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Conserved domains on  [gi|30265082|ref|NP_847459|]
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methyl-accepting chemotaxis protein [Bacillus anthracis str. Ames]

Protein classification: methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

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 ...
313-512 1.61e-49

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: 170.88  E-value: 1.61e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 313 DDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNATSEVVERLITHTKYIDTAVQSISNIAEQT 392
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 393 NLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMMSQGRSEAFEGIHVIREAGNS 472
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30265082 473 FTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIA 512
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
183-254 2.21e-11

HAMP domain;


:

Pssm-ID: 279063  Cd Length: 69  Bit Score: 60.28  E-value: 2.21e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30265082   183 IFFSLITCTVTSILLAWWFSGKLVKPIQQIDEKLKELAsqDGDLTARLHvTSKDEIGDIANSFNQMLANLQR 254
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIA--SGDLDVPLE-SGRDEIGELARAFNQMAERLRE 69
MCP_signal super family cl23763
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
236-330 3.53e-04

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.


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 304920  Cd Length: 200  Bit Score: 40.68  E-value: 3.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 236 DEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVFIETTASMENTAKTEETMNALEHNIRSQVSSIEESSTAMDDM 315
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 30265082 316 AVSVQRIAESATSVT 330
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
133-562 4.24e-62

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 211.77  E-value: 4.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 133 WDEASKIALAQTDYVNDLLSRFTKYANEENDKRDALIADVESSSSLIQYIIFFSLITCTVTSILLAWWFSGKLVKPIQQI 212
Cdd:COG0840  12 IELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 213 DEKLKELAsqDGDLTARLHVTSKDEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVfiettasmentaktEETMN 292
Cdd:COG0840  92 LEVVERIA--AGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEI--------------AASAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 293 ALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNatsEVVERLI 372
Cdd:COG0840 156 ELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 373 THTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMM 452
Cdd:COG0840 233 ESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHM 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 453 SQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSetaataqsaekk 532
Cdd:COG0840 313 EESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAA------------ 380
                       410       420       430
                ....*....|....*....|....*....|
gi 30265082 533 vvTMNEMTQTAKQMKQTVEELDQLVSHFKT 562
Cdd:COG0840 381 --AVEELAAASEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
313-512 1.61e-49

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: 170.88  E-value: 1.61e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 313 DDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNATSEVVERLITHTKYIDTAVQSISNIAEQT 392
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 393 NLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMMSQGRSEAFEGIHVIREAGNS 472
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30265082 473 FTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIA 512
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
183-254 2.21e-11

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 60.28  E-value: 2.21e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30265082   183 IFFSLITCTVTSILLAWWFSGKLVKPIQQIDEKLKELAsqDGDLTARLHvTSKDEIGDIANSFNQMLANLQR 254
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIA--SGDLDVPLE-SGRDEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
205-256 3.33e-10

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640  Cd Length: 53  Bit Score: 56.49  E-value: 3.33e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30265082    205 LVKPIQQIDEKLKELAsqDGDLTARLHVTSKDEIGDIANSFNQMLANLQRII 256
Cdd:smart00304   3 LLRPLRRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
205-254 4.63e-09

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 53.02  E-value: 4.63e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30265082 205 LVKPIQQIDEKLKELASqdGDLTARLHVTSKDEIGDIANSFNQMLANLQR 254
Cdd:cd06225   1 ILRPLRRLAEAAQRIAA--GDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
236-330 3.53e-04

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: 40.68  E-value: 3.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 236 DEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVFIETTASMENTAKTEETMNALEHNIRSQVSSIEESSTAMDDM 315
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 30265082 316 AVSVQRIAESATSVT 330
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
seadorna_VP4 TIGR04235
seadornavirus VP4 protein; This protein family occurs in the seadornavirus virus group, with ...
294-487 2.79e-03

seadornavirus VP4 protein; This protein family occurs in the seadornavirus virus group, with designation VP4 in Banna virus, Kadipiro virus, and Liao ning virus. Although this family has been suggested to resemble methyltransferases, members show apparent N-terminal sequence similarity to the outer capsid protein VP5 of the orbivirus group, such as bluetongue virus, which also belong to the Reoviridae.


