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Conserved domains on  [gi|2495942583|ref|WP_280109754|]
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MULTISPECIES: PAS domain S-box protein [Methylobacterium]

Protein Classification

PAS domain-containing methyl-accepting chemotaxis protein; sensor domain-containing diguanylate cyclase( domain architecture ID 13492224)

PAS domain-containing methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior| sensor domain-containing diguanylate cyclase containing PAS sensor domain(s), catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13559 super family cl36265
hypothetical protein; Provisional
 6-465 1.03e-69

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK13559:

Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 225.85  E-value: 1.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNR 85
Cdd:PRK13559   45 FEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  86 RKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTlekerlvilqrdrdaleaesarrsleliqseerlrftlkagrlgaw 165
Cdd:PRK13559  125 RKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVT---------------------------------------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 166 tldlgvmrlissdglrenlgrsphaplsyeemiaaihpddrhrklaardaaiaghsdydiEIRiitprgEIRwlqfrgra 245
Cdd:PRK13559  159 ------------------------------------------------------------DIR------AVR-------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 246 syradgtplsiagislditdRKRAEEHRdlLAGELNHRIQNTLATVQSIARQTLRGAASLEEAQvAMESRLQSLSAATEM 325
Cdd:PRK13559  165 --------------------ALEAHERR--LAREVDHRSKNVFAVVDSIVRLTGRADDPSLYAA-AIQERVQALARAHET 221

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 326 LArGSGDWAT--LTEVVIAALHPFGVEQDqRFKIGGPILRLAPRIALAFALAIHELATNSVKYGSLSVDDGRVIVSWDvv 403
Cdd:PRK13559  222 LL-DERGWETveVEELIRAQVAPYAPRAT-RVAFEGPGIRLGAASVQPLGLVLHELAVNAIKHGALSADQGRISISWK-- 297

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495942583 404 DGSSPDRLWFQWQEVGGPRVSRPTRTGFGSRMIERALAQEIGGTAEIDYRPRGVVFTAEAPL 465
Cdd:PRK13559  298 PSPEGAGFRIDWQEQGGPTPPKLAKRGFGTVIIGAMVESQLNGQLEKTWSDDGLLARIEIPS 359
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 177-259 4.52e-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: 64.67  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 177 SDGLRENLGRSPHAPLS-YEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLS 255
Cdd:pfam08447   5 SPRFEEILGYTPEELLGkGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKPVR 84


                  ....
gi 2495942583 256 IAGI 259
Cdd:pfam08447  85 VIGV 88
 
Name Accession Description Interval E-value
PRK13559 PRK13559
hypothetical protein; Provisional
 6-465 1.03e-69

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 225.85  E-value: 1.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNR 85
Cdd:PRK13559   45 FEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  86 RKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTlekerlvilqrdrdaleaesarrsleliqseerlrftlkagrlgaw 165
Cdd:PRK13559  125 RKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVT---------------------------------------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 166 tldlgvmrlissdglrenlgrsphaplsyeemiaaihpddrhrklaardaaiaghsdydiEIRiitprgEIRwlqfrgra 245
Cdd:PRK13559  159 ------------------------------------------------------------DIR------AVR-------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 246 syradgtplsiagislditdRKRAEEHRdlLAGELNHRIQNTLATVQSIARQTLRGAASLEEAQvAMESRLQSLSAATEM 325
Cdd:PRK13559  165 --------------------ALEAHERR--LAREVDHRSKNVFAVVDSIVRLTGRADDPSLYAA-AIQERVQALARAHET 221

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 326 LArGSGDWAT--LTEVVIAALHPFGVEQDqRFKIGGPILRLAPRIALAFALAIHELATNSVKYGSLSVDDGRVIVSWDvv 403
Cdd:PRK13559  222 LL-DERGWETveVEELIRAQVAPYAPRAT-RVAFEGPGIRLGAASVQPLGLVLHELAVNAIKHGALSADQGRISISWK-- 297

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495942583 404 DGSSPDRLWFQWQEVGGPRVSRPTRTGFGSRMIERALAQEIGGTAEIDYRPRGVVFTAEAPL 465
Cdd:PRK13559  298 PSPEGAGFRIDWQEQGGPTPPKLAKRGFGTVIIGAMVESQLNGQLEKTWSDDGLLARIEIPS 359
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 7-470 1.99e-46

