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Conserved domains on  [gi|1499838889|gb|RMU58511|]
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Sensory box protein/methyl-accepting chemotaxis protein [Pseudomonas savastanoi pv. glycinea]

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];
262-433 1.26e-48

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 173.67  E-value: 1.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 262 DEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGGIAQQTNLLALNA 341
Cdd:COG0840   305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNA 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 342 AIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAVIVEIQEG 421
Cdd:COG0840   385 AIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEA 464

                         170
                  ....*....|..
gi 1499838889 422 AKQVVGAVGRFA 433
Cdd:COG0840   465 VEEVSDLIQEIA 476
PAS COG2202
PAS domain [Signal transduction mechanisms];
34-263 1.92e-23

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 98.94  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  34 LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQlDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQ 113
Cdd:COG2202    25 IITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 114 PVLDDQGKLVTLQCYGSDITQTVETAA---ENSAFIQALLRST--AVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHS 188
Cdd:COG2202   104 PVRDEDGEITGFVGIARDITERKRAEEalrESEERLRLLVENApdGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLL 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499838889 189 MFCDPAEtsLAPYREFWAMLNRGEFVAGR--FKRIDSSGREVWLEATYNPVHDAQGKLYkVVKFATLVTDQVAREDE 263
Cdd:COG2202   184 DLLHPED--RERLLELLRRLLEGGRESYEleLRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEA 257
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
262-433 1.26e-48

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 173.67  E-value: 1.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 262 DEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGGIAQQTNLLALNA 341
Cdd:COG0840   305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNA 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 342 AIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAVIVEIQEG 421
Cdd:COG0840   385 AIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEA 464

                         170
                  ....*....|..
gi 1499838889 422 AKQVVGAVGRFA 433
Cdd:COG0840   465 VEEVSDLIQEIA 476
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 250-434 2.04e-47

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: 163.61  E-value: 2.04e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  250 FATLVTDQVAREDEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGG 329
Cdd:smart00283  23 LAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDD 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  330 IAQQTNLLALNAAIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLAN 409
Cdd:smart00283 103 IADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE 182

                          170       180
                   ....*....|....*....|....*
gi 1499838889  410 EAGAVIVEIQEGAKQVVGAVGRFAN 434
Cdd:smart00283 183 ETGDALEEIVDSVEEIADLVQEIAA 207
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 255-429 6.55e-44

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: 152.39  E-value: 6.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 255 TDQVAREDEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGGIAQQT 334
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 335 NLLALNAAIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAV 414
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170
                  ....*....|....*
gi 1499838889 415 IVEIQEGAKQVVGAV 429
Cdd:cd11386   161 FEEIVASVEEVADGI 175
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 273-433 5.53e-35

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


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 127.55  E-value: 5.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 273 EISQQTDVSAQRGADVVQNTVQTMRKISeemqsassgiealgKQSLLISSIVQTIGGIAQQTNLLALNAAIEAARAGEQG 352
Cdd:pfam00015   2 DLAQLASEEAQDGGKEVANVVGQMEQIA--------------QSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 353 RGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAVIVEIQEGAKQVVGAVGRF 432
Cdd:pfam00015  68 RGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147


                  .
gi 1499838889 433 A 433
Cdd:pfam00015 148 A 148
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
266-434 3.61e-25

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 108.12  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 266 QAASVAFEISQqtdvSAQRGADVVQNTVQTMRKISEEMQSassgiealgkqsllISSIVQTIGGIAQQTNLLALNAAIEA 345
Cdd:PRK15041  325 QASHLALSASE----TAQRGGKVVDNVVQTMRDISTSSQK--------------IADIISVIDGIAFQTNILALNAAVEA 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 346 ARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQqnqsladeavrgmaNSRTQAEQGLLLANEAGAVIVEIQEGAKQV 425
Cdd:PRK15041  387 ARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIE--------------DSVGKVDVGSTLVESAGETMAEIVSAVTRV 452


                  ....*....
gi 1499838889 426 VGAVGRFAN 434
Cdd:PRK15041  453 TDIMGEIAS 461
PAS COG2202
PAS domain [Signal transduction mechanisms];
34-263 1.92e-23

