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Conserved domains on  [gi|2008034186|ref|XP_040033852|]
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potassium voltage-gated channel subfamily H member 1a isoform X4 [Gasterosteus aculeatus aculeatus]

Protein Classification

PAS and CAP_ED domain-containing protein( domain architecture ID 13822798)

protein containing domains PAS, CAP_ED, and PRK11753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 227-627 1.96e-35

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 145.40  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 227 WDWVILILTFYTAIMVPYNVSFKTKQNNVTWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 305
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 306 DLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVAR---KLDHYIEYGAAVL--VLLVCVFGLAAHWLACIWFSI 380
Cdd:PLN03192  144 DVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQlftRLEKDIRFSYFWIrcARLLSVTLFLVHCAGCLYYLI 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 381 GDyevideetnivrmdswlyilaetvgnpyRFNASGTgKWEGG--PNKDSV-----YITSLYFTMTSLTSIGFGNIAPTT 453
Cdd:PLN03192  224 AD----------------------------RYPHQGK-TWIGAviPNFRETslwirYISAIYWSITTMTTVGYGDLHAVN 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 454 DGEKIFAVAMMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMINSVR---DFLKLYQVPKGLSERVMDYIASTWSmSRGI 530
Cdd:PLN03192  275 TIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESL 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 531 DTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVI- 609
Cdd:PLN03192  351 NQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIId 430

                         410       420
                  ....*....|....*....|.
gi 2008034186 610 ---QDEEVVAILGKGDVFGDV 627
Cdd:PLN03192  431 segEKERVVGTLGCGDIFGEV 451
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 48-142 1.33e-15

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: 72.88  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  48 PIVYSNDGFCKLSGYHRAEVMQKSSTCSFmygelTDKDSTEKVRLTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 126
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 2008034186 127 QEKVVLFLCTFSDITA 142
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PRK11753 super family cl36052
cAMP-activated global transcriptional regulator CRP;
588-692 3.66e-06

cAMP-activated global transcriptional regulator CRP;


The actual alignment was detected with superfamily member PRK11753:

Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 48.82  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 588 IYHAGESVDSLCFVVSGSLEV-IQDEE----VVAILGKGDVFGdvfwkEVTL----AQACANVRALTYCDLHVIKRDALQ 658
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVlIKDEEgkemILSYLNQGDFIG-----ELGLfeegQERSAWVRAKTACEVAEISYKKFR 105

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2008034186 659 KVL----EFYTAFSNHFSRNLLLTYnlrkrivfRKISD 692
Cdd:PRK11753  106 QLIqvnpDILMALSAQMARRLQNTS--------RKVGD 135
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 227-627 1.96e-35

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 145.40  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 227 WDWVILILTFYTAIMVPYNVSFKTKQNNVTWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 305
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 306 DLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVAR---KLDHYIEYGAAVL--VLLVCVFGLAAHWLACIWFSI 380
Cdd:PLN03192  144 DVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQlftRLEKDIRFSYFWIrcARLLSVTLFLVHCAGCLYYLI 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 381 GDyevideetnivrmdswlyilaetvgnpyRFNASGTgKWEGG--PNKDSV-----YITSLYFTMTSLTSIGFGNIAPTT 453
Cdd:PLN03192  224 AD----------------------------RYPHQGK-TWIGAviPNFRETslwirYISAIYWSITTMTTVGYGDLHAVN 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 454 DGEKIFAVAMMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMINSVR---DFLKLYQVPKGLSERVMDYIASTWSmSRGI 530
Cdd:PLN03192  275 TIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESL 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 531 DTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVI- 609
Cdd:PLN03192  351 NQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIId 430

                         410       420
                  ....*....|....*....|.
gi 2008034186 610 ---QDEEVVAILGKGDVFGDV 627
Cdd:PLN03192  431 segEKERVVGTLGCGDIFGEV 451
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 227-490 1.20e-32

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 127.00  E-value: 1.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 227 WDWVILILTFYTAIMVPYNVSFKTKQNNVTWL-VVDSIVDVIFLVDIVLNFHTTFvgpagevisdpklIRMNYLKT-WFV 304
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEPLTTVLeILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 305 IDLLSCLPYDVInaFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVL--VLLVCVFGLAAHWLACIWFSIGd 382
Cdd:pfam00520  71 LDFVVVLPSLIS--LVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLLFLFIFAIIG- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 383 yevideetnivrmdswlyilaetvgnpYRFNASGTGKWEGGPNKDSV---YITSLYFTMTSLTSIGFGNIAPTTDGEK-- 457
Cdd:pfam00520 148 ---------------------------YQLFGGKLKTWENPDNGRTNfdnFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2008034186 458 -----IFAVAMMMIGSLLYATIFGNVTTIFQQMYANTN 490
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 561-671 8.32e-24