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 168.16  E-value: 1.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   7 AAAVRATRMPMVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNRR 86
Cdd:COG3920    24 LLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  87 KDGTVFWNRLLVSPVFASDGELTYFFASQYDVTLEKERLVILQRDRDALEAESARRSLELIQSEERLRFTLKAGRLGAWT 166
Cdd:COG3920   104 LAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 167 LDLGVMRLISSDGLRENLGRSPHAPLSYEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRAS 246
Cdd:COG3920   184 LLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLL 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 247 YRADGtpLSIAGISLDITDRKRAE-------EHRDLLAGELNHRIQNTLATVQSIARQTLRGAASLE--EAQVAMESRLQ 317
Cdd:COG3920   264 LRALL--LLAAGIRLVITERKRAEeeleaslEEKELLLRELHHRVKNNLQVVSSLLRLQARRADDPEarEALEESQNRIQ 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 318 SLSAATEMLARgSGDWAT-----LTEVVIAALHPFGVEQDQRFKIGGPILRLAPRIALAFALAIHELATNSVKYGSLSVD 392
Cdd:COG3920   342 ALALVHELLYQ-SEDWEGvdlrdYLRELLEPLRDSYGGRGIRIELDGPDVELPADAAVPLGLILNELVTNALKHAFLSGE 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 393 DGRVIVSWDVVDgsspDRLWFQWQEVGG---PRVSRPTRTGFGSRMIeRALAQEIGGTAEIDyRPRGVVFTAEAPLPEIT 469
Cdd:COG3920   421 GGRIRVSWRRED----GRLRLTVSDNGVglpEDVDPPARKGLGLRLI-RALVRQLGGTLELD-RPEGTRVRITFPLAELA 494


                  .
gi 2495942583 470 R 470
Cdd:COG3920   495 A 495
HWE_HK pfam07536
HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate ...
 279-360 7.92e-27

HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate response regulator protein, represent the best-known apparatus for transducing external cues into a physiological response in bacteria. The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as pfam00512 and pfam07568. The family was defined by the presence of a highly conserved H residue in the kinase domain and a WxE motif in a C-terminal ATPase domain that is related to pfam02518. It has been demonstrated to show structural and functional correlation with pfam07568. These proteins are found in a variety of alpha- and gamma- proteobacteria, with significant enrichment in the rhizobia.


Pssm-ID: 429521 [Multi-domain]  Cd Length: 83  Bit Score: 103.11  E-value: 7.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 279 ELNHRIQNTLATVQSIARQTLRGAASLEEAQVAMESRLQSLSAATEMLARGSGDWATLTEVVIAALHPFGVEQDQRFKIG 358
Cdd:pfam07536   1 ELNHRVKNTLATVQSIARQTLRNAASLDEFVEAFEGRLQALSRAHDLLSRASWAGADLSELLEAELAPYGGEAGTRITLS 80


                  ..
gi 2495942583 359 GP 360
Cdd:pfam07536  81 GP 82
HWE_HK smart00911
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, ...
 279-360 3.92e-21

HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as. In. the HWE family was defined by the presence of conserved a H residue and a WXE motifs and was limited to members of the proteobacteria. However, many homologues of this domain are lack the WXE motif. Furthermore, homologues are found in a wide range of Gram-positive and Gram-negative bacteria as well as in several archaea.


Pssm-ID: 214907 [Multi-domain]  Cd Length: 84  Bit Score: 87.26  E-value: 3.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  279 ELNHRIQNTLATVQSIARQTLRGAASLEEAQVAMESRLQSLSAATEMLARGSGDWATLTEVVIAALHPFGVEQDQ-RFKI 357
Cdd:smart00911   1 ELNHRVKNLLAVVQAIARQTLRSASSLEDFAEAFEGRLQALARAHDLLSRSDWSGADLRDLVRAELAPYGGPGDGeRITL 80


                   ...
gi 2495942583  358 GGP 360
Cdd:smart00911  81 SGP 83
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 6-123 1.16e-13

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: 67.32  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIE-RRVTIEIDLKN 84
Cdd:TIGR00229   5 YRAIFESSPDAIIVIDL---EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEgEPEPVSEERRV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2495942583  85 RRKDGTVFWNRLLVSPVFAsDGELTYFFASQYDVTLEKE 123
Cdd:TIGR00229  82 RRKDGSEIWVEVSVSPIRT-NGGELGVVGIVRDITERKE 119
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 177-259 4.52e-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: 64.67  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 177 SDGLRENLGRSPHAPLS-YEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLS 255
Cdd:pfam08447   5 SPRFEEILGYTPEELLGkGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKPVR 84


