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Conserved domains on  [gi|30023073|ref|NP_834704.1|]
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methyl-accepting chemotaxis protein [Bacillus cereus ATCC 14579]

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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 ...
301-500 6.01e-50

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: 172.04  E-value: 6.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 301 DDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNATSEVVERLITHTKYIDTAVQSISNIAEQT 380
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 381 NLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVIREAGTS 460
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30023073 461 FSTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIA 500
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
193-242 5.76e-08

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: 49.94  E-value: 5.76e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30023073 193 LVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQH 242
Cdd:cd06225   1 ILRPLRRLAEAAQRIAA--GDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
224-318 3.75e-03

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


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 37.60  E-value: 3.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 224 DEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEKTNTSREATLRVQSSMSNLNASIQSQTSSMEESSTAMDDM 303
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 30023073 304 AVSVQRIAESASSVA 318
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
CHASE3 super family cl05000
CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes ...
5-187 7.25e-03

CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE3 domains are found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE3 domains are not known at this time.


The actual alignment was detected with superfamily member COG5278:

Pssm-ID: 262402  Cd Length: 207  Bit Score: 36.58  E-value: 7.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   5 ICALFGVALAFILFFAIDQSRKAETLQkEISPLATELKERGDAYQVQLSALRGYLLQHDQVELDKFNE----MSKRLEDS 80
Cdd:COG5278  18 GVLLLLLASGASYWSIQKSNQSTREVI-ETQQVLAAALDLLSAVSDAESGQRGYLLTGNDEYLEPYEEateeLDQKLEEL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  81 KDKLLSNPNLSSSVkSTMELGSTWRKFIEEKVFTLAKEQKWEEALQVASSENGTVykVIGDFTNYSNEQA----KLREQS 156
Cdd:COG5278  97 RALTADDPELLESL-DDLEPLIQWKLAEADETIPLRRDGKLEAAVQIISSDQGKV--LMDAIRQYLQEIEeeenERLTQA 173
                       170       180       190
                ....*....|....*....|....*....|.
gi 30023073 157 IEKIDQSALLIEYVIFLSLVVCIIVAIILAW 187
Cdd:COG5278 174 LAEQQNAARTLRIALIIGGIVILLVAVMLAL 204
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
135-550 1.52e-61

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 209.85  E-value: 1.52e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 135 VYKVIGDFTNYSNEQAKLREQSIEKIDQSALLIEYVIFLSLVVCIIVAIILAWWFSGKLVKPIQQIDTKLKELASqeGDL 214
Cdd:COG0840  26 LKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAA--GDL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 215 TARLQVNSNDEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEktntsreatlrvqsSMSNLNASIQSQTSSME 294
Cdd:COG0840 104 TKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAA--------------SATELSARADQQAESLE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 295 ESSTAMDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNatsEVVERLITHTKYIDTAVQSIS 374
Cdd:COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLSESSQEIEEITSVIN 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 375 NIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVI 454
Cdd:COG0840 247 SIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLV 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 455 REAGTSFSTIVEQVNKVSTQMQDISataeemaasaeemnASLNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTARKM 534
Cdd:COG0840 327 EETGSSLGEIAAAIEEVSQLISEIA--------------AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEEL 392
                       410
                ....*....|....*.
gi 30023073 535 KQTVEELDQLVSHFKT 550
Cdd:COG0840 393 KELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
301-500 6.01e-50

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: 172.04  E-value: 6.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 301 DDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNATSEVVERLITHTKYIDTAVQSISNIAEQT 380
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 381 NLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVIREAGTS 460
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30023073 461 FSTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIA 500
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
193-242 5.76e-08

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: 49.94  E-value: 5.76e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30023073 193 LVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQH 242
Cdd:cd06225   1 ILRPLRRLAEAAQRIAA--GDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
HAMP pfam00672
HAMP domain;
171-242 3.32e-13

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 65.33  E-value: 3.32e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30023073   171 IFLSLVVCIIVAIILAWWFSGKLVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQH 242
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIAS--GDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
193-245 8.45e-09