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 98.94  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  34 LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQlDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQ 113
Cdd:COG2202    25 IITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 114 PVLDDQGKLVTLQCYGSDITQTVETAA---ENSAFIQALLRST--AVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHS 188
Cdd:COG2202   104 PVRDEDGEITGFVGIARDITERKRAEEalrESEERLRLLVENApdGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLL 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499838889 189 MFCDPAEtsLAPYREFWAMLNRGEFVAGR--FKRIDSSGREVWLEATYNPVHDAQGKLYkVVKFATLVTDQVAREDE 263
Cdd:COG2202   184 DLLHPED--RERLLELLRRLLEGGRESYEleLRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEA 257
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-128 1.89e-13

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: 65.82  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  42 IVHANDNFLRALGYSADQLLGKD---LDQMVPSYVKQLdcYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQPVLDD 118
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGeswLDLVHPDDRERV--REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78

                          90
                  ....*....|
gi 1499838889 119 QGKLVTLQCY 128
Cdd:pfam08447  79 NGKPVRVIGV 88
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 34-132 1.17e-12

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: 63.81  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  34 LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYvKQLDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQ 113
Cdd:cd00130     6 IVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPE-DREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....*....
gi 1499838889 114 PVLDDQGKLVTLQCYGSDI 132
Cdd:cd00130    85 PIRDEGGEVIGLLGVVRDI 103
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 36-134 1.37e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 50.54  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  36 LDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQLDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQPV 115
Cdd:PRK11359  152 LDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231

                          90
                  ....*....|....*....
gi 1499838889 116 LDDQGKLVTLQCYGSDITQ 134
Cdd:PRK11359  232 YDVLAHLQNLVMTFSDITE 250
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 16-141 2.84e-06

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: 46.13  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  16 ELSMYRQMQKGMDARMVSLslDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQLDCYRNLKLAVQKGESVIDN 95
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVI--DLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1499838889  96 YRFLHANGSLVWIRAMWQPVLDDQGKLVtLQCYGSDITQTVETAAE 141
Cdd:TIGR00229  79 RRVRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITERKEAEEA 123
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 96-134 2.91e-06

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 43.71  E-value: 2.91e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1499838889   96 YRFLHANGSLVWIRAMWQPVLDDQGKLVTLQCYGSDITQ 134
Cdd:smart00086   4 YRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
262-433 1.26e-48

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 173.67  E-value: 1.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 262 DEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGGIAQQTNLLALNA 341
Cdd:COG0840   305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNA 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 342 AIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAVIVEIQEG 421
Cdd:COG0840   385 AIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEA 464

                         170
                  ....*....|..
gi 1499838889 422 AKQVVGAVGRFA 433
Cdd:COG0840   465 VEEVSDLIQEIA 476
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 250-434 2.04e-47

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: 163.61  E-value: 2.04e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  250 FATLVTDQVAREDEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGG 329
Cdd:smart00283  23 LAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDD 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  330 IAQQTNLLALNAAIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLAN 409
Cdd:smart00283 103 IADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE 182

                          170       180
                   ....*....|....*....|....*
gi 1499838889  410 EAGAVIVEIQEGAKQVVGAVGRFAN 434
Cdd:smart00283 183 ETGDALEEIVDSVEEIADLVQEIAA 207
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 255-429 6.55e-44

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: 152.39  E-value: 6.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 255 TDQVAREDEVSQAASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGGIAQQT 334
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 335 NLLALNAAIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAV 414
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170
                  ....*....|....*
gi 1499838889 415 IVEIQEGAKQVVGAV 429
Cdd:cd11386   161 FEEIVASVEEVADGI 175
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 273-433 5.53e-35

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


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 127.55  E-value: 5.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 273 EISQQTDVSAQRGADVVQNTVQTMRKISeemqsassgiealgKQSLLISSIVQTIGGIAQQTNLLALNAAIEAARAGEQG 352
Cdd:pfam00015   2 DLAQLASEEAQDGGKEVANVVGQMEQIA--------------QSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 353 RGFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAVIVEIQEGAKQVVGAVGRF 432
Cdd:pfam00015  68 RGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147


                  .
gi 1499838889 433 A 433
Cdd:pfam00015 148 A 148
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
266-434 3.61e-25

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 108.12  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 266 QAASVAFEISQqtdvSAQRGADVVQNTVQTMRKISEEMQSassgiealgkqsllISSIVQTIGGIAQQTNLLALNAAIEA 345
Cdd:PRK15041  325 QASHLALSASE----TAQRGGKVVDNVVQTMRDISTSSQK--------------IADIISVIDGIAFQTNILALNAAVEA 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 346 ARAGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQqnqsladeavrgmaNSRTQAEQGLLLANEAGAVIVEIQEGAKQV 425
Cdd:PRK15041  387 ARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIE--------------DSVGKVDVGSTLVESAGETMAEIVSAVTRV 452