                  ....
gi 2495942583 256 IAGI 259
Cdd:pfam08447  85 VIGV 88
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 13-118 5.58e-11

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: 59.18  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  13 TRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNRRKDGTVF 92
Cdd:cd00130     1 LPDGVIVLDL---DGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77

                          90       100
                  ....*....|....*....|....*.
gi 2495942583  93 WNRLLVSPVFASDGELTYFFASQYDV 118
Cdd:cd00130    78 WVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
141-271 6.47e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 62.73  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 141 RRSLELIQSEERLRFTLKAGRLGAWTLDLGVMRLISSDGLRENLGRSPhaplsyEEMI-----AAIHPDDRHRKLAARDA 215
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSA------EELLgktlrDLLPPEDDDEFLELLRA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2495942583 216 AIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLSIAGISLDITDRKRAEE 271
Cdd:COG2202    75 ALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEE 130
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 149-271 1.08e-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: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 149 SEERLRFTLKAGRLGAWTLDL-GVMRLISsDGLRENLGRSPhaplsyEEMIA-----AIHPDDR--HRKLAARDAAiAGH 220
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVIDLeGNILYVN-PAFEEIFGYSA------EELIGrnvleLIPEEDReeVRERIERRLE-GEP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2495942583 221 SDYDIEIRIITPRGEIRWLQFRGRaSYRADGTPLSIAGISLDITDRKRAEE 271
Cdd:TIGR00229  73 EPVSEERRVRRKDGSEIWVEVSVS-PIRTNGGELGVVGIVRDITERKEAEE 122
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 145-290 1.12e-05

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 48.13  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  145 ELIQSEERLRFTLKAGRLGawtldlgvMRLISSDG--------LRENLGRSPH--APLSYEEMIaaiHPDDRHRKLAARD 214
Cdd:PRK09776   277 HISESETRFRNAMEYSAIG--------MALVGTEGqwlqvnkaLCQFLGYSQEelRGLTFQQLT---WPEDLNKDLQQVE 345

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495942583  215 AAIAGHSD-YDIEIRIITPRGEIRWLQFRGRASYRADGTPLS-IAGISlDITDRKRAEEHRDLLAgelnHRIqnTLAT 290
Cdd:PRK09776   346 KLLSGEINsYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYfIAQIE-DINELKRTEQVNERLM----ERI--TLAN 416
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 177-263 1.24e-04

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: 41.08  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 177 SDGLRENLGRSPHAPL--SYEEMIaaiHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPL 254
Cdd:cd00130    18 NPAAEQLLGYSPEELIgkSLLDLI---HPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGEVI 94


                  ....*....
gi 2495942583 255 SIAGISLDI 263
Cdd:cd00130    95 GLLGVVRDI 103
 
Name Accession Description Interval E-value
PRK13559 PRK13559
hypothetical protein; Provisional
 6-465 1.03e-69

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 225.85  E-value: 1.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNR 85
Cdd:PRK13559   45 FEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  86 RKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTlekerlvilqrdrdaleaesarrsleliqseerlrftlkagrlgaw 165
Cdd:PRK13559  125 RKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVT---------------------------------------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 166 tldlgvmrlissdglrenlgrsphaplsyeemiaaihpddrhrklaardaaiaghsdydiEIRiitprgEIRwlqfrgra 245
Cdd:PRK13559  159 ------------------------------------------------------------DIR------AVR-------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 246 syradgtplsiagislditdRKRAEEHRdlLAGELNHRIQNTLATVQSIARQTLRGAASLEEAQvAMESRLQSLSAATEM 325
Cdd:PRK13559  165 --------------------ALEAHERR--LAREVDHRSKNVFAVVDSIVRLTGRADDPSLYAA-AIQERVQALARAHET 221

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 326 LArGSGDWAT--LTEVVIAALHPFGVEQDqRFKIGGPILRLAPRIALAFALAIHELATNSVKYGSLSVDDGRVIVSWDvv 403
Cdd:PRK13559  222 LL-DERGWETveVEELIRAQVAPYAPRAT-RVAFEGPGIRLGAASVQPLGLVLHELAVNAIKHGALSADQGRISISWK-- 297