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 52.25  E-value: 8.45e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 30023073    193 LVKPIQQIDTKLKELAsqEGDLTARLQVNSNDEIGAIATSFNKMLENLQHIIN 245
Cdd:smart00304   3 LLRPLRRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
224-318 3.75e-03

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


Pssm-ID: 206779  Cd Length: 200  Bit Score: 37.60  E-value: 3.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 224 DEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEKTNTSREATLRVQSSMSNLNASIQSQTSSMEESSTAMDDM 303
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 30023073 304 AVSVQRIAESASSVA 318
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
CHASE3 COG5278
Extracellular (periplasmic) sensor domain CHASE3 (specificity unknown) [Signal transduction ...
5-187 7.25e-03

Extracellular (periplasmic) sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 227603  Cd Length: 207  Bit Score: 36.58  E-value: 7.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   5 ICALFGVALAFILFFAIDQSRKAETLQkEISPLATELKERGDAYQVQLSALRGYLLQHDQVELDKFNE----MSKRLEDS 80
Cdd:COG5278  18 GVLLLLLASGASYWSIQKSNQSTREVI-ETQQVLAAALDLLSAVSDAESGQRGYLLTGNDEYLEPYEEateeLDQKLEEL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  81 KDKLLSNPNLSSSVkSTMELGSTWRKFIEEKVFTLAKEQKWEEALQVASSENGTVykVIGDFTNYSNEQA----KLREQS 156
Cdd:COG5278  97 RALTADDPELLESL-DDLEPLIQWKLAEADETIPLRRDGKLEAAVQIISSDQGKV--LMDAIRQYLQEIEeeenERLTQA 173
                       170       180       190
                ....*....|....*....|....*....|.
gi 30023073 157 IEKIDQSALLIEYVIFLSLVVCIIVAIILAW 187
Cdd:COG5278 174 LAEQQNAARTLRIALIIGGIVILLVAVMLAL 204
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
135-550 1.52e-61

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 209.85  E-value: 1.52e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 135 VYKVIGDFTNYSNEQAKLREQSIEKIDQSALLIEYVIFLSLVVCIIVAIILAWWFSGKLVKPIQQIDTKLKELASqeGDL 214
Cdd:COG0840  26 LKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAA--GDL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 215 TARLQVNSNDEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEktntsreatlrvqsSMSNLNASIQSQTSSME 294
Cdd:COG0840 104 TKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAA--------------SATELSARADQQAESLE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 295 ESSTAMDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNatsEVVERLITHTKYIDTAVQSIS 374
Cdd:COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLSESSQEIEEITSVIN 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 375 NIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVI 454
Cdd:COG0840 247 SIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLV 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 455 REAGTSFSTIVEQVNKVSTQMQDISataeemaasaeemnASLNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTARKM 534
Cdd:COG0840 327 EETGSSLGEIAAAIEEVSQLISEIA--------------AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEEL 392
                       410
                ....*....|....*.
gi 30023073 535 KQTVEELDQLVSHFKT 550
Cdd:COG0840 393 KELAEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
275-549 1.43e-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: 197.51  E-value: 1.43e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073    275 VQSSMSNLNASIQSQTSSMEESSTAMDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNATSE 354
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073    355 VVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTE 434
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073    435 TASSMMSQGRSEAFEGINVIREAGTSFSTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSETAATA 514
Cdd:smart00283 162 EAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 30023073    515 QSAEQkvivmnemtvtarkMKQTVEELDQLVSHFK 549
Cdd:smart00283 242 AAAEE--------------LSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
315-551 3.35e-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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 136.81  E-value: 3.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   315 SSVAELAVATSEHASDGSTVIQKSVSQMTtiheavnatsEVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARA 394
Cdd:pfam00015   1 AQASDLAQLASEEALDEMSQIGQVVDDAV----------ETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   395 GEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVIREAGTSFSTIVEQVNKVSTQ 474
Cdd:pfam00015  71 GEQGRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADI 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30023073   475 MQDISATAeemaasaeemnaslNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTARKMKQTVEELDQLVSHFKTE 551
Cdd:pfam00015 151 VQEIAAAS--------------DEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
142-532 2.87e-32