Pssm-ID: 211958  Cd Length: 618  Bit Score: 39.11  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   294 LEHNIrsqvssIEESSTAMDDMAVSVQRIAESATSVTE---LAVATSEQANDGSTVIQKS----VSQMTTIHDAVNATSE 366
Cdd:TIGR04235  45 IEHDI------IKSTKQEMMDRQVLKEDYKALALAVGQeikFDNATQHQLNRLGSAIYKAdherEKELTDLLNAINENEI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   367 VVERLITHTKYIDTavqsisniAEQTNLLaLNASIEAARAgeQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTE 446
Cdd:TIGR04235 119 AVNDIIENQKAITA--------AEKADLI-LEIVISTARA--VAATGRAAADGVGVVPVFGPSVANGAKVGIDTAESVAE 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 30265082   447 TA----SSMMSQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQM 487
Cdd:TIGR04235 188 TAiavkASGIITQLNDVFHAFQSVHVAPNDVIKPAVVVAGTSTDL 232
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
133-562 4.24e-62

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 211.77  E-value: 4.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 133 WDEASKIALAQTDYVNDLLSRFTKYANEENDKRDALIADVESSSSLIQYIIFFSLITCTVTSILLAWWFSGKLVKPIQQI 212
Cdd:COG0840  12 IELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 213 DEKLKELAsqDGDLTARLHVTSKDEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVfiettasmentaktEETMN 292
Cdd:COG0840  92 LEVVERIA--AGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEI--------------AASAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 293 ALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNatsEVVERLI 372
Cdd:COG0840 156 ELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 373 THTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMM 452
Cdd:COG0840 233 ESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHM 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 453 SQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSetaataqsaekk 532
Cdd:COG0840 313 EESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAA------------ 380
                       410       420       430
                ....*....|....*....|....*....|
gi 30265082 533 vvTMNEMTQTAKQMKQTVEELDQLVSHFKT 562
Cdd:COG0840 381 --AVEELAAASEELKELAEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
286-561 7.11e-58

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: 195.58  E-value: 7.11e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    286 KTEETMNALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNATS 365
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    366 EVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDT 445
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    446 ETASSMMSQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSEtaat 525
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAM---- 236
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 30265082    526 aqsaekkvvtMNEMTQTAKQMKQTVEELDQLVSHFK 561
Cdd:smart00283 237 ----------SEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
330-560 2.98e-37

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: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 136.81  E-value: 2.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   330 TELAVATSEQANDGSTVIQKSVSQMTtihdavnatsEVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQ 409
Cdd:pfam00015   1 SDLAQLASEEALDEMSQIGQVVDDAV----------ETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   410 GKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMMSQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQD 489
Cdd:pfam00015  71 GRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30265082   490 ISATAeemaasaeemnaslNNIASISTEVSSETAATAQSAEKKVVTMNEMTQTAKQMKQTVEELDQLVSHF 560
Cdd:pfam00015 151 IAAAS--------------DEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
148-492 2.80e-34

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 135.13  E-value: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  148 NDLLSRFTKYANEENDKRDALIADVESSSSLIQYIIffSLITCTVTSILLAWWFSGK--LVKPIQQIDEKLKELASqdGD 225
Cdd:PRK15048 159 NAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQL--AVIALVVVLILLVAWYGIRrmLLTPLAKIIAHIREIAG--GN 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  226 LTARLHVTSKDEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVfieTTASMENTAKTEEtmnalehnirsQVSSI 305
Cdd:PRK15048 235 LANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREI---AAGNTDLSSRTEQ-----------QASAL 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  306 EESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAvnatsevverlithTKYIDTAVQSI 385
Cdd:PRK15048 301 EETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVI 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  386 SNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMmsqgrseafegihv 465
Cdd:PRK15048 367 DGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVL-------------- 432
                        330       340
                 ....*....|....*....|....*..
gi 30265082  466 IREAGNSFTTIVEQVNKVSTQMQDISA 492
Cdd:PRK15048 433 VESAGETMNNIVNAVTRVTDIMGEIAS 459
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
177-253 1.39e-03