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495942583 404 DGSSPDRLWFQWQEVGGPRVSRPTRTGFGSRMIERALAQEIGGTAEIDYRPRGVVFTAEAPL 465
Cdd:PRK13559  298 PSPEGAGFRIDWQEQGGPTPPKLAKRGFGTVIIGAMVESQLNGQLEKTWSDDGLLARIEIPS 359
PRK13557 PRK13557
histidine kinase; Provisional
 2-137 5.86e-56

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 194.50  E-value: 5.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   2 GSDPFAAAVRATRMPMVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEID 81
Cdd:PRK13557   28 RSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2495942583  82 LKNRRKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTlekerlvilqRDRDALEA 137
Cdd:PRK13557  108 ILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVS----------RRRDAEDA 153
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 7-470 1.99e-46

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 168.16  E-value: 1.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   7 AAAVRATRMPMVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNRR 86
Cdd:COG3920    24 LLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  87 KDGTVFWNRLLVSPVFASDGELTYFFASQYDVTLEKERLVILQRDRDALEAESARRSLELIQSEERLRFTLKAGRLGAWT 166
Cdd:COG3920   104 LAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 167 LDLGVMRLISSDGLRENLGRSPHAPLSYEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRAS 246
Cdd:COG3920   184 LLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLL 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 247 YRADGtpLSIAGISLDITDRKRAE-------EHRDLLAGELNHRIQNTLATVQSIARQTLRGAASLE--EAQVAMESRLQ 317
Cdd:COG3920   264 LRALL--LLAAGIRLVITERKRAEeeleaslEEKELLLRELHHRVKNNLQVVSSLLRLQARRADDPEarEALEESQNRIQ 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 318 SLSAATEMLARgSGDWAT-----LTEVVIAALHPFGVEQDQRFKIGGPILRLAPRIALAFALAIHELATNSVKYGSLSVD 392
Cdd:COG3920   342 ALALVHELLYQ-SEDWEGvdlrdYLRELLEPLRDSYGGRGIRIELDGPDVELPADAAVPLGLILNELVTNALKHAFLSGE 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 393 DGRVIVSWDVVDgsspDRLWFQWQEVGG---PRVSRPTRTGFGSRMIeRALAQEIGGTAEIDyRPRGVVFTAEAPLPEIT 469
Cdd:COG3920   421 GGRIRVSWRRED----GRLRLTVSDNGVglpEDVDPPARKGLGLRLI-RALVRQLGGTLELD-RPEGTRVRITFPLAELA 494


                  .
gi 2495942583 470 R 470
Cdd:COG3920   495 A 495
PAS COG2202
PAS domain [Signal transduction mechanisms];
6-271 8.27e-37

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 135.92  E-value: 8.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNR 85
Cdd:COG2202    13 LRALVESSPDAIIITDL---DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  86 RKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTLEKerlvilqrdrdalEAESArrsleLIQSEERLRFTLKAGRLGAW 165
Cdd:COG2202    90 RKDGSLFWVELSISPVRDEDGEITGFVGIARDITERK-------------RAEEA-----LRESEERLRLLVENAPDGIF 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 166 TLDLGVMRLISSDGLRENLGRSPHApLSYEEMIAAIHPDDRHRKLAARDAAIAGHSD-YDIEIRIITPRGEIRWLQFRGR 244
Cdd:COG2202   152 VLDLDGRILYVNPAAEELLGYSPEE-LLGKSLLDLLHPEDRERLLELLRRLLEGGREsYELELRLKDGDGRWVWVEASAV 230

                         250       260
                  ....*....|....*....|....*..
gi 2495942583 245 AsYRADGTPLSIAGISLDITDRKRAEE 271
Cdd:COG2202   231 P-LRDGGEVIGVLGIVRDITERKRAEE 256
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 17-136 2.27e-35

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 139.20  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  17 MVITDPRLPDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNRRKDGTVFWNRL 96
Cdd:PRK13558  161 ITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2495942583  97 LVSPVFASDGELTYFFASQYDVTLEKERLVILQRDRDALE 136
Cdd:PRK13558  241 DIAPIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKLQ 280
HWE_HK pfam07536
HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate ...
 279-360 7.92e-27

HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate response regulator protein, represent the best-known apparatus for transducing external cues into a physiological response in bacteria. The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as pfam00512 and pfam07568. The family was defined by the presence of a highly conserved H residue in the kinase domain and a WxE motif in a C-terminal ATPase domain that is related to pfam02518. It has been demonstrated to show structural and functional correlation with pfam07568. These proteins are found in a variety of alpha- and gamma- proteobacteria, with significant enrichment in the rhizobia.