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 128.92  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  142 FTNYSNEQAKLREQSIEKIDQSALLIEYVifLSLVVCIIVAIILAWWFSGK--LVKPIQQIDTKLKELASqeGDLTARLQ 219
Cdd:PRK15041 167 YVAYMEQNDRLYDIAVSDNNASYSQAMWI--LVGVMIVVLAVIFAVWFGIKasLVAPMNRLIDSIRHIAG--GDLVKPIE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  220 VNSNDEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEKTNtsreatlrvqssmsNLNASIQSQTSSMEESSTA 299
Cdd:PRK15041 243 VDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNN--------------DLSSRTEQQAASLEETAAS 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  300 MDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIheavnATSevverlithTKYIDTAVQSISNIAEQ 379
Cdd:PRK15041 309 MEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDI-----STS---------SQKIADIISVIDGIAFQ 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  380 TNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMmsqgrseafeginvIREAGT 459
Cdd:PRK15041 375 TNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTL--------------VESAGE 440
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30023073  460 SFSTIVEQVNKVSTQMQDISATAEEMAASAEEMN---ASLNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTAR 532
Cdd:PRK15041 441 TMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGlavAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
149-289 3.10e-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: 38.96  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   149 QAKLREQSIEKIDQSALliEYVIFLSLVVCIIVAIIL---AWWFSGKLVKPIQQIDTKLkelaSQEGDLTARLQV-NSND 224
Cdd:TIGR03785 389 IAEQTTNGIRTLRNSAL--EKLFNVILAIMSIGTLALfgfASWISWRIRRLSDDAEAAI----DSQGRISGAIPAsRSRD 462
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30023073   225 EIGAIATSFNKMLENLQhiinrvqktsvEVQTASENMLEK-TNTSREATLRVQSSMSNLNASIQSQ 289
Cdd:TIGR03785 463 EIGDLSRSFAQMVARLR-----------QYTHYLENMSSRlSHELRTPVAVVRSSLENLELQALEQ 517
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
301-500 6.01e-50

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: 172.04  E-value: 6.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 301 DDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNATSEVVERLITHTKYIDTAVQSISNIAEQT 380
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 381 NLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVIREAGTS 460
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30023073 461 FSTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIA 500
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
193-242 5.76e-08

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: 49.94  E-value: 5.76e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30023073 193 LVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQH 242
Cdd:cd06225   1 ILRPLRRLAEAAQRIAA--GDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
HAMP pfam00672
HAMP domain;
171-242 3.32e-13

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 65.33  E-value: 3.32e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30023073   171 IFLSLVVCIIVAIILAWWFSGKLVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQH 242
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIAS--GDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
193-245 8.45e-09

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 52.25  E-value: 8.45e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 30023073    193 LVKPIQQIDTKLKELAsqEGDLTARLQVNSNDEIGAIATSFNKMLENLQHIIN 245
Cdd:smart00304   3 LLRPLRRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
224-318 3.75e-03

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


Pssm-ID: 206779  Cd Length: 200  Bit Score: 37.60  E-value: 3.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 224 DEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEKTNTSREATLRVQSSMSNLNASIQSQTSSMEESSTAMDDM 303
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 30023073 304 AVSVQRIAESASSVA 318
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
CHASE3 COG5278
Extracellular (periplasmic) sensor domain CHASE3 (specificity unknown) [Signal transduction ...
5-187 7.25e-03

Extracellular (periplasmic) sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 227603  Cd Length: 207  Bit Score: 36.58  E-value: 7.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   5 ICALFGVALAFILFFAIDQSRKAETLQkEISPLATELKERGDAYQVQLSALRGYLLQHDQVELDKFNE----MSKRLEDS 80
Cdd:COG5278  18 GVLLLLLASGASYWSIQKSNQSTREVI-ETQQVLAAALDLLSAVSDAESGQRGYLLTGNDEYLEPYEEateeLDQKLEEL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  81 KDKLLSNPNLSSSVkSTMELGSTWRKFIEEKVFTLAKEQKWEEALQVASSENGTVykVIGDFTNYSNEQA----KLREQS 156
Cdd:COG5278  97 RALTADDPELLESL-DDLEPLIQWKLAEADETIPLRRDGKLEAAVQIISSDQGKV--LMDAIRQYLQEIEeeenERLTQA 173
                       170       180       190
                ....*....|....*....|....*....|.
gi 30023073 157 IEKIDQSALLIEYVIFLSLVVCIIVAIILAW 187
Cdd:COG5278 174 LAEQQNAARTLRIALIIGGIVILLVAVMLAL 204
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
135-550 1.52e-61