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 97.01  E-value: 8.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 561 AFRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQD-----EEVVAILGKGDVFGDVFWkeVTLA 635
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLdedgrEQIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2008034186 636 QACANVRALTYCDLHVIKRDALQKVLEFYTAFSNHF 671
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 562-678 1.68e-18

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 82.06  E-value: 1.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  562 FRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQD-----EEVVAILGKGDVFGdvfwkE---VT 633
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFG-----ElalLT 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2008034186  634 LAQACANVRALTYCdLHVIKRDALQKVLEFYTAFSNHFSRNLLLT 678
Cdd:smart00100  77 NSRRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 48-142 1.33e-15

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: 72.88  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  48 PIVYSNDGFCKLSGYHRAEVMQKSSTCSFmygelTDKDSTEKVRLTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 126
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 2008034186 127 QEKVVLFLCTFSDITA 142
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
46-145 2.45e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.99  E-value: 2.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMQKssTCSFMYGELTDKDSTEKVRLTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 125
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                          90       100
                  ....*....|....*....|
gi 2008034186 126 EQEKVVLFLCTFSDITAFKQ 145
Cdd:COG2202   108 EDGEITGFVGIARDITERKR 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 562-675 5.39e-14

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 71.94  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 562 FRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQ-----DEEVVAILGKGDVFGDVFWkeVTLAQ 636
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSL--LGGEP 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2008034186 637 ACANVRALTYCDLHVIKRDALQKVLEFYTAFSNHFSRNL 675
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 46-145 4.81e-12

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 69.87  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMQKSstCSFMYGELTDKDSTEKVRLTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 125
Cdd:PRK13558  170 DEPLIYINDAFERITGYSPDEVLGRN--CRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                          90       100
                  ....*....|....*....|
gi 2008034186 126 EQEKVVLFLCTFSDITAFKQ 145
Cdd:PRK13558  248 EDGTVTHYVGFQTDVTERKE 267
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 46-140 1.31e-08

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 53.41  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMQKSstcsfmYGELTDKDSTEKVRLTFENY----EMNSFEILMYKKNRTPVWFFVKIA 121
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKS------LLDLIHPEDREELRERLENLlsggEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....*....
gi 2008034186 122 PIRNEQEKVVLFLCTFSDI 140
Cdd:cd00130    85 PIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 101-142 4.09e-07

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: 47.18  E-value: 4.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2008034186  101 SFEILMYKKNRTPVWFFVKIAPIRNEQEKVVLFLCTFSDITA 142
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
588-692 3.66e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 48.82  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 588 IYHAGESVDSLCFVVSGSLEV-IQDEE----VVAILGKGDVFGdvfwkEVTL----AQACANVRALTYCDLHVIKRDALQ 658
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVlIKDEEgkemILSYLNQGDFIG-----ELGLfeegQERSAWVRAKTACEVAEISYKKFR 105

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2008034186 659 KVL----EFYTAFSNHFSRNLLLTYnlrkrivfRKISD 692
Cdd:PRK11753  106 QLIqvnpDILMALSAQMARRLQNTS--------RKVGD 135
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 49-145 1.19e-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: 45.74  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  49 IVYSNDGFCKLSGYHRAEVMQKSSTcsfmygELTDKDSTEKVRLTFENYEM-----NSFEILMYKKNRTPVWFFVKIAPI 123
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRNVL------ELIPEEDREEVRERIERRLEgepepVSEERRVRRKDGSEIWVEVSVSPI 98

                          90       100
                  ....*....|....*....|..
gi 2008034186 124 RNEQEKVVlFLCTFSDITAFKQ 145
Cdd:TIGR00229  99 RTNGGELG-VVGIVRDITERKE 119
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 227-627 1.96e-35

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 145.40  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 227 WDWVILILTFYTAIMVPYNVSFKTKQNNVTWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 305
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 306 DLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVAR---KLDHYIEYGAAVL--VLLVCVFGLAAHWLACIWFSI 380
Cdd:PLN03192  144 DVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQlftRLEKDIRFSYFWIrcARLLSVTLFLVHCAGCLYYLI 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 381 GDyevideetnivrmdswlyilaetvgnpyRFNASGTgKWEGG--PNKDSV-----YITSLYFTMTSLTSIGFGNIAPTT 453
Cdd:PLN03192  224 AD----------------------------RYPHQGK-TWIGAviPNFRETslwirYISAIYWSITTMTTVGYGDLHAVN 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 454 DGEKIFAVAMMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMINSVR---DFLKLYQVPKGLSERVMDYIASTWSmSRGI 530
Cdd:PLN03192  275 TIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESL 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 531 DTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVI- 609
Cdd:PLN03192  351 NQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIId 430

                         410       420
                  ....*....|....*....|.
gi 2008034186 610 ---QDEEVVAILGKGDVFGDV 627
Cdd:PLN03192  431 segEKERVVGTLGCGDIFGEV 451
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 227-490 1.20e-32

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 127.00  E-value: 1.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 227 WDWVILILTFYTAIMVPYNVSFKTKQNNVTWL-VVDSIVDVIFLVDIVLNFHTTFvgpagevisdpklIRMNYLKT-WFV 304
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEPLTTVLeILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 305 IDLLSCLPYDVInaFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVL--VLLVCVFGLAAHWLACIWFSIGd 382
Cdd:pfam00520  71 LDFVVVLPSLIS--LVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLLFLFIFAIIG- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 383 yevideetnivrmdswlyilaetvgnpYRFNASGTGKWEGGPNKDSV---YITSLYFTMTSLTSIGFGNIAPTTDGEK-- 457
Cdd:pfam00520 148 ---------------------------YQLFGGKLKTWENPDNGRTNfdnFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2008034186 458 -----IFAVAMMMIGSLLYATIFGNVTTIFQQMYANTN 490
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 561-671 8.32e-24

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 97.01  E-value: 8.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 561 AFRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQD-----EEVVAILGKGDVFGDVFWkeVTLA 635
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLdedgrEQIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2008034186 636 QACANVRALTYCDLHVIKRDALQKVLEFYTAFSNHF 671
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 562-678 1.68e-18

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 82.06  E-value: 1.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  562 FRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQD-----EEVVAILGKGDVFGdvfwkE---VT 633
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFG-----ElalLT 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2008034186  634 LAQACANVRALTYCdLHVIKRDALQKVLEFYTAFSNHFSRNLLLT 678
Cdd:smart00100  77 NSRRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 48-142 1.33e-15

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: 72.88  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  48 PIVYSNDGFCKLSGYHRAEVMQKSSTCSFmygelTDKDSTEKVRLTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 126
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 2008034186 127 QEKVVLFLCTFSDITA 142
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
46-145 2.45e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.99  E-value: 2.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMQKssTCSFMYGELTDKDSTEKVRLTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 125
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                          90       100
                  ....*....|....*....|
gi 2008034186 126 EQEKVVLFLCTFSDITAFKQ 145
Cdd:COG2202   108 EDGEITGFVGIARDITERKR 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 562-675 5.39e-14

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 71.94  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 562 FRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQ-----DEEVVAILGKGDVFGDVFWkeVTLAQ 636
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSL--LGGEP 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2008034186 637 ACANVRALTYCDLHVIKRDALQKVLEFYTAFSNHFSRNL 675
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 580-662 1.08e-13

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 67.25  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 580 IHCAPGDLIYHAGESVDSLCFVVSGSLEVIQD-----EEVVAILGKGDVFGDVFWkeVTLAQACANVRALTYCDLHVIKR 654
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTledgrEQILAVLGPGDFFGELAL--LGGEPRSATVVALTDSELLVIPR 79


                  ....*...
gi 2008034186 655 DALQKVLE 662
Cdd:pfam00027  80 EDFLELLE 87
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 46-145 4.81e-12

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 69.87  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMQKSstCSFMYGELTDKDSTEKVRLTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 125
Cdd:PRK13558  170 DEPLIYINDAFERITGYSPDEVLGRN--CRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                          90       100
                  ....*....|....*....|
gi 2008034186 126 EQEKVVLFLCTFSDITAFKQ 145
Cdd:PRK13558  248 EDGTVTHYVGFQTDVTERKE 267
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 430-484 8.05e-12

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 61.90  E-value: 8.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2008034186 430 YITSLYFTMTSLTSIGFGNIAPTTDGEKIFAVAMMMIGSLLYATIFGNVTTIFQQ 484
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK13559 PRK13559
hypothetical protein; Provisional
 32-144 2.30e-10

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 63.30  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  32 QTDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSstCSFMYGELTDKDSTEKVRLTFENYEMNSFEILMYKKNR 111
Cdd:PRK13559   51 QTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRN--CRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDG 128

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2008034186 112 TPVWFFVKIAPIRNEQEKVVLFLCTFSDITAFK 144
Cdd:PRK13559  129 EPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIR 161
PRK13557 PRK13557
histidine kinase; Provisional
 46-141 9.73e-09

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 58.91  E-value: 9.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMqkSSTCSFMYGELTDKDSTEKVRLTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 125
Cdd:PRK13557   52 DNPIVFANRAFLEMTGYAAEEII--GNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYN 129

                          90
                  ....*....|....*.
gi 2008034186 126 EQEKVVLFLCTFSDIT 141
Cdd:PRK13557  130 DAGDLVYFFGSQLDVS 145
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 46-140 1.31e-08

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 53.41  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  46 DWPIVYSNDGFCKLSGYHRAEVMQKSstcsfmYGELTDKDSTEKVRLTFENY----EMNSFEILMYKKNRTPVWFFVKIA 121
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKS------LLDLIHPEDREELRERLENLlsggEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....*....
gi 2008034186 122 PIRNEQEKVVLFLCTFSDI 140
Cdd:cd00130    85 PIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 101-142 4.09e-07

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: 47.18  E-value: 4.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2008034186  101 SFEILMYKKNRTPVWFFVKIAPIRNEQEKVVLFLCTFSDITA 142
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
588-692 3.66e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 48.82  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186 588 IYHAGESVDSLCFVVSGSLEV-IQDEE----VVAILGKGDVFGdvfwkEVTL----AQACANVRALTYCDLHVIKRDALQ 658
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVlIKDEEgkemILSYLNQGDFIG-----ELGLfeegQERSAWVRAKTACEVAEISYKKFR 105

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2008034186 659 KVL----EFYTAFSNHFSRNLLLTYnlrkrivfRKISD 692
Cdd:PRK11753  106 QLIqvnpDILMALSAQMARRLQNTS--------RKVGD 135
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 49-145 1.19e-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: 45.74  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  49 IVYSNDGFCKLSGYHRAEVMQKSSTcsfmygELTDKDSTEKVRLTFENYEM-----NSFEILMYKKNRTPVWFFVKIAPI 123
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRNVL------ELIPEEDREEVRERIERRLEgepepVSEERRVRRKDGSEIWVEVSVSPI 98

                          90       100
                  ....*....|....*....|..
gi 2008034186 124 RNEQEKVVlFLCTFSDITAFKQ 145
Cdd:TIGR00229  99 RTNGGELG-VVGIVRDITERKE 119
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 49-140 1.64e-05

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 44.72  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  49 IVYSNDGFCKLSGYHRAEVMQKSstcsfMYGELTDKDSTEKVRLTFENYEMNS----FEILMYKKNRTPVWFFVKIAPIR 124
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKS-----LLDLIPEEDDAEVAELLRQALLQGEesrgFEVSFRVPDGRPRHVEVRASPVR 97

                          90
                  ....*....|....*.
gi 2008034186 125 NEQEKVVLFLCTFSDI 140
Cdd:pfam00989  98 DAGGEILGFLGVLRDI 113
PAS COG2202
PAS domain [Signal transduction mechanisms];
49-145 6.54e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.79  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  49 IVYSNDGFCKLSGYHRAEVMQKSSTcsfmygELTDKDSTEKVRLTFENY---EMNSFEILMYKKNRTPVWFFVKIAPIRN 125
Cdd:COG2202   159 ILYVNPAAEELLGYSPEELLGKSLL------DLLHPEDRERLLELLRRLlegGRESYELELRLKDGDGRWVWVEASAVPL 232

                          90       100
                  ....*....|....*....|.
gi 2008034186 126 EQE-KVVLFLCTFSDITAFKQ 145
Cdd:COG2202   233 RDGgEVIGVLGIVRDITERKR 253
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 49-136 7.45e-04

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: 39.63  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  49 IVYSNDGFCKLSGYHRAEVMQKSSTC-SFMYGEltDKdstEKVRLTFENYEMN----SFEILMYKKNRTPVWFFVKIAPI 123
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWlDLVHPD--DR---ERVREALWEALKGgepySGEYRIRRKDGEYRWVEARARPI 75

                          90
                  ....*....|...
gi 2008034186 124 RNEQEKVVLFLCT 136
Cdd:pfam08447  76 RDENGKPVRVIGV 88
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
49-145 1.58e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 41.76  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008034186  49 IVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDSTEKVRltfENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQE 128
Cdd:COG3852    29 ITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALA---EGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEG 105

                          90
                  ....*....|....*..
gi 2008034186 129 KvVLFLCTFSDITAFKQ 145
Cdd:COG3852   106 E-GGVLLVLRDITERKR 121
PRK10537 PRK10537
voltage-gated potassium channel protein;
432-478 2.62e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 41.16  E-value: 2.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2008034186 432 TSLYFTMTSLTSIGFGNIAPTTDGEKIFAVAMMMIGSLLYAT----IFGNV 478
Cdd:PRK10537  171 TAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
 
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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