Pssm-ID: 429521 [Multi-domain]  Cd Length: 83  Bit Score: 103.11  E-value: 7.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 279 ELNHRIQNTLATVQSIARQTLRGAASLEEAQVAMESRLQSLSAATEMLARGSGDWATLTEVVIAALHPFGVEQDQRFKIG 358
Cdd:pfam07536   1 ELNHRVKNTLATVQSIARQTLRNAASLDEFVEAFEGRLQALSRAHDLLSRASWAGADLSELLEAELAPYGGEAGTRITLS 80


                  ..
gi 2495942583 359 GP 360
Cdd:pfam07536  81 GP 82
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 32-271 4.06e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 100.13  E-value: 4.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   32 VNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRV-TIEIDLKNRRKDGTVFWNRLLVSPVFASDGELTY 110
Cdd:PRK09776   308 VNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEInSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLY 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  111 FFASQYDVTLEKErlvilqrdrdaleAESARRSLEliqseERLRFTLKAGRLGAWTLDLGVMRLISSDGLRENLGRSPHA 190
Cdd:PRK09776   388 FIAQIEDINELKR-------------TEQVNERLM-----ERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHI 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  191 PLSYEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGeIRWLQFRGRASYRADGTPLSIAGISLDITDRKRAE 270
Cdd:PRK09776   450 KPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQLN 528


                   .
gi 2495942583  271 E 271
Cdd:PRK09776   529 E 529
HWE_HK smart00911
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, ...
 279-360 3.92e-21

HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as. In. the HWE family was defined by the presence of conserved a H residue and a WXE motifs and was limited to members of the proteobacteria. However, many homologues of this domain are lack the WXE motif. Furthermore, homologues are found in a wide range of Gram-positive and Gram-negative bacteria as well as in several archaea.


Pssm-ID: 214907 [Multi-domain]  Cd Length: 84  Bit Score: 87.26  E-value: 3.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  279 ELNHRIQNTLATVQSIARQTLRGAASLEEAQVAMESRLQSLSAATEMLARGSGDWATLTEVVIAALHPFGVEQDQ-RFKI 357
Cdd:smart00911   1 ELNHRVKNLLAVVQAIARQTLRSASSLEDFAEAFEGRLQALARAHDLLSRSDWSGADLRDLVRAELAPYGGPGDGeRITL 80


                   ...
gi 2495942583  358 GGP 360
Cdd:smart00911  81 SGP 83
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 29-291 3.10e-20

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: 93.12  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  29 IVYVNDAFVRLTGYAREEIIGRNCRFLQGPE--TSLKDVARVRDAIERRVTIEIDLKNrrKDGTVFWNRLLVSPVFASDG 106
Cdd:COG5809    37 ILKVNPAAERIFGYTEDELLGTNILDFLHPDdeKELREILKLLKEGESRDELEFELRH--KNGKRLEFSSKLSPIFDQNG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 107 ELTYFFASQYDVTLEKerlvilqrdrdaleaesaRRSLELIQSEERLRFTLKAGRLGAWTLDLGVMRLISSDGLRENLGr 186
Cdd:COG5809   115 DIEGMLAISRDITERK------------------RMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLG- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 187 sphapLSYEEMIAA-----IHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRaDGTPLSIAGISL 261
Cdd:COG5809   176 -----ISIEELIGKsilelIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKK-NGEVDGIVIIFR 249

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2495942583 262 DITDRKRAEE---HRDLLA--GEL----NHRIQNTLATV 291
Cdd:COG5809   250 DITERKKLEEllrKSEKLSvvGELaagiAHEIRNPLTSL 288
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 26-119 1.04e-19

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: 83.66  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  26 DNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLknRRKDGTVFWNRLLVSPVFASD 105
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVVL--YRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|....
gi 2495942583 106 GELTYFFASQYDVT 119
Cdd:pfam13426  79 GELVGIIAILRDIT 92
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 29-291 2.46e-14

