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Conserved domains on  [gi|489829360|ref|WP_003733114|]
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methyl-accepting chemotaxis protein [Listeria monocytogenes]

Protein Classification

PAS and Tar domain-containing protein( domain architecture ID 11451354)

PAS and Tar domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
114-286 1.16e-33

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 128.98  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 114 VAKIATDITRREETVHDFASGLKSMATNLKEHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTING 193
Cdd:COG0840  293 TAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDD 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 194 IASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINTISSGTERVEAKVEESQEVLI 273
Cdd:COG0840  373 IAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVE 452

                        170
                 ....*....|...
gi 489829360 274 LSLEDFSQIESAS 286
Cdd:COG0840  453 EAGEALEEIVEAV 465
PAS COG2202
PAS domain [Signal transduction mechanisms];
5-127 5.52e-14

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 70.44  E-value: 5.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   5 AETEDATLLLDGLLQN--VAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQSAsYKAMWTNLLAGQKF 82
Cdd:COG2202    4 EALEESERRLRALVESspDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEF-LELLRAALAGGGVW 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489829360  83 QNKIERKNARGERVWFEATYIPIIRED-TVVGVAKIATDITRREET 127
Cdd:COG2202   83 RGELRNRRKDGSLFWVELSISPVRDEDgEITGFVGIARDITERKRA 128
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
114-286 1.16e-33

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 128.98  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 114 VAKIATDITRREETVHDFASGLKSMATNLKEHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTING 193
Cdd:COG0840  293 TAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDD 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 194 IASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINTISSGTERVEAKVEESQEVLI 273
Cdd:COG0840  373 IAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVE 452

                        170
                 ....*....|...
gi 489829360 274 LSLEDFSQIESAS 286
Cdd:COG0840  453 EAGEALEEIVEAV 465
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 132-295 5.45e-33

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 [Multi-domain]  Cd Length: 200  Bit Score: 120.03  E-value: 5.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 132 ASGLKSMATNLKEHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTINGIASQTNLLALNAAIEAAR 211
Cdd:cd11386   14 ADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 212 AGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINT-----------ISSGTERVEAKVEESQEVLILSLEDFS 280
Cdd:cd11386   94 AGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEaveameetseeVEEGVELVEETGRAFEEIVASVEEVAD 173

                        170
                 ....*....|....*
gi 489829360 281 QIESASTALDQNAGA 295
Cdd:cd11386  174 GIQEISAATQEQSAS 188
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 117-291 1.08e-30

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: 115.85  E-value: 1.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   117 IATDITRREETVHDFASGLKSMATNLK---EHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTING 193
Cdd:smart00283  23 LAERMEELSASIEEVAANADEIAATAQsaaEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDD 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   194 IASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINTISSGTERVEAKVEESQEVLI 273
Cdd:smart00283 103 IADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE 182

                          170
                   ....*....|....*...
gi 489829360   274 LSLEDFSQIESASTALDQ 291
Cdd:smart00283 183 ETGDALEEIVDSVEEIAD 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 165-287 2.76e-27

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: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 104.44  E-value: 2.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  165 KESNENTDTLHDLQTEAQNIHGIINTINGIASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSV 244
Cdd:pfam00015  16 KEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALI 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489829360  245 NGITQEINTISSGTERVEAKVEESQEVLILSLEDFSQIESAST 287
Cdd:pfam00015  96 IEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVA 138
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
171-299 9.33e-21

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 92.06  E-value: 9.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 171 TDTLHDLQTEAQNIHGIINTINGIASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKE----VEKSVNG 246
Cdd:PRK09793 344 THTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEikglIEESVNR 423

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489829360 247 ITQEINTISSGTERVEAKVEESQEVLILSLEDFSQIESASTALDQNAGAFTKM 299
Cdd:PRK09793 424 VQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQM 476
PAS COG2202
PAS domain [Signal transduction mechanisms];
5-127 5.52e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 70.44  E-value: 5.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   5 AETEDATLLLDGLLQN--VAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQSAsYKAMWTNLLAGQKF 82
Cdd:COG2202    4 EALEESERRLRALVESspDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEF-LELLRAALAGGGVW 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489829360  83 QNKIERKNARGERVWFEATYIPIIRED-TVVGVAKIATDITRREET 127
Cdd:COG2202   83 RGELRNRRKDGSLFWVELSISPVRDEDgEITGFVGIARDITERKRA 128
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 20-126 3.02e-12