                  ....*....
gi 1499838889 426 VGAVGRFAN 434
Cdd:PRK15041  453 TDIMGEIAS 461
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
266-431 1.43e-24

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 105.92  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 266 QAASVA----------FEISQQTDvSAQRGADVVQNTVQTMRKISEEMQSASSGIEALGKQSLLISSIVQTIGGIAQQTN 335
Cdd:PRK09793  294 QAASLAqtaasmeqltATVGQNAD-NARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTN 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 336 LLALNAAIEAARAGEQGRGFAVVADEVRQLAGRTSAATEEI-------VSVVQQNQSLADEAVRGMANSRTQAEQGLLLA 408
Cdd:PRK09793  373 ILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIkglieesVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIM 452

                         170       180
                  ....*....|....*....|...
gi 1499838889 409 NEAGAVIVEIQEGAKQVVGAVGR 431
Cdd:PRK09793  453 GEIASASEEQRRGIEQVAQAVSQ 475
PAS COG2202
PAS domain [Signal transduction mechanisms];
34-263 1.92e-23

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 98.94  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  34 LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQlDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQ 113
Cdd:COG2202    25 IITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 114 PVLDDQGKLVTLQCYGSDITQTVETAA---ENSAFIQALLRST--AVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHS 188
Cdd:COG2202   104 PVRDEDGEITGFVGIARDITERKRAEEalrESEERLRLLVENApdGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLL 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499838889 189 MFCDPAEtsLAPYREFWAMLNRGEFVAGR--FKRIDSSGREVWLEATYNPVHDAQGKLYkVVKFATLVTDQVAREDE 263
Cdd:COG2202   184 DLLHPED--RERLLELLRRLLEGGRESYEleLRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEA 257
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 268-434 1.63e-22

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 100.08  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 268 ASVAFEISQQTDVSAQRGADVVQNTVQTMRKISEemqsassgiealgkQSLLISSIVQTIGGIAQQTNLLALNAAIEAAR 347
Cdd:PRK15048  321 ARQASQLAQSASDTAQHGGKVVDGVVKTMHEIAD--------------SSKKIADIISVIDGIAFQTNILALNAAVEAAR 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 348 AGEQGRGFAVVADEVRQLAGRTSAATEEIVSVVQqnqsladeavrgmaNSRTQAEQGLLLANEAGAVIVEIQEGAKQVVG 427
Cdd:PRK15048  387 AGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE--------------DSVSRVDTGSVLVESAGETMNNIVNAVTRVTD 452


                  ....*..
gi 1499838889 428 AVGRFAN 434
Cdd:PRK15048  453 IMGEIAS 459
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 1-274 1.16e-19

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: 91.19  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889   1 MFNTRLKKELQAQhaeLSMYRQ-MQKGMDArmvSLSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMV-PSYVKQLDC 78
Cdd:COG5809     1 MKSSKMELQLRKS---EQRFRSlFENAPDA---ILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLhPDDEKELRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  79 YRNLKlavQKGESVID-NYRFLHANGSLVWIRAMWQPVLDDQGKLVTLQCYGSDITQTVETAAENSAFiQALLRS----- 152
Cdd:COG5809    75 ILKLL---KEGESRDElEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRES-EEKFRLifnhs 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 153 -TAVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPAETSLApYREFWAMLNRGEFVAGRFKRIDSSGREVWLE 231
Cdd:COG5809   151 pDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENV-AAFISQLLKDGGIAQGEVRFWTKDGRWRLLE 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1499838889 232 ATYNPVHDaQGKLYKVVKFATLVTDQVAREDEVSQ----------AASVAFEI 274
Cdd:COG5809   230 ASGAPIKK-NGEVDGIVIIFRDITERKKLEELLRKseklsvvgelAAGIAHEI 281
PAS COG2202
PAS domain [Signal transduction mechanisms];
134-263 4.28e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.68  E-value: 4.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 134 QTVETAAENSAFIQALLRST--AVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPaETSLAPYREFWAMLNRG 211
Cdd:COG2202     1 TAEEALEESERRLRALVESSpdAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP-EDDDEFLELLRAALAGG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1499838889 212 EFVAGRFKRIDSSGREVWLEATYNPVHDAQGKLYKVVKFATLVTDQVAREDE 263
Cdd:COG2202    80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEA 131
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-128 1.89e-13