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: 75.15  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  29 IVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSlKDVARVRDAIERRVTIEIDLKNRRKDGTVFWNRLLVSPVFASDGEL 108
Cdd:COG5805    56 VIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYH-YRVKTRIERLQKGYDVVMIEQIYCKDGELIYVEVKLFPIYNQNGQA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 109 TYFFASqyDVTlekerlvilqrDRDALEAEsarrsleLIQSEERLRFTLKAGRLGAWTLDL-GVMRLISSDGLRenLGRS 187
Cdd:COG5805   135 AILALR--DIT-----------KKKKIEEI-------LQEQEERLQTLIENSPDLICVIDTdGRILFINESIER--LFGA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 188 PHAPLSYEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLSIAGISLDITDRK 267
Cdd:COG5805   193 PREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKK 272

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2495942583 268 RAEE---HRDLL--AGELN----HRIQNTLATV 291
Cdd:COG5805   273 EAEElmaRSEKLsiAGQLAagiaHEIRNPLTSI 305
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 6-123 1.16e-13

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: 67.32  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIE-RRVTIEIDLKN 84
Cdd:TIGR00229   5 YRAIFESSPDAIIVIDL---EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEgEPEPVSEERRV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2495942583  85 RRKDGTVFWNRLLVSPVFAsDGELTYFFASQYDVTLEKE 123
Cdd:TIGR00229  82 RRKDGSEIWVEVSVSPIRT-NGGELGVVGIVRDITERKE 119
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 177-259 4.52e-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: 64.67  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 177 SDGLRENLGRSPHAPLS-YEEMIAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLS 255
Cdd:pfam08447   5 SPRFEEILGYTPEELLGkGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKPVR 84


                  ....
gi 2495942583 256 IAGI 259
Cdd:pfam08447  85 VIGV 88
PRK13560 PRK13560
hypothetical protein; Provisional
 49-465 1.24e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 70.09  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  49 GRNCRFLQGPETSLKDVARVRDAIERRVtieidlknRRKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTLEKErlvil 128
Cdd:PRK13560  401 GRPMAFDACPMAKTIKGGKIFDGQEVLI--------EREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQ----- 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 129 qrdrdalEAESARRSLELIQSEERLRFTLKAGRlgAWTLDLgVMRLISsdglreNLGRSPHAPLSYEEMIAA-IHPDDRh 207
Cdd:PRK13560  468 -------VEEQLLLANLIVENSPLVLFRWKAEE--GWPVEL-VSKNIT------QFGYEPDEFISGKRMFAAiIHPADL- 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 208 RKLAARDAAIA--GHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLSIAGISLDITDRKRAEE-------HRDLLAG 278
Cdd:PRK13560  531 EQVAAEVAEFAaqGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEkikaaltEKEVLLK 610

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 279 ELNHRIQNTLATVQS---IARQTLRGaaslEEAQVAM---ESRLQSLSAATEMLARGSG----DWATLTEVVIAALH--- 345
Cdd:PRK13560  611 EIHHRVKNNLQIISSlldLQAEKLHD----EEAKCAFaesQDRICAMALAHEKLYQSEDladiDFLDYIESLTAHLKnsf 686

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 346 --PFGVEQdqrFKIGGPILRLAPRIALAFALAIHELATNSVKY-------GSLSVD---DGRVIVSWDVVDGSspdrlwf 413
Cdd:PRK13560  687 aiDFGRID---CKIDADDGCLDIDKAIPCGLIISELLSNALKHafpdgaaGNIKVEireQGDGMVNLCVADDG------- 756

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2495942583 414 qwqeVGGPRVSRPTRTGFGSRMIERALAQEIGGTAEIDYRpRGVVFTAEAPL 465
Cdd:PRK13560  757 ----IGLPAGFDFRAAETLGLQLVCALVKQLDGEIALDSR-GGARFNIRFPM 803
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
 3-130 5.29e-12

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 67.62  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   3 SDPFAAAVRATRMPMVITDprLPDNpIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDL 82
Cdd:TIGR02938   3 PEAYRQTVDQAPLAISITD--LKAN-ILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2495942583  83 KNRRKDGTVFWNRLLVSPVFASDGELTYFFASQYDVTLEK--ERLVILQR 130
Cdd:TIGR02938  80 LNRRKDGELYLAELTVAPVLNEAGETTHFLGMHRDITELHrlEQVVANQK 129
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 13-118 5.58e-11

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: 59.18  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  13 TRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAIERRVTIEIDLKNRRKDGTVF 92
Cdd:cd00130     1 LPDGVIVLDL---DGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77