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 209.85  E-value: 1.52e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 135 VYKVIGDFTNYSNEQAKLREQSIEKIDQSALLIEYVIFLSLVVCIIVAIILAWWFSGKLVKPIQQIDTKLKELASqeGDL 214
Cdd:COG0840  26 LKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAA--GDL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 215 TARLQVNSNDEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEktntsreatlrvqsSMSNLNASIQSQTSSME 294
Cdd:COG0840 104 TKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAA--------------SATELSARADQQAESLE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 295 ESSTAMDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNatsEVVERLITHTKYIDTAVQSIS 374
Cdd:COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLSESSQEIEEITSVIN 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 375 NIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVI 454
Cdd:COG0840 247 SIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLV 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 455 REAGTSFSTIVEQVNKVSTQMQDISataeemaasaeemnASLNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTARKM 534
Cdd:COG0840 327 EETGSSLGEIAAAIEEVSQLISEIA--------------AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEEL 392
                       410
                ....*....|....*.
gi 30023073 535 KQTVEELDQLVSHFKT 550
Cdd:COG0840 393 KELAEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
275-549 1.43e-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: 197.51  E-value: 1.43e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073    275 VQSSMSNLNASIQSQTSSMEESSTAMDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIHEAVNATSE 354
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073    355 VVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTE 434
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073    435 TASSMMSQGRSEAFEGINVIREAGTSFSTIVEQVNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSETAATA 514
Cdd:smart00283 162 EAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 30023073    515 QSAEQkvivmnemtvtarkMKQTVEELDQLVSHFK 549
Cdd:smart00283 242 AAAEE--------------LSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
315-551 3.35e-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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 136.81  E-value: 3.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   315 SSVAELAVATSEHASDGSTVIQKSVSQMTtiheavnatsEVVERLITHTKYIDTAVQSISNIAEQTNLLALNASIEAARA 394
Cdd:pfam00015   1 AQASDLAQLASEEALDEMSQIGQVVDDAV----------ETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   395 GEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMMSQGRSEAFEGINVIREAGTSFSTIVEQVNKVSTQ 474
Cdd:pfam00015  71 GEQGRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADI 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30023073   475 MQDISATAeemaasaeemnaslNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTARKMKQTVEELDQLVSHFKTE 551
Cdd:pfam00015 151 VQEIAAAS--------------DEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
142-532 2.87e-32

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 128.92  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  142 FTNYSNEQAKLREQSIEKIDQSALLIEYVifLSLVVCIIVAIILAWWFSGK--LVKPIQQIDTKLKELASqeGDLTARLQ 219
Cdd:PRK15041 167 YVAYMEQNDRLYDIAVSDNNASYSQAMWI--LVGVMIVVLAVIFAVWFGIKasLVAPMNRLIDSIRHIAG--GDLVKPIE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  220 VNSNDEIGAIATSFNKMLENLQHIINRVQKTSVEVQTASENMLEKTNtsreatlrvqssmsNLNASIQSQTSSMEESSTA 299
Cdd:PRK15041 243 VDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNN--------------DLSSRTEQQAASLEETAAS 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  300 MDDMAVSVQRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTIheavnATSevverlithTKYIDTAVQSISNIAEQ 379
Cdd:PRK15041 309 MEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDI-----STS---------SQKIADIISVIDGIAFQ 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  380 TNLLALNASIEAARAGEQGKGFAVVADEVRKLAEQSKTAATDINQLLHQIQNDTETASSMmsqgrseafeginvIREAGT 459
Cdd:PRK15041 375 TNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTL--------------VESAGE 440
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30023073  460 SFSTIVEQVNKVSTQMQDISATAEEMAASAEEMN---ASLNNIASISTEVSSETAATAQSAEQKVIVMNEMTVTAR 532
Cdd:PRK15041 441 TMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGlavAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
173-549 2.42e-31