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 40.11  E-value: 1.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30265082   177 SLIQYIIFFSLITcTVTSILLAWWFSGKLVKPIQQIDEKLkelaSQDGDLTARLHV-TSKDEIGDIANSFNQMLANLQ 253
Cdd:TIGR03785 407 KLFNVILAIMSIG-TLALFGFASWISWRIRRLSDDAEAAI----DSQGRISGAIPAsRSRDEIGDLSRSFAQMVARLR 479
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
313-512 1.61e-49

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: 170.88  E-value: 1.61e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 313 DDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNATSEVVERLITHTKYIDTAVQSISNIAEQT 392
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 393 NLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMMSQGRSEAFEGIHVIREAGNS 472
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30265082 473 FTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIA 512
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
183-254 2.21e-11

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 60.28  E-value: 2.21e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30265082   183 IFFSLITCTVTSILLAWWFSGKLVKPIQQIDEKLKELAsqDGDLTARLHvTSKDEIGDIANSFNQMLANLQR 254
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIA--SGDLDVPLE-SGRDEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
205-256 3.33e-10

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640  Cd Length: 53  Bit Score: 56.49  E-value: 3.33e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30265082    205 LVKPIQQIDEKLKELAsqDGDLTARLHVTSKDEIGDIANSFNQMLANLQRII 256
Cdd:smart00304   3 LLRPLRRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
205-254 4.63e-09

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 53.02  E-value: 4.63e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30265082 205 LVKPIQQIDEKLKELASqdGDLTARLHVTSKDEIGDIANSFNQMLANLQR 254
Cdd:cd06225   1 ILRPLRRLAEAAQRIAA--GDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
236-330 3.53e-04

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: 40.68  E-value: 3.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 236 DEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVFIETTASMENTAKTEETMNALEHNIRSQVSSIEESSTAMDDM 315
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 30265082 316 AVSVQRIAESATSVT 330
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
seadorna_VP4 TIGR04235
seadornavirus VP4 protein; This protein family occurs in the seadornavirus virus group, with ...
294-487 2.79e-03

seadornavirus VP4 protein; This protein family occurs in the seadornavirus virus group, with designation VP4 in Banna virus, Kadipiro virus, and Liao ning virus. Although this family has been suggested to resemble methyltransferases, members show apparent N-terminal sequence similarity to the outer capsid protein VP5 of the orbivirus group, such as bluetongue virus, which also belong to the Reoviridae.


Pssm-ID: 211958  Cd Length: 618  Bit Score: 39.11  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   294 LEHNIrsqvssIEESSTAMDDMAVSVQRIAESATSVTE---LAVATSEQANDGSTVIQKS----VSQMTTIHDAVNATSE 366
Cdd:TIGR04235  45 IEHDI------IKSTKQEMMDRQVLKEDYKALALAVGQeikFDNATQHQLNRLGSAIYKAdherEKELTDLLNAINENEI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   367 VVERLITHTKYIDTavqsisniAEQTNLLaLNASIEAARAgeQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTE 446
Cdd:TIGR04235 119 AVNDIIENQKAITA--------AEKADLI-LEIVISTARA--VAATGRAAADGVGVVPVFGPSVANGAKVGIDTAESVAE 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 30265082   447 TA----SSMMSQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQM 487
Cdd:TIGR04235 188 TAiavkASGIITQLNDVFHAFQSVHVAPNDVIKPAVVVAGTSTDL 232
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
133-562 4.24e-62

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 211.77  E-value: 4.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 133 WDEASKIALAQTDYVNDLLSRFTKYANEENDKRDALIADVESSSSLIQYIIFFSLITCTVTSILLAWWFSGKLVKPIQQI 212
Cdd:COG0840  12 IELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 213 DEKLKELAsqDGDLTARLHVTSKDEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVfiettasmentaktEETMN 292
Cdd:COG0840  92 LEVVERIA--AGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEI--------------AASAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 293 ALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNatsEVVERLI 372
Cdd:COG0840 156 ELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 373 THTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMM 452
Cdd:COG0840 233 ESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHM 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 453 SQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSetaataqsaekk 532
Cdd:COG0840 313 EESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAA------------ 380
                       410       420       430
                ....*....|....*....|....*....|
gi 30265082 533 vvTMNEMTQTAKQMKQTVEELDQLVSHFKT 562
Cdd:COG0840 381 --AVEELAAASEELKELAEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
286-561 7.11e-58