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: 65.82  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  42 IVHANDNFLRALGYSADQLLGKD---LDQMVPSYVKQLdcYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQPVLDD 118
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGeswLDLVHPDDRERV--REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDE 78

                          90
                  ....*....|
gi 1499838889 119 QGKLVTLQCY 128
Cdd:pfam08447  79 NGKPVRVIGV 88
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 164-251 7.88e-13

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: 63.90  E-value: 7.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 164 VLTANDQFLRGMGYNLAQIKGK--HHSMFCDPAETSLApYREFWAMLNRGEFVAGRFKRIDSSGREVWLEATYNPVHDAQ 241
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERV-REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 1499838889 242 GKLYKVVKFA 251
Cdd:pfam08447  80 GKPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 34-132 1.17e-12

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: 63.81  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  34 LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYvKQLDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQ 113
Cdd:cd00130     6 IVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPE-DREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....*....
gi 1499838889 114 PVLDDQGKLVTLQCYGSDI 132
Cdd:cd00130    85 PIRDEGGEVIGLLGVVRDI 103
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 39-134 2.09e-11

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: 60.17  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  39 NNHIVHANDNFLRALGYSADQLLGKDLDQMVPSyvkqLDCYRNLKLAVQKGESVID-NYRFLHANGSLVWIRAMWQPVLD 117
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAE----PEDSERLREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIRD 76

                          90
                  ....*....|....*..
gi 1499838889 118 DQGKLVTLQCYGSDITQ 134
Cdd:pfam13426  77 DGGELVGIIAILRDITE 93
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
34-141 1.88e-09

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 59.09  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  34 LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPsyvKQLDCYRNLKLAVQKGESVIDN-YRFLHANGSLVWIRAMW 112
Cdd:COG3852    21 IVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP---EDSPLRELLERALAEGQPVTEReVTLRRKDGEERPVDVSV 97

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1499838889 113 QPVLDDQGK---LVTLQcygsDITQTVETAAE 141
Cdd:COG3852    98 SPLRDAEGEggvLLVLR----DITERKRLERE 125
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 162-256 7.35e-09

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: 52.85  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 162 GHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPAETSLAPYRefwAMLNRGEFVAGRFKRIDSSGREVWLEATYNPVHDAQ 241
Cdd:pfam13426   2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLRE---ALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|....*
gi 1499838889 242 GKLYKVVKFATLVTD 256
Cdd:pfam13426  79 GELVGIIAILRDITE 93
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 36-137 1.59e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. 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: 52.42  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  36 LDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPsyvkqLDCYRNLKLAVQK---GESVIDNYRFLHANGSLVWIRAMW 112
Cdd:pfam08448  11 LDPDGRVRYANAAAAELFGLPPEELLGKTLAELLP-----PEDAARLERALRRaleGEEPIDFLEELLLNGEERHYELRL 85

                          90       100
                  ....*....|....*....|....*
gi 1499838889 113 QPVLDDQGKLVTLQCYGSDITQTVE 137
Cdd:pfam08448  86 TPLRDPDGEVIGVLVISRDITERRR 110
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 19-132 4.38e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. 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: 51.26  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  19 MYRQMQKGMDARMvsLSLDANNHIVHANDNFLRALGYSADQLLGKDL-DQMV-PSYVKQLDCYRnlKLAVQKGESVIDNY 96
Cdd:pfam00989   2 DLRAILESLPDGI--FVVDEDGRILYVNAAAEELLGLSREEVIGKSLlDLIPeEDDAEVAELLR--QALLQGEESRGFEV 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1499838889  97 RFLHANGSLVWIRAMWQPVLDDQGKLVTLQCYGSDI 132
Cdd:pfam00989  78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 154-259 1.66e-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. 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: 49.33  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 154 AVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKH-HSMFcdpAETSLAPYREFWAMLNRGEFVAGRFKRIDSSGREVWLEA 232
Cdd:pfam08448   7 ALAVLDPDGRVRYANAAAAELFGLPPEELLGKTlAELL---PPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYEL 83