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 126.27  E-value: 2.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  173 LSLVVCIIVAIILAWWFSGK--LVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQHIINRVQKT 250
Cdd:PRK15048 194 LAVIALVVVLILLVAWYGIRrmLLTPLAKIIAHIREIAG--GNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREG 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  251 SVEVQTAsenmlektntsreaTLRVQSSMSNLNASIQSQTSSMEESSTAMDDMAVSVQRIAESASSVAELAVATSEHASD 330
Cdd:PRK15048 272 SDAIYAG--------------TREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQH 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  331 GSTVIQKSVSQMTTIHEAvnatsevverlithTKYIDTAVQSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEVRK 410
Cdd:PRK15048 338 GGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRN 403
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  411 LAEQSKTAATDINQLLHQIQNDTETASSMmsqgrseafeginvIREAGTSFSTIVEQVNKVSTQMQDISATAEEMAasae 490
Cdd:PRK15048 404 LASRSAQAAKEIKALIEDSVSRVDTGSVL--------------VESAGETMNNIVNAVTRVTDIMGEIASASDEQS---- 465
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30023073  491 emnaslNNIASISTEVSSETAATAQSAEqkviVMNEMTVTARKMKQTVEELDQLVSHFK 549
Cdd:PRK15048 466 ------RGIDQVALAVSEMDRVTQQNAS----LVQESAAAAAALEEQASRLTQAVSAFR 514
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
170-551 7.06e-26

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 110.16  E-value: 7.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  170 VIFLSLVVCIIVAIILAWWFSGKL-VKPIQQIDTKLKELAsqEGDLTARLQVNSNDEIGAIATSFNKMLENLQHIINRVQ 248
Cdd:PRK09793 190 LVFISMIIVAAIYISSALWWTRKMiVQPLAIIGSHFDSIA--AGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVR 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  249 KTSVEVQTASENMLEKTNtsreatlrvqssmsNLNASIQSQTSSMEESSTAMDDMAVSVQRIAESASSVAELAVATSEHA 328
Cdd:PRK09793 268 KGSQEMHIGIAEIVAGNN--------------DLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTA 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  329 SDGSTviqkSVSQMTTIHEAVNATSEVVERLIThtkyidtavqSISNIAEQTNLLALNASIEAARAGEQGKGFAVVADEV 408
Cdd:PRK09793 334 QAGGV----QVSTMTHTMQEIATSSQKIGDIIS----------VIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  409 RKLAEQSKTAATDINQLLHQIQNDTETASSMmsqgrseafeginvIREAGTSFSTIVEQVNKVSTQMQDISATAEEMAas 488
Cdd:PRK09793 400 RNLASRSAQAAKEIKGLIEESVNRVQQGSKL--------------VNNAAATMTDIVSSVTRVNDIMGEIASASEEQR-- 463
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30023073  489 aeemnaslNNIASISTEVSSETAATAQSAEqkviVMNEMTVTARKMKQTVEELDQLVSHFKTE 551
Cdd:PRK09793 464 --------RGIEQVAQAVSQMDQVTQQNAS----LVEEAAVATEQLANQADHLSSRVAVFTLE 514
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
150-241 5.27e-09

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 57.47  E-value: 5.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 150 AKLREQSIEKID-QSALLIEYVIFLSLVvcIIVAIILAWWFSGKLVKPIQQIDTKLKELAsqEGDLTARLQVNSNDE-IG 227
Cdd:COG5000 263 AEYRELEAGRDGlQIAFALLYLSTALLV--LLAAIWTAIAFARRIVRPIRKLIEAADEVA--DGDLDVQVPVRRVDEdVG 338
                        90
                ....*....|....
gi 30023073 228 AIATSFNKMLENLQ 241
Cdd:COG5000 339 RLSKAFNKMTEQLS 352
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
308-520 3.61e-05