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 62.05  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLcFPDFVQSAsYKAMWTNLLAGQKFQNKIERKNARGERVWFE 99
Cdd:pfam08448   5 PDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAAR-LERALRRALEGEEPIDFLEELLLNGEERHYE 82

                          90       100
                  ....*....|....*....|....*...
gi 489829360  100 ATYIPIIRED-TVVGVAKIATDITRREE 126
Cdd:pfam08448  83 LRLTPLRDPDgEVIGVLVISRDITERRR 110
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 20-127 3.25e-10

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 56.92  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQsaSYKAMWTNLLAGQKFQNKIER--KNARGERVW 97
Cdd:TIGR00229  13 PDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE--EVRERIERRLEGEPEPVSEERrvRRKDGSEIW 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 489829360   98 FEATYIPIIREDTVVGVAKIATDITRREET 127
Cdd:TIGR00229  91 VEVSVSPIRTNGGELGVVGIVRDITERKEA 120
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 20-121 2.83e-08

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 50.71  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQsaSYKAMWTNLLAGQKFQNK-IERKNARGERVWF 98
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE--ELRERLENLLSGGEPVTLeVRLRRKDGSVIWV 79

                         90       100
                 ....*....|....*....|....
gi 489829360  99 EATYIPIIREDT-VVGVAKIATDI 121
Cdd:cd00130   80 LVSLTPIRDEGGeVIGLLGVVRDI 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 20-65 6.51e-03

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 34.68  E-value: 6.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 489829360    20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQ 65
Cdd:smart00091  11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRE 56
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
114-286 1.16e-33

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 128.98  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 114 VAKIATDITRREETVHDFASGLKSMATNLKEHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTING 193
Cdd:COG0840  293 TAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDD 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 194 IASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINTISSGTERVEAKVEESQEVLI 273
Cdd:COG0840  373 IAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVE 452

                        170
                 ....*....|...
gi 489829360 274 LSLEDFSQIESAS 286
Cdd:COG0840  453 EAGEALEEIVEAV 465
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 132-295 5.45e-33

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 [Multi-domain]  Cd Length: 200  Bit Score: 120.03  E-value: 5.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 132 ASGLKSMATNLKEHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTINGIASQTNLLALNAAIEAAR 211
Cdd:cd11386   14 ADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 212 AGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINT-----------ISSGTERVEAKVEESQEVLILSLEDFS 280
Cdd:cd11386   94 AGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEaveameetseeVEEGVELVEETGRAFEEIVASVEEVAD 173

                        170
                 ....*....|....*
gi 489829360 281 QIESASTALDQNAGA 295
Cdd:cd11386  174 GIQEISAATQEQSAS 188
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 117-291 1.08e-30

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: 115.85  E-value: 1.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   117 IATDITRREETVHDFASGLKSMATNLK---EHSSVGKTRSEALLELVKSITKESNENTDTLHDLQTEAQNIHGIINTING 193
Cdd:smart00283  23 LAERMEELSASIEEVAANADEIAATAQsaaEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDD 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   194 IASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINTISSGTERVEAKVEESQEVLI 273
Cdd:smart00283 103 IADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE 182

                          170
                   ....*....|....*...
gi 489829360   274 LSLEDFSQIESASTALDQ 291
Cdd:smart00283 183 ETGDALEEIVDSVEEIAD 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 165-287 2.76e-27

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: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 104.44  E-value: 2.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  165 KESNENTDTLHDLQTEAQNIHGIINTINGIASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSV 244
Cdd:pfam00015  16 KEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALI 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489829360  245 NGITQEINTISSGTERVEAKVEESQEVLILSLEDFSQIESAST 287
Cdd:pfam00015  96 IEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVA 138
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
171-299 9.33e-21

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 92.06  E-value: 9.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 171 TDTLHDLQTEAQNIHGIINTINGIASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKE----VEKSVNG 246
Cdd:PRK09793 344 THTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEikglIEESVNR 423