                          90       100
                  ....*....|....*....|....*..
gi 1499838889 233 TYNPVHDAQGKLYKVVKFATLVTDQVA 259
Cdd:pfam08448  84 RLTPLRDPDGEVIGVLVISRDITERRR 110
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 36-134 1.37e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 50.54  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  36 LDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQLDCYRNLKLAVQKGESVIDNYRFLHANGSLVWIRAMWQPV 115
Cdd:PRK11359  152 LDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231

                          90
                  ....*....|....*....
gi 1499838889 116 LDDQGKLVTLQCYGSDITQ 134
Cdd:PRK11359  232 YDVLAHLQNLVMTFSDITE 250
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
140-274 1.44e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.84  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 140 AENSAFIQALLRS--TAVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPAETSLAPYREfwAMLNRGEFVAGR 217
Cdd:COG3852     3 RESEELLRAILDSlpDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLER--ALAEGQPVTERE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499838889 218 FKRIDSSGREVWLEATYNPVHDAQGKLYkVVKFATLVTDQVAREDEVSQ----------AASVAFEI 274
Cdd:COG3852    81 VTLRRKDGEERPVDVSVSPLRDAEGEGG-VLLVLRDITERKRLERELRRaeklaavgelAAGLAHEI 146
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 152-252 1.76e-06

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: 46.47  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 152 STAVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPAEtSLAPYREFWAMLNRGEFVAGRFKRIDSSGREVWLE 231
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|.
gi 1499838889 232 ATYNPVHDAQGKLYKVVKFAT 252
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVR 101
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 16-141 2.84e-06

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: 46.13  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  16 ELSMYRQMQKGMDARMVSLslDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQLDCYRNLKLAVQKGESVIDN 95
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVI--DLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1499838889  96 YRFLHANGSLVWIRAMWQPVLDDQGKLVtLQCYGSDITQTVETAAE 141
Cdd:TIGR00229  79 RRVRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITERKEAEEA 123
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 96-134 2.91e-06

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 43.71  E-value: 2.91e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1499838889   96 YRFLHANGSLVWIRAMWQPVLDDQGKLVTLQCYGSDITQ 134
Cdd:smart00086   4 YRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 148-256 1.04e-05

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: 44.59  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 148 ALLRSTAV--IEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPaetslaPYRE-----FWAML-NRGEFVAGRFK 219
Cdd:TIGR00229   7 AIFESSPDaiIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPE------EDREevrerIERRLeGEPEPVSEERR 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1499838889 220 RIDSSGREVWLEATYNPVHDAQGKLYkVVKFATLVTD 256
Cdd:TIGR00229  81 VRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITE 116
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 18-70 3.83e-05

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: 41.62  E-value: 3.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1499838889   18 SMYRQMQKGMDarMVSLSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVP 70
Cdd:smart00091   1 ERLRAILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIH 51
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 2-144 7.97e-05

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 44.57  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889   2 FNtRLKKELQAQHAELSMYRQMQKGMDARMVS--LSLDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVKQLDCY 79
Cdd:COG5000    71 FN-RMTDQLKEQREELEERRRYLETILENLPAgvIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLR 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499838889  80 RNLKLAVQKGESV-IDNYRFLHANGSlvwiramwqpVLDDQGKLVTLQcygsDITQTVEtAAENSA 144
Cdd:COG5000   150 EALERGWQEEIELtRDGRRTLLVRAS----------PLRDDGYVIVFD----DITELLR-AERLAA 200
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 36-141 9.85e-05

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: 44.38  E-value: 9.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  36 LDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYVkqldcyrnLKLAVQKGESVIDnyRFLHANGSLVWIRAMWQPV 115
Cdd:COG3829    27 VDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSP--------LLEVLKTGKPVTG--VIQKTGGKGKTVIVTAIPI 96

                          90       100
                  ....*....|....*....|....*.
gi 1499838889 116 LDDqGKLVTLQCYGSDITQTVETAAE 141
Cdd:COG3829    97 FED-GEVIGAVETFRDITELKRLERK 121
PRK13557 PRK13557
histidine kinase; Provisional
 30-123 6.66e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 41.97  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  30 RMVSLSLDAN---NHIVHANDNFLRALGYSADQLLGK--------DLDQMVPSYVKQLDCYRNlKLAVQkgesvIDNYRf 98
Cdd:PRK13557   40 RMPMIVTDPNqpdNPIVFANRAFLEMTGYAAEEIIGNncrflqgpETDRATVAEVRDAIAERR-EIATE-----ILNYR- 112