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: 195.58  E-value: 7.11e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    286 KTEETMNALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVNATS 365
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    366 EVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDT 445
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    446 ETASSMMSQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSEtaat 525
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAM---- 236
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 30265082    526 aqsaekkvvtMNEMTQTAKQMKQTVEELDQLVSHFK 561
Cdd:smart00283 237 ----------SEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
330-560 2.98e-37

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: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 136.81  E-value: 2.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   330 TELAVATSEQANDGSTVIQKSVSQMTtihdavnatsEVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQ 409
Cdd:pfam00015   1 SDLAQLASEEALDEMSQIGQVVDDAV----------ETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082   410 GKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMMSQGRSEAFEGIHVIREAGNSFTTIVEQVNKVSTQMQD 489
Cdd:pfam00015  71 GRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30265082   490 ISATAeemaasaeemnaslNNIASISTEVSSETAATAQSAEKKVVTMNEMTQTAKQMKQTVEELDQLVSHF 560
Cdd:pfam00015 151 IAAAS--------------DEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
148-492 2.80e-34

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 135.13  E-value: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  148 NDLLSRFTKYANEENDKRDALIADVESSSSLIQYIIffSLITCTVTSILLAWWFSGK--LVKPIQQIDEKLKELASqdGD 225
Cdd:PRK15048 159 NAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQL--AVIALVVVLILLVAWYGIRrmLLTPLAKIIAHIREIAG--GN 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  226 LTARLHVTSKDEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVfieTTASMENTAKTEEtmnalehnirsQVSSI 305
Cdd:PRK15048 235 LANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREI---AAGNTDLSSRTEQ-----------QASAL 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  306 EESSTAMDDMAVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAvnatsevverlithTKYIDTAVQSI 385
Cdd:PRK15048 301 EETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVI 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  386 SNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQQDTETASSMmsqgrseafegihv 465
Cdd:PRK15048 367 DGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVL-------------- 432
                        330       340
                 ....*....|....*....|....*..
gi 30265082  466 IREAGNSFTTIVEQVNKVSTQMQDISA 492
Cdd:PRK15048 433 VESAGETMNNIVNAVTRVTDIMGEIAS 459
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
169-538 7.13e-34

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 133.93  E-value: 7.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  169 IADVESSSSLIQYIIFFSLITCTVTSILLAWWFSGK--LVKPIQQIDEKLKELASqdGDLTARLHVTSKDEIGDIANSFN 246
Cdd:PRK15041 180 IAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKasLVAPMNRLIDSIRHIAG--GDLVKPIEVDGSNEMGQLAESLR 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  247 QMLANLQRIIKQVQQTSTSVKEASENVfiettaSMENtakteetmNALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESA 326
Cdd:PRK15041 258 HMQGELMRTVGDVRNGANAIYSGASEI------ATGN--------NDLSSRTEQQAASLEETAASMEQLTATVKQNAENA 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  327 TSVTELAVATSEQANDGSTVIQKSVSQMTTIhdavnATSevverlithTKYIDTAVQSISNIAEQTNLLALNASIEAARA 406
Cdd:PRK15041 324 RQASHLALSASETAQRGGKVVDNVVQTMRDI-----STS---------SQKIADIISVIDGIAFQTNILALNAAVEAARA 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  407 GEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQiqqdtetassmmSQGRSEAfeGIHVIREAGNSFTTIVEQVNKVSTQ 486
Cdd:PRK15041 390 GEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIED------------SVGKVDV--GSTLVESAGETMAEIVSAVTRVTDI 455
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30265082  487 MQDISATAEEMAASAEEMN---ASLNNIASISTEVSSETAATAQSAEKKVVTMNE 538
Cdd:PRK15041 456 MGEIASASDEQSRGIDQVGlavAEMDRVTQQNAALVEESAAAAAALEEQASRLTE 510
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
182-563 3.04e-24