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489829360 247 ITQEINTISSGTERVEAKVEESQEVLILSLEDFSQIESASTALDQNAGAFTKM 299
Cdd:PRK09793 424 VQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQM 476
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 113-299 1.03e-20

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 91.99  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 113 GVAKIA---TDITRR--------EET---VHDFASGLKSMATNLKEHSSVGKTRSEALL---ELVKSITKesnentdTLH 175
Cdd:PRK15048 278 GTREIAagnTDLSSRteqqasalEETaasMEQLTATVKQNADNARQASQLAQSASDTAQhggKVVDGVVK-------TMH 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 176 DLQTEAQNIHGIINTINGIASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVEKSVNGITQEINT-- 253
Cdd:PRK15048 351 EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTgs 430

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489829360 254 --ISSGTERVEAKVEESQEVLILSLEDFSQIESASTALDQNAGAFTKM 299
Cdd:PRK15048 431 vlVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEM 478
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
113-272 7.40e-20

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 89.63  E-value: 7.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 113 GVAKIAT---DITRREE----TVHDFASGLKSMATNLKEHSSVGKTRSEALL---ELVKSITKESNENTDTLHDLQTEAQ 182
Cdd:PRK15041 280 GASEIATgnnDLSSRTEqqaaSLEETAASMEQLTATVKQNAENARQASHLALsasETAQRGGKVVDNVVQTMRDISTSSQ 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360 183 NIHGIINTINGIASQTNLLALNAAIEAARAGDAGRGFSVVAEEVRKLSSRVEEAIKEVeKSVngITQEINTISSGTERVE 262
Cdd:PRK15041 360 KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREI-KSL--IEDSVGKVDVGSTLVE 436

                        170
                 ....*....|
gi 489829360 263 AKVEESQEVL 272
Cdd:PRK15041 437 SAGETMAEIV 446
PAS COG2202
PAS domain [Signal transduction mechanisms];
5-127 5.52e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 70.44  E-value: 5.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   5 AETEDATLLLDGLLQN--VAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQSAsYKAMWTNLLAGQKF 82
Cdd:COG2202    4 EALEESERRLRALVESspDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEF-LELLRAALAGGGVW 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489829360  83 QNKIERKNARGERVWFEATYIPIIRED-TVVGVAKIATDITRREET 127
Cdd:COG2202   83 RGELRNRRKDGSLFWVELSISPVRDEDgEITGFVGIARDITERKRA 128
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 20-126 3.02e-12

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 62.05  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLcFPDFVQSAsYKAMWTNLLAGQKFQNKIERKNARGERVWFE 99
Cdd:pfam08448   5 PDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAAR-LERALRRALEGEEPIDFLEELLLNGEERHYE 82

                          90       100
                  ....*....|....*....|....*...
gi 489829360  100 ATYIPIIRED-TVVGVAKIATDITRREE 126
Cdd:pfam08448  83 LRLTPLRDPDgEVIGVLVISRDITERRR 110
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 20-127 3.25e-10

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 56.92  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQsaSYKAMWTNLLAGQKFQNKIER--KNARGERVW 97
Cdd:TIGR00229  13 PDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE--EVRERIERRLEGEPEPVSEERrvRRKDGSEIW 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 489829360   98 FEATYIPIIREDTVVGVAKIATDITRREET 127
Cdd:TIGR00229  91 VEVSVSPIRTNGGELGVVGIVRDITERKEA 120
PAS COG2202
PAS domain [Signal transduction mechanisms];
20-127 6.38e-10

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 58.50  E-value: 6.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQSAsyKAMWTNLLAG--QKFQNKIERKNARGERVW 97
Cdd:COG2202  147 PDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERL--LELLRRLLEGgrESYELELRLKDGDGRWVW 224

                         90       100       110
                 ....*....|....*....|....*....|
gi 489829360  98 FEATYIPIIREDTVVGVAKIATDITRREET 127
Cdd:COG2202  225 VEASAVPLRDGGEVIGVLGIVRDITERKRA 254
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
3-126 2.67e-08

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 54.47  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   3 VNAETEDATLLLDGLlqNVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDfvqSASYKAMWTNLLAGQKF 82
Cdd:COG3852    2 LRESEELLRAILDSL--PDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED---SPLRELLERALAEGQPV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489829360  83 -QNKIERKNARGERVWFEATYIPIIREDTVVGVAKIATDITRREE 126
Cdd:COG3852   77 tEREVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKR 121
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 20-121 2.83e-08