                          90       100
                  ....*....|....*....|....*
gi 1499838889  99 lhANGSLVWIRAMWQPVLDDQGKLV 123
Cdd:PRK13557  113 --KDGSSFWNALFVSPVYNDAGDLV 135
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
194-435 7.63e-04

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 41.93  E-value: 7.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 194 AETSLAPYREFWAMLNRGEFVAGRFKRIDSSGREVWLEATYNPVHDAQGKLYKVVKFATLVTDQVAREDEVSQAASVAFE 273
Cdd:COG0840   108 ALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 274 ISQQTDVSAQRGADVVQNTVQTMRKISEEMQSASSG-----IEALGKQSL---------LISSIVQTIGGIAQQTNLLAL 339
Cdd:COG0840   188 LLALVALAIILALLLSRSITRPLRELLEVLERIAEGdltvrIDVDSKDEIgqladafnrMIENLRELVGQVRESAEQVAS 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 340 NAAIEAARAGEQGRGFAVVADEVRQlagrTSAATEEIVSVVQQNQSLADEAVRGMANSRTQAEQGLLLANEAGAVIVEIQ 419
Cdd:COG0840   268 ASEELAASAEELAAGAEEQAASLEE----TAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIR 343

                         250
                  ....*....|....*.
gi 1499838889 420 EGAKQVVGAVGRFANQ 435
Cdd:COG0840   344 ESVEETAETIEELGES 359
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
154-274 2.24e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 40.34  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 154 AVIEFDLGGHVLTANDQFLRGMGYNLAQIKGKHHSMFCDPAETSLAPYREFWAmlnRGEFVAGRFKRIDSSGREVWLEAT 233
Cdd:PRK11360  274 GVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLDTLE---HGTEHVDLEISFPGRDRTIELSVS 350

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1499838889 234 YNPVHDAQGKLYKVVKFATLVTDQVAREDEVSQA----------ASVAFEI 274
Cdd:PRK11360  351 TSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQerlaalgelvAGVAHEI 401
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
262-389 2.83e-03

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 40.00  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 262 DEV----SQAASVAFEISQQTDVSAQRgadvVQNTVQTMRKISEEMQSASSGIEALGKQsllISSIVQTIGGIAQQTNLL 337
Cdd:COG0840   403 DEVrklaERSAEATKEIEELIEEIQSE----TEEAVEAMEEGSEEVEEGVELVEEAGEA---LEEIVEAVEEVSDLIQEI 475

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1499838889 338 AlNAAIEAARAGEQgrgFAVVADEVRQLAGRTSAATEEIVSVVQQNQSLADE 389
Cdd:COG0840   476 A-AASEEQSAGTEE---VNQAIEQIAAAAQENAASVEEVAAAAEELAELAEE 523
PRK13560 PRK13560
hypothetical protein; Provisional
 36-267 9.57e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 38.50  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889  36 LDANNHIVHANDNFLRALGYSADQLLGKDLDQMVPSYvkQLDCYRNLKLAVQK--GESVIDNYrFLHANGSLVWIRAMWQ 113
Cdd:PRK13560  220 KDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQ--PADDYQEADAAKFDadGSQIIEAE-FQNKDGRTRPVDVIFN 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 114 PV--LDDQGKLVTLQCYGSDI-----TQTVETAAEN--SAFIQALlrSTAVIEFDLGGHVLTANDQFL-RGMGYNLAQIK 183
Cdd:PRK13560  297 HAefDDKENHCAGLVGAITDIsgrraAERELLEKEDmlRAIIEAA--PIAAIGLDADGNICFVNNNAAeRMLGWSAAEVM 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499838889 184 GKHHSMFcDP---AETSLAPYREFWAMLNRGEFVAGRFKRIDSSGR-----EVWLE----------ATYNPVHDAQGKLY 245
Cdd:PRK13560  375 GKPLPGM-DPelnEEFWCGDFQEWYPDGRPMAFDACPMAKTIKGGKifdgqEVLIEreddgpadcsAYAEPLHDADGNII 453

                         250       260
                  ....*....|....*....|..
gi 1499838889 246 KVVKFATLVTDQVAREDEVSQA 267
Cdd:PRK13560  454 GAIALLVDITERKQVEEQLLLA 475
 
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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