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 105.15  E-value: 3.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  182 IIFFSLITCTVTSILLAWWFSGKL-VKPIQQIDEKLKELAsqDGDLTARLHVTSKDEIGDIANSFNQMLANLQRIIKQVQ 260
Cdd:PRK09793 190 LVFISMIIVAAIYISSALWWTRKMiVQPLAIIGSHFDSIA--AGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVR 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  261 QTSTSVKEASENVfiettaSMENtakteetmNALEHNIRSQVSSIEESSTAMDDMAVSVQRIAESATSVTELAVATSEQA 340
Cdd:PRK09793 268 KGSQEMHIGIAEI------VAGN--------NDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTA 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  341 NDGSTviqkSVSQMTTIHDAVNATSEVVERLIThtkyidtavqSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEV 420
Cdd:PRK09793 334 QAGGV----QVSTMTHTMQEIATSSQKIGDIIS----------VIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  421 RKLAEQSKTAATDINQLLhqiqqdtETASSMMSQGRSeafegihVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAas 500
Cdd:PRK09793 400 RNLASRSAQAAKEIKGLI-------EESVNRVQQGSK-------LVNNAAATMTDIVSSVTRVNDIMGEIASASEEQR-- 463
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30265082  501 aeemnaslNNIASISTEVSSETAATAQSAEkkvvTMNEMTQTAKQMKQTVEELDQLVSHFKTE 563
Cdd:PRK09793 464 --------RGIEQVAQAVSQMDQVTQQNAS----LVEEAAVATEQLANQADHLSSRVAVFTLE 514
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
170-280 5.32e-07

Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 51.31  E-value: 5.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 170 ADVESSSSLIQYIIFFSLITCTVTSILLAWW----FSGKLVKPIQQIDEKLKELAsqDGDLTARLHVTSKDE-IGDIANS 244
Cdd:COG5000 266 RELEAGRDGLQIAFALLYLSTALLVLLAAIWtaiaFARRIVRPIRKLIEAADEVA--DGDLDVQVPVRRVDEdVGRLSKA 343
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30265082 245 FNQMLANLQRIIKQVQQTSTSVKEASEnvFIETTAS 280
Cdd:COG5000 344 FNKMTEQLSSQQEALERAKDALEQRRR--FLEAVLS 377
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
344-558 2.53e-06

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 49.04  E-value: 2.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 344 STVIQKSVSQMTTihdAVNATSEVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEqgkGFAVVADEVRKL 423
Cdd:COG1511 166 KVVAFPTIYDLGG---GVKGAADGAEKLKDGTDEASNGNKKLSDLLNTLNNSSATFSDGLNALTS---GLTTLTDGLNQL 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 424 AEQSKTAATDINQLLHQIQQdTETASSMMSQGRSEAFEGIhvireagNSFTTIVEQVNKVSTQMQDISATAEEMAASAEE 503
Cdd:COG1511 240 DSGLGTLAAGIGELKQGAEQ-LNEGIGEFSSGLSELNSGV-------QDLAAGVPQLNQGISALAAGLSLPDSLGDQFSS 311
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30265082 504 MNASLNNIASISTEVSSETAATAQSAEKKVVTM----NEMTQTAKQMKQTVEELDQLVS 558
Cdd:COG1511 312 LQEALTQIAQGLKQKTSSSLEAAQGSLSSLQSMlalsKSLDLTAEGATVDALGAPDGVQ 370
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
194-254 9.35e-06

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 46.94  E-value: 9.35e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30265082  194 SILLA----WWFSGKLVKPIQQIDEKLKELASqdGDLTARLHVTSKDEIGDIANSFNQMLANLQR 254
Cdd:PRK10549 173 STLLAalatFLLARGLLAPVKRLVEGTHKLAA--GDFTTRVTPTSRDELGRLAQDFNQLASTLEK 235
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms];
167-262 1.06e-03