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


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 45.19  E-value: 3.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 308 QRIAESASSVAELAVATSEHASDGSTVIQKSVSQMTTiheAVNATSEVVERLITHTKYIDTAVQSISNIAEQTNLLALNA 387
Cdd:COG1511 142 PKITEKAADKLLNEISKELTETYTKVVAFPTIYDLGG---GVKGAADGAEKLKDGTDEASNGNKKLSDLLNTLNNSSATF 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 388 SIEAARAGEqgkGFAVVADEVRKLAEQSKTAATDINQLLhQIQNDTETASSMMSQGRSEAFEGINvireagtSFSTIVEQ 467
Cdd:COG1511 219 SDGLNALTS---GLTTLTDGLNQLDSGLGTLAAGIGELK-QGAEQLNEGIGEFSSGLSELNSGVQ-------DLAAGVPQ 287
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 30023073 468 VNKVSTQMQDISATAEEMAASAEEMNASLNNIASISTEVSSETAATAQSAEQK 520
Cdd:COG1511 288 LNQGISALAAGLSLPDSLGDQFSSLQEALTQIAQGLKQKTSSSLEAAQGSLSS 340
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms];
154-241 1.43e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 43.19  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 154 EQSIEKI-DQSALLIEYVIFLSLVVCIIVAIILAWwFSGKLVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATS 232
Cdd:COG5002  15 EASIEDVyNQMNFINNILISGTLIALIITALLGIL-LARTITKPITDMRKQAVDMAR--GNYSRKVKVYGTDEIGELADS 91

                ....*....
gi 30023073 233 FNKMLENLQ 241
Cdd:COG5002  92 FNDLTKRVQ 100
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
162-278 1.63e-04

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 43.10  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073 162 QSALLIeyVIFLSLVVCIivaiilaWWFSGKLVKPIQQIDTKLKELasQEGDLTARLQVNSNDEIGAIATSFNKMLENLq 241
Cdd:COG3850 153 QLAGML--LILLLVVFTI-------YWLRRRVVRPLNQLTSAAQRI--GRRQFDQRPTDTGRNELGLLGRAFNQMSGEL- 220
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30023073 242 HIINRVQKTSVEVQTASenmLEKTNtsREATLRVQSS 278
Cdd:COG3850 221 KKLYADLEQRVEEKTRD---LEQKN--QRLSFLYQSS 252
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
182-241 1.31e-03

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 40.00  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073  182 AIILAWWFSGKLVKPIQQIDTKLKELASqeGDLTARLQVNSNDEIGAIATSFNKMLENLQ 241
Cdd:PRK10549 177 AALATFLLARGLLAPVKRLVEGTHKLAA--GDFTTRVTPTSRDELGRLAQDFNQLASTLE 234
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
149-289 3.10e-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: 38.96  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   149 QAKLREQSIEKIDQSALliEYVIFLSLVVCIIVAIIL---AWWFSGKLVKPIQQIDTKLkelaSQEGDLTARLQV-NSND 224
Cdd:TIGR03785 389 IAEQTTNGIRTLRNSAL--EKLFNVILAIMSIGTLALfgfASWISWRIRRLSDDAEAAI----DSQGRISGAIPAsRSRD 462
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30023073   225 EIGAIATSFNKMLENLQhiinrvqktsvEVQTASENMLEK-TNTSREATLRVQSSMSNLNASIQSQ 289
Cdd:TIGR03785 463 EIGDLSRSFAQMVARLR-----------QYTHYLENMSSRlSHELRTPVAVVRSSLENLELQALEQ 517
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
169-303 4.97e-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: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   169 YVIFLSLVVCIIVAIILAWWFSGKLVKPIQQIDTKLKELASQegDLTARLQV-NSNDEIGAIATSFNKMLENLQHIINRV 247
Cdd:TIGR01386 164 KWLILIAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPE--SLDQRLDPsRAPAELRELAQSFNAMLGRLEDAFQRL 241
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30023073   248 QKTSV----EVQTASENMLEKTntsrEATLRVQSSMSNLNASIQSQTSSMEESSTAMDDM 303
Cdd:TIGR01386 242 SQFSAdlahELRTPLTNLLGQT----QVALSQPRTGEEYREVLESNLEELERLSRMVSDM 297
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
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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