                          90       100
                  ....*....|....*....|....*.
gi 2495942583  93 WNRLLVSPVFASDGELTYFFASQYDV 118
Cdd:cd00130    78 WVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
141-271 6.47e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 62.73  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 141 RRSLELIQSEERLRFTLKAGRLGAWTLDLGVMRLISSDGLRENLGRSPhaplsyEEMI-----AAIHPDDRHRKLAARDA 215
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSA------EELLgktlrDLLPPEDDDEFLELLRA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2495942583 216 AIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLSIAGISLDITDRKRAEE 271
Cdd:COG2202    75 ALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEE 130
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 6-118 2.05e-10

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: 57.81  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLKDVARVRDAI---ERRVTIEIDL 82
Cdd:pfam00989   3 LRAILESLPDGIFVVDE---DGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALlqgEESRGFEVSF 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2495942583  83 knRRKDGTVFWNRLLVSPVFASDGELTYFFASQYDV 118
Cdd:pfam00989  80 --RVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 29-111 1.33e-09

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: 54.65  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  29 IVYVNDAFVRLTGYAREEIIGRNCRFLQG--PEtslkDVARVRDAIERRVT----IEIDLKNRRKDGTVFWNRLLVSPVF 102
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhPD----DRERVREALWEALKggepYSGEYRIRRKDGEYRWVEARARPIR 76


                  ....*....
gi 2495942583 103 ASDGELTYF 111
Cdd:pfam08447  77 DENGKPVRV 85
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
3-137 4.33e-09

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 57.93  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   3 SDPFAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPETSLkdVARVRDAIERRVTI-EID 81
Cdd:COG3852     6 EELLRAILDSLPDAVIVLDA---DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPL--RELLERALAEGQPVtERE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2495942583  82 LKNRRKDGTVFWNRLLVSPVFASDGElTYFFASQYDVTlEKERLVILQRDRDALEA 137
Cdd:COG3852    81 VTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDIT-ERKRLERELRRAEKLAA 134
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 6-74 3.67e-07

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 47.39  E-value: 3.67e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495942583    6 FAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPEtslkDVARVRDAIER 74
Cdd:smart00091   3 LRAILESLPDGIFVLDL---DGRILYANPAAEELLGYSPEELIGKSLLELIHPE----DRERVQEALQR 64
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 9-143 1.23e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 50.92  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   9 AVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNC-RFLQGPETSLKDVARVRDAIERRVTIEIDLKNRRK 87
Cdd:PRK11359  141 AVDHLDRPVIVLDP---ERRIVQCNRAFTEMFGYCISEASGMQPdTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTR 217

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2495942583  88 DGTVFWNRLLVSPVFASDGELTYFFASQYDVTLEKErlvILQRDRDALEAESARRS 143
Cdd:PRK11359  218 TGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQ---IRQLEGNILAAMCSSPP 270
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 79-119 2.21e-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: 44.48  E-value: 2.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2495942583   79 EIDLKNRRKDGTVFWNRLLVSPVFASDGELTYFFASQYDVT 119
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 149-271 1.08e-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: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 149 SEERLRFTLKAGRLGAWTLDL-GVMRLISsDGLRENLGRSPhaplsyEEMIA-----AIHPDDR--HRKLAARDAAiAGH 220
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVIDLeGNILYVN-PAFEEIFGYSA------EELIGrnvleLIPEEDReeVRERIERRLE-GEP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2495942583 221 SDYDIEIRIITPRGEIRWLQFRGRaSYRADGTPLSIAGISLDITDRKRAEE 271
Cdd:TIGR00229  73 EPVSEERRVRRKDGSEIWVEVSVS-PIRTNGGELGVVGIVRDITERKEAEE 122
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 145-290 1.12e-05

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 48.13  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  145 ELIQSEERLRFTLKAGRLGawtldlgvMRLISSDG--------LRENLGRSPH--APLSYEEMIaaiHPDDRHRKLAARD 214
Cdd:PRK09776   277 HISESETRFRNAMEYSAIG--------MALVGTEGqwlqvnkaLCQFLGYSQEelRGLTFQQLT---WPEDLNKDLQQVE 345

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495942583  215 AAIAGHSD-YDIEIRIITPRGEIRWLQFRGRASYRADGTPLS-IAGISlDITDRKRAEEHRDLLAgelnHRIqnTLAT 290
Cdd:PRK09776   346 KLLSGEINsYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYfIAQIE-DINELKRTEQVNERLM----ERI--TLAN 416
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 16-147 1.15e-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: 47.46  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  16 PMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQgPETSLKDVARvrdaiERRVTIEIDLKNRRKDGTVFWNR 95
Cdd:COG3829    23 GIIVVDA---DGRITYVNRAAERILGLPREEVIGKNVTELI-PNSPLLEVLK-----TGKPVTGVIQKTGGKGKTVIVTA 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2495942583  96 llvSPVFaSDGELTYFFASQYDVTlEKERLVILQRDRDALEAESARRSLELI 147
Cdd:COG3829    94 ---IPIF-EDGEVIGAVETFRDIT-ELKRLERKLREEELERGLSAKYTFDDI 140
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 138-271 1.81e-05

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: 46.89  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 138 ESARRSLELIQSEERLRFTLKAGRLGAWTLDLGVMRLISSDGLRENLGRSPHApLSYEEMIAAIHPDDRHRKLAARDAAI 217
Cdd:COG5809     2 KSSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDE-LLGTNILDFLHPDDEKELREILKLLK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2495942583 218 AGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPLSIAGISLDITDRKRAEE 271
Cdd:COG5809    81 EGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEE 134
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 224-266 8.19e-05

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: 39.86  E-value: 8.19e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2495942583  224 DIEIRIITPRGEIRWLQFRGRASYRADGTPLSIAGISLDITDR 266
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 177-263 1.24e-04

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: 41.08  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 177 SDGLRENLGRSPHAPL--SYEEMIaaiHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPL 254
Cdd:cd00130    18 NPAAEQLLGYSPEELIgkSLLDLI---HPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGEVI 94


                  ....*....
gi 2495942583 255 SIAGISLDI 263
Cdd:cd00130    95 GLLGVVRDI 103
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 6-142 3.80e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 43.22  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583   6 FAAAVRATRMPMVITDPrlpDNPIVYVNDAFVRLTGYAREEIIGRNCRFLQGPE---TSLKDVARVRDAIERRV-TIEID 81
Cdd:PRK11359   14 FFPALEQNMMGAVLINE---NDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpAHPEYIRHNREGGKARVeGMSRE 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495942583  82 LKNRRKDGTVFWNRLLVSPVFAsDGElTYFFASQYDVTLEKE-----RLVIL---QRDRDALEAESARR 142
Cdd:PRK11359   91 LQLEKKDGSKIWTRFALSKVSA-EGK-VYYLALVRDASVEMAqkeqtRQLIIavdHLDRPVIVLDPERR 157
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
362-462 8.10e-04

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.51  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 362 LRLAPRIALAFALAIHELATNSVKYGSLSVDDGRVIVSWDVvdgsSPDRL---------WFQWQEVGGPRVSRPTRtGFG 432
Cdd:COG2172    25 LGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVEVELEL----DPDGLeievrdegpGFDPEDLPDPYSTLAEG-GRG 99

                          90       100       110
                  ....*....|....*....|....*....|
gi 2495942583 433 SRMIeRALAQEIggtaEIDYRPRGVVFTAE 462
Cdd:COG2172   100 LFLI-RRLMDEV----EYESDPGGTTVRLV 124
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
198-327 3.51e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 39.44  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583 198 IAAIHPDDRHRKLAARDAAIAGHSDYDIEIRIITPRGEIRWLQFRGRASYRADGTPlSIAGISLDITDRKRAEEHRDL-- 275
Cdd:COG3852    52 LAELFPEDSPLRELLERALAEGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRae 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495942583 276 -------LAGELNHRIQNTLATVqsiarqtlRGAASL-----------EEAQVAMES--RLQSLsaATEMLA 327
Cdd:COG3852   131 klaavgeLAAGLAHEIRNPLTGI--------RGAAQLlerelpddelrEYTQLIIEEadRLNNL--VDRLLS 192
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 29-123 6.57e-03

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: 36.24  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495942583  29 IVYVNDAFVRLTGYAREEIIGRNCRFLQGPEtslkDVARVRDAIER----RVTIEIDLKNRRKDGTVFWnRLLVSPVFAS 104
Cdd:pfam08448  17 VRYANAAAAELFGLPPEELLGKTLAELLPPE----DAARLERALRRalegEEPIDFLEELLLNGEERHY-ELRLTPLRDP 91

                          90
                  ....*....|....*....
gi 2495942583 105 DGELTYFFASQYDVTLEKE 123
Cdd:pfam08448  92 DGEVIGVLVISRDITERRR 110
 
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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