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082 167 ALIADVESSSSLIQYIIFFS-LITCTVTSILLAWwFSGKLVKPIQQIDEKLKELASqdGDLTARLHVTSKDEIGDIANSF 245
Cdd:COG5002  16 ASIEDVYNQMNFINNILISGtLIALIITALLGIL-LARTITKPITDMRKQAVDMAR--GNYSRKVKVYGTDEIGELADSF 92
                        90
                ....*....|....*..
gi 30265082 246 NqmlaNLQRIIKQVQQT 262
Cdd:COG5002  93 N----DLTKRVQEAQAN 105
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
182-255 1.32e-03

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 40.02  E-value: 1.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30265082 182 IIFFSLITCTVTSILLAWWFSGKLVKPIQQIDEKLKELasQDGDLTARLHVTSKDEIGDIANSFNQMLANLQRI 255
Cdd:COG3850 152 VQLAGMLLILLLVVFTIYWLRRRVVRPLNQLTSAAQRI--GRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKL 223
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
177-253 1.39e-03

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 40.11  E-value: 1.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30265082   177 SLIQYIIFFSLITcTVTSILLAWWFSGKLVKPIQQIDEKLkelaSQDGDLTARLHV-TSKDEIGDIANSFNQMLANLQ 253
Cdd:TIGR03785 407 KLFNVILAIMSIG-TLALFGFASWISWRIRRLSDDAEAAI----DSQGRISGAIPAsRSRDEIGDLSRSFAQMVARLR 479
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
157-255 3.83e-03

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 38.80  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  157 YANEendkrdaLIADVESSSSLIQYIIFFSLITCTVTSILLAWWFSGKLVKPIQQIDEKLKELASqdgDLTARLHVTSkD 236
Cdd:PRK11360 173 WANE-------LTEDIRRQAWKMDRRIYAVLAAGLVIGLLLIFLLSRRFSANVDIIKDGLSTLEN---DLSTRLPPLP-G 241
                         90
                 ....*....|....*....
gi 30265082  237 EIGDIANSFNQMLANLQRI 255
Cdd:PRK11360 242 ELGEISQAINNLAQALRET 260
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
194-263 5.24e-03

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 38.14  E-value: 5.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30265082   194 SILLAWWFSGKLVKPIQQIDEKLKELASQDgdLTARLHVTSK-DEIGDIANSFNQMLANLQRIIKQVQQTS 263
Cdd:TIGR01386 177 TALLGWWITRLGLEPLRRLSAVAARISPES--LDQRLDPSRApAELRELAQSFNAMLGRLEDAFQRLSQFS 245
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
236-362 7.56e-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: 36.88  E-value: 7.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082    236 DEIGDIANSFNQMLANLQRIIKQVQQTSTSVKEASENVFIETTASMENTAKTEETMNALEHNIRSQVSSIEESSTAMDDM 315
Cdd:smart00283 133 DEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQ 212
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 30265082    316 AVSVQRIAESATSVTELAVATSEQANDGSTVIQKSVSQMTTIHDAVN 362
Cdd:smart00283 213 AAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVE 259
PRK12807 PRK12807
flagellin; Provisional
306-555 8.43e-03

flagellin; Provisional


Pssm-ID: 171737 [Multi-domain]  Cd Length: 287  Bit Score: 37.11  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  306 EESSTAMDDMAvSVQRIAESATSVTELAVATSEQANDGSTVI-----QKSVSQMTTIHDAVNATSEVVERLithtkyIDT 380
Cdd:PRK12807  21 DKMNVSMNRLS-SGKRINSAADDAAGLAIATRMRARQSGLEKasqntQDGMSLIRTAESAMNSVSNILTRM------RDI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  381 AVQSISNIAEQTNLLALNA-------SIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDIN---------QLLHQIQQD 444
Cdd:PRK12807  94 AVQSSNGTNTAENQSALQKefaelqeQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISietldssatNQQITIKLA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265082  445 TETASSMMSQGRSEAfEGIHVIREAGNSFTTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSETAA 524
Cdd:PRK12807 174 NTTAEKLGIDATTSN-ISISGAASALAAISALNTALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMA 252
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 30265082  525 TAQSAEKKVVTMNE----MTQTAKQMKQTVEELDQ 555
Cdd:PRK12807 253 KEMSEMTKFKILNEagisMLSQANQTPQMVSKLLQ 287
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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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