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 50.71  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQsaSYKAMWTNLLAGQKFQNK-IERKNARGERVWF 98
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE--ELRERLENLLSGGEPVTLeVRLRRKDGSVIWV 79

                         90       100
                 ....*....|....*....|....
gi 489829360  99 EATYIPIIREDT-VVGVAKIATDI 121
Cdd:cd00130   80 LVSLTPIRDEGGeVIGLLGVVRDI 103
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 31-122 4.61e-08

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 49.77  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   31 KVTYANALFAEAMGYSEEEMLKLSHPDLcFPDFVQSASYKAMWTNLLAGQKFQNKIERKNarGERVWFEATYIPIIRED- 109
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDL-FAEPEDSERLREALREGKAVREFEVVLYRKD--GEPFPVLVSLAPIRDDGg 79

                          90
                  ....*....|...
gi 489829360  110 TVVGVAKIATDIT 122
Cdd:pfam13426  80 ELVGIIAILRDIT 92
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 22-127 1.20e-07

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 52.67  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  22 AIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLcFPDFVQSASYKAMWTNLLAGQKFQNKIERKNARGERVWFEAT 101
Cdd:COG5809  153 GIIVTDLDGRIIYANPAACKLLGISIEELIGKSILEL-IHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEAS 231

                         90       100
                 ....*....|....*....|....*.
gi 489829360 102 YIPIIREDTVVGVAKIATDITRREET 127
Cdd:COG5809  232 GAPIKKNGEVDGIVIIFRDITERKKL 257
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 32-115 3.08e-07

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 47.33  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   32 VTYANALFAEAMGYSEEEMLKLSHP--DLCFPDfVQSASYKAMWTNLLAGQKFQNKIERKNARGERVWFEATYIPIIRED 109
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESwlDLVHPD-DRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 489829360  110 T----VVGVA 115
Cdd:pfam08447  80 GkpvrVIGVA 89
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 6-165 8.59e-06

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 46.69  E-value: 8.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   6 ETEDATLLLDGLLQNV--AIIRFDTNKKVTYANALFAEAMGYSEEEMLKLShpdlCFPDFVQSASYKAmwtnLLAGQKFQ 83
Cdd:COG3829    5 ELKELEEELEAILDSLddGIIVVDADGRITYVNRAAERILGLPREEVIGKN----VTELIPNSPLLEV----LKTGKPVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360  84 NKIERKNARGERVwfEATYIPIIREDTVVGVAKIATDITRREETVHDFASGLKSMATNLKEHSSVGKTRSEALLELVKSI 163
Cdd:COG3829   77 GVIQKTGGKGKTV--IVTAIPIFEDGEVIGAVETFRDITELKRLERKLREEELERGLSAKYTFDDIIGKSPAMKELLELA 154


                 ..
gi 489829360 164 TK 165
Cdd:COG3829  155 KR 156
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 13-121 1.56e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 43.17  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   13 LLDGLLQN--VAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDfVQSASYKAMWTNLLAGQKFQN-KIERK 89
Cdd:pfam00989   2 DLRAILESlpDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEE-DDAEVAELLRQALLQGEESRGfEVSFR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489829360   90 NARGERVWFEATYIPII-REDTVVGVAKIATDI 121
Cdd:pfam00989  81 VPDGRPRHVEVRASPVRdAGGEILGFLGVLRDI 113
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 7-126 2.48e-04

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 42.41  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829360   7 TEDATLLLDGLlqNVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFvqSASYKAMWTNLLAGQKFQNKI 86
Cdd:COG5805   33 TEELETILENL--PDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEY--HYRVKTRIERLQKGYDVVMIE 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489829360  87 ERKNARGERVWFEATYIPIIREDTVVGVAKIaTDITRREE 126
Cdd:COG5805  109 QIYCKDGELIYVEVKLFPIYNQNGQAAILAL-RDITKKKK 147
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 20-65 6.51e-03

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 34.68  E-value: 6.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 489829360    20 NVAIIRFDTNKKVTYANALFAEAMGYSEEEMLKLSHPDLCFPDFVQ 65
Cdd:smart00091  11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRE 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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