 AASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
331-522 3.43e-55

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: 186.88  E-value: 3.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   331 VAARLTQESSEVAA----QGGAVVGELVATMQGLDASSRKMAEIVSVIEGIAFQTNILALNAAVEAARAGEQGKGFAVVA 406
Cdd:pfam00015   2 QASDLAQLASEEALdemsQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   407 AEVRSLAQRTAQAAKEVKVLIDDSVGRM--------------STGSAQAGRAGETMRELVQSVERVTALMAEISTASGEQ 472
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVKQTndstasiqqtrtevEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 33596249   473 STGVAQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEAIGVFR 522
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
PAS_9 pfam13426
PAS domain;
24-114 2.45e-17

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 78.19  E-value: 2.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAMPVI 103
Cdd:pfam13426   7 LDPEGRIVYANPAALRLLGYTREELLGKSIRDLFGPGTDEEAVARLREALRNGGEVEVELELRRKDGEPFPVLVSASPVR 86
                          90
                  ....*....|..
gi 33596249   104 -EAGNVTGYASV 114
Cdd:pfam13426  87 dEDGEVVGIVGI 98
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
24-121 2.56e-14

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: 70.00  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKN-RHKSGGFYWVLANAMPV 102
Cdd:TIGR00229  19 IDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEREPVSEERRvRRKDGSEIWVEVSVSPI 98
                          90       100
                  ....*....|....*....|....*
gi 33596249   103 IEAGNVTGYASV------RVKATQA 121
Cdd:TIGR00229  99 RTNGGELGVVGIvrditeRKQAEEA 123
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
21-111 5.55e-13

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: 69.93  E-value: 5.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    21 ISKTDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAM 100
Cdd:TIGR02938  17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96
                          90
                  ....*....|..
gi 33596249   101 PVI-EAGNVTGY 111
Cdd:TIGR02938  97 PVLnEAGETTHF 108
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
24-111 2.94e-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: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 60.88  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    24 TDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPeDVFADMWATLQARKPWLAV-VKNRHKSGGFYWVLANAMPV 102
Cdd:pfam00989  17 VDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDD-AVAELLRQALLQGEESRGFeVSFRVRDGRPRHVEVRASPV 95

                  ....*....
gi 33596249   103 IEAGNVTGY 111
Cdd:pfam00989  96 RDAGGEIGF 104
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
10-120 3.80e-09

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 56.01  E-value: 3.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  10 HEFVLQDDQYLISKTDLKGRITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQA--RKPWLAVVKNRH 87
Cdd:COG2202 114 LRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEgrGGPLEIEYRVRR 193
                        90       100       110
                ....*....|....*....|....*....|....
gi 33596249  88 KSGG-FYWVLANAMPVIEAGNVTGYASVRVKATQ 120
Cdd:COG2202 194 KDGErVRWILSRISPVRDDGEIVGVVGIARDITE 227
PRK13558 PRK13558
bacterio-opsin activator; Provisional
30-111 1.12e-05

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 46.75  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249   30 ITYCNPAFIAISGFSREELLGQPHNIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANAMPV-IEAGNV 108
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIrDEDGTV 252

                 ...
gi 33596249  109 TGY 111
Cdd:PRK13558 253 THY 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
287-522 1.11e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 40.42  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    287 ISRLREDSQGLAARTEAQSAALQDTASSVEQLAETV----------------------TRNAESAGVAARLTQ---ESSE 341
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleelsrqisalrkdlaRLEAEVEQLEERIAQlskELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    342 VAAQGGAVVGELVATMQGLDASSRKMAEIVSVIEgiAFQTNILALNAAVEAARA--GEQGKGFAVVAAEVRSLAQRTAQA 419
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIE--QLKEELKALREALDELRAelTLLNEEAANLRERLESLERRIAAT 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249    420 AKEVKVLiddsvgrmstgSAQAGRAGETMRELVQSVERVTALMAEISTA----SGEQSTGVAQISSAVHRMEEVVQQNVS 495
Cdd:TIGR02168  837 ERRLEDL-----------EEQIEELSEDIESLAAEIEELEELIEELESElealLNERASLEEALALLRSELEELSEELRE 905
                          250       260       270
                   ....*....|....*....|....*....|
gi 33596249    496 M---VGELTHVAEHLGQESGSLVEAIGVFR 522
Cdd:TIGR02168  906 LeskRSELRRELEELREKLAQLELRLEGLE 935
COG5283 COG5283
Phage-related tail protein [Function unknown]
287-519 3.28e-03

Phage-related tail protein [Function unknown]


Pssm-ID: 227608 [Multi-domain]  Cd Length: 1213  Bit Score: 39.14  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  287 ISRLREDSQGLAARTEAQSAALQDTASSVEQLAETVTRNAESAGVAARLTQESSEVAAQGGAVVGELVATM--------Q 358
Cdd:COG5283   73 YEDLKQEVKEVNRATQASKKAYQEYNAQYTQAENKLRSLSGQFGVASEQLMLQQKEIQRLQYAISTLNKSMaaqarlleQ 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  359 GLDASSRKMAEIVSVIEGIAFQTNilALNAAVEaaragEQGKGFAVVAAEVRSLAQRTAQAAKEVKVLIDDSVGRMSTGS 438
Cdd:COG5283  153 TGNKFGTADAKVVGLRESFGRQTE--ALNKQLE-----RTKKVADALTYVLDEAQQKLSQALSARLERLQESRTQMSQSS 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  439 AQAGRAGETMRELVQSVERVTALMAEISTASGEQSTGVAQISSAVHRMEEVVQQNVSMVGELTHVAEHLGQESGSLVEAI 518
Cdd:COG5283  226 GQLGKRLETDKAGAGALGLLGAALAGSFAAIGAAVRRTAQMNGELMDKTKQVKGARDNLGKVTSQGEEMSDAIQETAEHI 305

                 .
gi 33596249  519 G 519
Cdd:COG5283  306 K 306
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
20-139 5.10e-03

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 37.52  E-value: 5.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33596249  20 LISKTDLKGRITYCNPAFIAISGFSREELLGQPhnIVRHPDMPEDVFADMWATLQARKPWLAVVKNRHKSGGFYWVLANA 99
Cdd:COG2202   1 LILVLDRDGRIIYANEAAEELLGYSAEELLGLL--LALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSA 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 33596249 100 MPVI-EAGNVTGYASV-----RVKATQAQIEAAEHFYAQVESGRMG 139
Cdd:COG2202  79 APLRdGEGRVLGLLGLrditeRKRAEEALRESEERLRALLEASPDG 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH