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Conserved domains on  [gi|71989969|ref|NP_503402|]
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Potassium voltage-gated channel protein eag [Caenorhabditis elegans]

Protein Classification

cyclic nucleotide-gated ion channel; ion transporter( domain architecture ID 13822764)

cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP| ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium, across cell membranes

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
 189-632 3.31e-33

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 138.08  E-value: 3.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  189 LGGdmlPQYRQETPKTSPHIILHYSSFKTIWDWSILALTFYTAFMVPFNIAFKNSlrpfylissreNPGGGIDsvaLMDS 268
Cdd:PLN03192  37 LGV---PSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNA-----------SPKRGLE---IADN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  269 IVDVIFFADILLNFHTTFVGPGGEVVI-EPSVIRQNYFKSWFLIDLLSCLPYDIFYMFKRDDERIGSLFSALKVVRLLRL 347
Cdd:PLN03192 100 VVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  348 GRVaRKLDNYLE------YGAATLLLLLCAYVIVAHWLACVWFWIGDSEVRLKMDnlalpdgWLWKLSNDLRQhynipls 421
Cdd:PLN03192 180 RRV-KQLFTRLEkdirfsYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKT-------WIGAVIPNFRE------- 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  422 nkttlvggPSRTSAYISSLYYTMSCMSTVGFGNI-ASNTdNEKIFGVCMMIISALLYAAIFGHMTTIIQQMTSSTVRYHE 500
Cdd:PLN03192 245 --------TSLWIRYISAIYWSITTMTTVGYGDLhAVNT-IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRN 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  501 MISNVREFIKLQEIPKELAERVMDYVVSTWAmTKGIDTAKVLGYCPKDMKADICVHLNRKVFNEHSCFRLASDGCLRSLA 580
Cdd:PLN03192 316 SIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLV 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71989969  581 MFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVI----QDDEVVAILGKGDVFGD 632
Cdd:PLN03192 395 TKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGE 450
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 39-134 8.81e-17

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: 76.35  E-value: 8.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHgevgsLQKMQEALENARTEQA-EIGLCKKNKTPIWLLVHLAPIK 117
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPED-----SERLREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*..
gi 71989969   118 NHKDAVVLYLCQFKDIT 134
Cdd:pfam13426  76 DDGGELVGIIAILRDIT 92
cyc_nuc_ocin super family cl28242
bacteriocin-type transport-associated protein; Members of this protein family are ...
 591-691 4.10e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


The actual alignment was detected with superfamily member TIGR03896:

Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 43.73  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   591 GDLLYHTGESVDALWFVVSGSLEV-IQDDE---VVAILGKGDVFGdEFWKANGSTgQSAANVRALTYSDLHMIKKDKLMD 666
Cdd:TIGR03896 169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILG-ETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAA 246

                          90       100
                  ....*....|....*....|....*
gi 71989969   667 VLDFYKAFANSFARnmTLTYNLTHR 691
Cdd:TIGR03896 247 KLQQDVGFASRFYR--VIASLLSQR 269
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 189-632 3.31e-33

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 138.08  E-value: 3.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  189 LGGdmlPQYRQETPKTSPHIILHYSSFKTIWDWSILALTFYTAFMVPFNIAFKNSlrpfylissreNPGGGIDsvaLMDS 268
Cdd:PLN03192  37 LGV---PSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNA-----------SPKRGLE---IADN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  269 IVDVIFFADILLNFHTTFVGPGGEVVI-EPSVIRQNYFKSWFLIDLLSCLPYDIFYMFKRDDERIGSLFSALKVVRLLRL 347
Cdd:PLN03192 100 VVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  348 GRVaRKLDNYLE------YGAATLLLLLCAYVIVAHWLACVWFWIGDSEVRLKMDnlalpdgWLWKLSNDLRQhynipls 421
Cdd:PLN03192 180 RRV-KQLFTRLEkdirfsYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKT-------WIGAVIPNFRE------- 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  422 nkttlvggPSRTSAYISSLYYTMSCMSTVGFGNI-ASNTdNEKIFGVCMMIISALLYAAIFGHMTTIIQQMTSSTVRYHE 500
Cdd:PLN03192 245 --------TSLWIRYISAIYWSITTMTTVGYGDLhAVNT-IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRN 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  501 MISNVREFIKLQEIPKELAERVMDYVVSTWAmTKGIDTAKVLGYCPKDMKADICVHLNRKVFNEHSCFRLASDGCLRSLA 580
Cdd:PLN03192 316 SIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLV 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71989969  581 MFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVI----QDDEVVAILGKGDVFGD 632
Cdd:PLN03192 395 TKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGE 450
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 218-495 8.39e-27

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: 110.05  E-value: 8.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   218 IWDWSILALTFYTAFMVPFNIAFKNSLRPFYLIssrenpgggidsvALMDSIVDVIFFADILLNFHTTFvgpggevviep 297
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEPLTTVL-------------EILDYVFTGIFTLEMLLKIIAAG----------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   298 svIRQNYFKS-WFLIDLLSCLPYDIFYMFkrDDERIGSLFSALKVVRLLRLGRVARKLDNY--LEYGAATLLLLLCAYVI 374
Cdd:pfam00520  59 --FKKRYFRSpWNILDFVVVLPSLISLVL--SSVGSLSGLRVLRLLRLLRLLRLIRRLEGLrtLVNSLIRSLKSLGNLLL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   375 VAHWLACVWFWIGDSEVRLKMDNLALPDGWLWKLSNdlrqhyniplsnkttlvggpsrtsaYISSLYYTMSCMSTVGFGN 454
Cdd:pfam00520 135 LLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDN-------------------------FPNAFLWLFQTMTTEGWGD 189

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 71989969   455 IASNTDNEK-------IFGVCMMIISALLYAAIFGHMTTIIQQMTSST 495
Cdd:pfam00520 190 IMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 568-679 9.57e-21

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: 88.54  E-value: 9.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969 568 FRLASDGCLRSLAMFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEFWKANgstG 642
Cdd:cd00038   2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGN---G 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71989969 643 QSAANVRALTYSDLHMIKKDKLMDVLDFYKAFANSFA 679
Cdd:cd00038  79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 39-134 8.81e-17

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: 76.35  E-value: 8.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHgevgsLQKMQEALENARTEQA-EIGLCKKNKTPIWLLVHLAPIK 117
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPED-----SERLREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*..
gi 71989969   118 NHKDAVVLYLCQFKDIT 134
Cdd:pfam13426  76 DDGGELVGIIAILRDIT 92
PAS COG2202
PAS domain [Signal transduction mechanisms];
39-138 4.21e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 73.52  E-value: 4.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLaFMHGEHGEvGSLQKMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKN 118
Cdd:COG2202  30 DGRILYVNPAFERLTGYSAEELLGKTLRD-LLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                        90       100
                ....*....|....*....|
gi 71989969 119 HKDAVVLYLCQFKDITPLKQ 138
Cdd:COG2202 108 EDGEITGFVGIARDITERKR 127
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 568-682 2.86e-13

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: 67.43  E-value: 2.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    568 FRLASDGCLRSLAMFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEfwkANGSTG 642
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGEL---ALLTNS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 71989969    643 QSAANVRALTYSdLHMIKKDKLMDVLDFYKAFANSFARNM 682
Cdd:smart00100  79 RRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 568-682 1.28e-12

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: 67.70  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969 568 FRLASDGCLRSLAMFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEFWKANGStg 642
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEP-- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71989969 643 qSAANVRALTYSDLHMIKKDKLMDVLDFYKAFANSFARNM 682
Cdd:COG0664  79 -SPATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-133 9.87e-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: 59.57  E-value: 9.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  42 IVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHGEVgsLQKMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKNHKD 121
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREEL--RERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                        90
                ....*....|..
gi 71989969 122 AVVLYLCQFKDI 133
Cdd:cd00130  92 EVIGLLGVVRDI 103
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 21-138 1.06e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 56.00  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   21 RRCNNADTSFILANAQVVDYPIVYCNDGFSKLVGYTRAEIMQKPCSlaFMHGEHGEVGSLQKMQEALENARTEQAEIGLC 100
Cdd:PRK13558 152 RALDEAPVGITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCR--FLQGEDTNEERVAELREAIDEERPTSVELRNY 229

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71989969  101 KKNKTPIWLLVHLAPIKNhKDAVVLYLCQFK-DITPLKQ 138
Cdd:PRK13558 230 RKDGSTFWNQVDIAPIRD-EDGTVTHYVGFQtDVTERKE 267
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 42-138 1.05e-06

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 48.44  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    42 IVYCNDGFSKLVGYTRAEIMQKPcSLAFMHGEHgevgsLQKMQEALENARTEQAEI-----GLCKKNKTPIWLLVHLAPI 116
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRN-VLELIPEED-----REEVRERIERRLEGEPEPvseerRVRRKDGSEIWVEVSVSPI 98

                          90       100
                  ....*....|....*....|..
gi 71989969   117 KNHKDaVVLYLCQFKDITPLKQ 138
Cdd:TIGR00229  99 RTNGG-ELGVVGIVRDITERKE 119
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 591-691 4.10e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 43.73  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   591 GDLLYHTGESVDALWFVVSGSLEV-IQDDE---VVAILGKGDVFGdEFWKANGSTgQSAANVRALTYSDLHMIKKDKLMD 666
Cdd:TIGR03896 169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILG-ETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAA 246

                          90       100
                  ....*....|....*....|....*
gi 71989969   667 VLDFYKAFANSFARnmTLTYNLTHR 691
Cdd:TIGR03896 247 KLQQDVGFASRFYR--VIASLLSQR 269
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 96-134 6.34e-04

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: 38.32  E-value: 6.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 71989969     96 EIGLCKKNKTPIWLLVHLAPIKNHKDAVVLYLCQFKDIT 134
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 189-632 3.31e-33

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 138.08  E-value: 3.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  189 LGGdmlPQYRQETPKTSPHIILHYSSFKTIWDWSILALTFYTAFMVPFNIAFKNSlrpfylissreNPGGGIDsvaLMDS 268
Cdd:PLN03192  37 LGV---PSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNA-----------SPKRGLE---IADN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  269 IVDVIFFADILLNFHTTFVGPGGEVVI-EPSVIRQNYFKSWFLIDLLSCLPYDIFYMFKRDDERIGSLFSALKVVRLLRL 347
Cdd:PLN03192 100 VVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  348 GRVaRKLDNYLE------YGAATLLLLLCAYVIVAHWLACVWFWIGDSEVRLKMDnlalpdgWLWKLSNDLRQhynipls 421
Cdd:PLN03192 180 RRV-KQLFTRLEkdirfsYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKT-------WIGAVIPNFRE------- 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  422 nkttlvggPSRTSAYISSLYYTMSCMSTVGFGNI-ASNTdNEKIFGVCMMIISALLYAAIFGHMTTIIQQMTSSTVRYHE 500
Cdd:PLN03192 245 --------TSLWIRYISAIYWSITTMTTVGYGDLhAVNT-IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRN 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  501 MISNVREFIKLQEIPKELAERVMDYVVSTWAmTKGIDTAKVLGYCPKDMKADICVHLNRKVFNEHSCFRLASDGCLRSLA 580
Cdd:PLN03192 316 SIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLV 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71989969  581 MFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVI----QDDEVVAILGKGDVFGD 632
Cdd:PLN03192 395 TKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGE 450
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 218-495 8.39e-27

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: 110.05  E-value: 8.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   218 IWDWSILALTFYTAFMVPFNIAFKNSLRPFYLIssrenpgggidsvALMDSIVDVIFFADILLNFHTTFvgpggevviep 297
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEPLTTVL-------------EILDYVFTGIFTLEMLLKIIAAG----------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   298 svIRQNYFKS-WFLIDLLSCLPYDIFYMFkrDDERIGSLFSALKVVRLLRLGRVARKLDNY--LEYGAATLLLLLCAYVI 374
Cdd:pfam00520  59 --FKKRYFRSpWNILDFVVVLPSLISLVL--SSVGSLSGLRVLRLLRLLRLLRLIRRLEGLrtLVNSLIRSLKSLGNLLL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   375 VAHWLACVWFWIGDSEVRLKMDNLALPDGWLWKLSNdlrqhyniplsnkttlvggpsrtsaYISSLYYTMSCMSTVGFGN 454
Cdd:pfam00520 135 LLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDN-------------------------FPNAFLWLFQTMTTEGWGD 189

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 71989969   455 IASNTDNEK-------IFGVCMMIISALLYAAIFGHMTTIIQQMTSST 495
Cdd:pfam00520 190 IMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 568-679 9.57e-21

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: 88.54  E-value: 9.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969 568 FRLASDGCLRSLAMFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEFWKANgstG 642
Cdd:cd00038   2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGN---G 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71989969 643 QSAANVRALTYSDLHMIKKDKLMDVLDFYKAFANSFA 679
Cdd:cd00038  79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 39-134 8.81e-17

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: 76.35  E-value: 8.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHgevgsLQKMQEALENARTEQA-EIGLCKKNKTPIWLLVHLAPIK 117
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPED-----SERLREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*..
gi 71989969   118 NHKDAVVLYLCQFKDIT 134
Cdd:pfam13426  76 DDGGELVGIIAILRDIT 92
PAS COG2202
PAS domain [Signal transduction mechanisms];
39-138 4.21e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 73.52  E-value: 4.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLaFMHGEHGEvGSLQKMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKN 118
Cdd:COG2202  30 DGRILYVNPAFERLTGYSAEELLGKTLRD-LLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                        90       100
                ....*....|....*....|
gi 71989969 119 HKDAVVLYLCQFKDITPLKQ 138
Cdd:COG2202 108 EDGEITGFVGIARDITERKR 127
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 568-682 2.86e-13

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: 67.43  E-value: 2.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    568 FRLASDGCLRSLAMFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEfwkANGSTG 642
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGEL---ALLTNS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 71989969    643 QSAANVRALTYSdLHMIKKDKLMDVLDFYKAFANSFARNM 682
Cdd:smart00100  79 RRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 568-682 1.28e-12

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: 67.70  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969 568 FRLASDGCLRSLAMFLELNHAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEFWKANGStg 642
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEP-- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71989969 643 qSAANVRALTYSDLHMIKKDKLMDVLDFYKAFANSFARNM 682
Cdd:COG0664  79 -SPATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 587-669 1.53e-11

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: 61.09  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   587 HAAPGDLLYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGDEfwkANGSTGQSAANVRALTYSDLHMIKK 661
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL---ALLGGEPRSATVVALTDSELLVIPR 79


                  ....*...
gi 71989969   662 DKLMDVLD 669
Cdd:pfam00027  80 EDFLELLE 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-133 9.87e-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: 59.57  E-value: 9.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  42 IVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHGEVgsLQKMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKNHKD 121
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREEL--RERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                        90
                ....*....|..
gi 71989969 122 AVVLYLCQFKDI 133
Cdd:cd00130  92 EVIGLLGVVRDI 103
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-133 3.23e-08

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 52.42  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    42 IVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHGEV-GSLQKMQEALENARTEqaEIGLCKKNKTPIWLLVHLAPIKNHK 120
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVaELLRQALLQGEESRGF--EVSFRVPDGRPRHVEVRASPVRDAG 100

                          90
                  ....*....|...
gi 71989969   121 DAVVLYLCQFKDI 133
Cdd:pfam00989 101 GEILGFLGVLRDI 113
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 21-138 1.06e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 56.00  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   21 RRCNNADTSFILANAQVVDYPIVYCNDGFSKLVGYTRAEIMQKPCSlaFMHGEHGEVGSLQKMQEALENARTEQAEIGLC 100
Cdd:PRK13558 152 RALDEAPVGITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCR--FLQGEDTNEERVAELREAIDEERPTSVELRNY 229

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71989969  101 KKNKTPIWLLVHLAPIKNhKDAVVLYLCQFK-DITPLKQ 138
Cdd:PRK13558 230 RKDGSTFWNQVDIAPIRD-EDGTVTHYVGFQtDVTERKE 267
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
9-138 1.18e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 54.85  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   9 VAPQNTFLENVIrrcNNADTSFILANAQVVdypIVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHgevgSLQKMQEALE 88
Cdd:COG3852   2 LRESEELLRAIL---DSLPDAVIVLDADGR---ITYVNPAAERLLGLSAEELLGRPLAELFPEDSP----LRELLERALA 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71989969  89 NARTE-QAEIGLCKKNKTPIWLLVHLAPIKNHkDAVVLYLCQFKDITPLKQ 138
Cdd:COG3852  72 EGQPVtEREVTLRRKDGEERPVDVSVSPLRDA-EGEGGVLLVLRDITERKR 121
PRK13559 PRK13559
hypothetical protein; Provisional
 31-126 2.63e-07

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 53.67  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   31 ILANAQVVDYPIVYCNDGFSKLVGYTRAEIMQKPCSlaFMHGEHGEVGSLQKMQEALENARTEQAEIGLCKKNKTPIWLL 110
Cdd:PRK13559  57 CITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCR--FLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134

                         90
                 ....*....|....*.
gi 71989969  111 VHLAPIKNhKDAVVLY 126
Cdd:PRK13559 135 LHLGPVYG-EDGRLLY 149
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 436-490 6.24e-07

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: 47.65  E-value: 6.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71989969   436 YISSLYYTMSCMSTVGFGNIASNTDNEKIFGVCMMIISALLYAAIFGHMTTIIQQ 490
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 42-138 1.05e-06

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 48.44  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    42 IVYCNDGFSKLVGYTRAEIMQKPcSLAFMHGEHgevgsLQKMQEALENARTEQAEI-----GLCKKNKTPIWLLVHLAPI 116
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRN-VLELIPEED-----REEVRERIERRLEGEPEPvseerRVRRKDGSEIWVEVSVSPI 98

                          90       100
                  ....*....|....*....|..
gi 71989969   117 KNHKDaVVLYLCQFKDITPLKQ 138
Cdd:TIGR00229  99 RTNGG-ELGVVGIVRDITERKE 119
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 39-155 1.42e-06

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: 51.90  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHGEVGSLqkMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKN 118
Cdd:COG5809 160 DGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAF--ISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKK 237

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71989969 119 HKDaVVLYLCQFKDITPLKQPLDD-ENNKGLSRILQIA 155
Cdd:COG5809 238 NGE-VDGIVIIFRDITERKKLEELlRKSEKLSVVGELA 274
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-138 3.58e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 49.64  E-value: 3.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  42 IVYCNDGFSKLVGYTRAEIMQKPCsLAFMHGEHGEVGsLQKMQEALENARtEQAEIGLCKKNKTPIWLLVHLAPIKN-HK 120
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGKSL-LDLLHPEDRERL-LELLRRLLEGGR-ESYELELRLKDGDGRWVWVEASAVPLrDG 235

                        90
                ....*....|....*...
gi 71989969 121 DAVVLYLCQFKDITPLKQ 138
Cdd:COG2202 236 GEVIGVLGIVRDITERKR 253
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 13-167 5.39e-06

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 50.15  E-value: 5.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969  13 NTFLENVIrrcNNADTSFILANAqvvDYPIVYCNDGFSKLVGYTRAEIMQKPCSlafmhgehgEVGSLQKMQEALENART 92
Cdd:COG3829  10 EEELEAIL---DSLDDGIIVVDA---DGRITYVNRAAERILGLPREEVIGKNVT---------ELIPNSPLLEVLKTGKP 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71989969  93 EQAEIglCKKNKTPIWLLVHLAPIKNHkDAVVLYLCQFKDITPLKQpLDDENNKglsriLQIARIAKSKQQFNQI 167
Cdd:COG3829  75 VTGVI--QKTGGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKR-LERKLRE-----EELERGLSAKYTFDDI 140
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-128 6.08e-06

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: 45.41  E-value: 6.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    42 IVYCNDGFSKLVGYTRAEIMQKPCS-LAFMHGEHGEVgSLQKMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKNHK 120
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESwLDLVHPDDRER-VREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79


                  ....*...
gi 71989969   121 DAVVLYLC 128
Cdd:pfam08447  80 GKPVRVIG 87
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 591-691 4.10e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 43.73  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   591 GDLLYHTGESVDALWFVVSGSLEV-IQDDE---VVAILGKGDVFGdEFWKANGSTgQSAANVRALTYSDLHMIKKDKLMD 666
Cdd:TIGR03896 169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILG-ETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAA 246

                          90       100
                  ....*....|....*....|....*
gi 71989969   667 VLDFYKAFANSFARnmTLTYNLTHR 691
Cdd:TIGR03896 247 KLQQDVGFASRFYR--VIASLLSQR 269
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 96-134 6.34e-04

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: 38.32  E-value: 6.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 71989969     96 EIGLCKKNKTPIWLLVHLAPIKNHKDAVVLYLCQFKDIT 134
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 39-138 6.57e-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. 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: 40.09  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969    39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSLAFMHGEHGEVGSLqkMQEALENART-EQAEIGLCkkNKTPIWLLVHLAPIK 117
Cdd:pfam08448  14 DGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERA--LRRALEGEEPiDFLEELLL--NGEERHYELRLTPLR 89

                          90       100
                  ....*....|....*....|.
gi 71989969   118 NHKDAVVLYLCQFKDITPLKQ 138
Cdd:pfam08448  90 DPDGEVIGVLVISRDITERRR 110
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-90 1.20e-03

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 38.15  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 71989969     42 IVYCNDGFSKLVGYTRAEIMQKPCsLAFMHGEHgevgsLQKMQEALENA 90
Cdd:smart00091  23 ILYANPAAEELLGYSPEELIGKSL-LELIHPED-----RERVQEALQRL 65
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 24-145 2.40e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 41.68  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   24 NNADTSFILANAQvvdYPIVYCNDGFSKLVGYTRAEIM-QKPCSlaFMHGEHGEVGSLQKMQEALENARTEQAEIGLCKK 102
Cdd:PRK11359 143 DHLDRPVIVLDPE---RRIVQCNRAFTEMFGYCISEASgMQPDT--LLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTR 217

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 71989969  103 NKTPIWLLVHLAPIKNHKDAVVLYLCQFKDITPLKQPLDDENN 145
Cdd:PRK11359 218 TGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGN 260
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
594-632 2.99e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.96  E-value: 2.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 71989969  594 LYHTGESVDALWFVVSGSLEVIQDDE-----VVAILGKGDVFGD 632
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGE 74
PRK13557 PRK13557
histidine kinase; Provisional
 39-118 4.00e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 40.81  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989969   39 DYPIVYCNDGFSKLVGYTRAEIMQKPCSlaFMHGEHGEVGSLQKMQEALENARTEQAEIGLCKKNKTPIWLLVHLAPIKN 118
Cdd:PRK13557  52 DNPIVFANRAFLEMTGYAAEEIIGNNCR--FLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYN 129
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 595-630 6.91e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 36.08  E-value: 6.91e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 71989969   595 YHTGEsvDALWFVVSGSLEVIQDDEVVaILGKGDVF 630
Cdd:pfam07883  15 RHPGE--DEFFYVLEGEGELTVDGEEV-VLKAGDSV 47
PRK10537 PRK10537
voltage-gated potassium channel protein;
440-502 8.90e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 39.62  E-value: 8.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71989969  440 LYYTMSCMSTVGFGNIASNTDNEKIFGVCMMI---------ISALLYAAIFGHMTTIIQQMTSSTVRYHEMI 502
Cdd:PRK10537 173 FYFSIVTMSTVGYGDIVPVSESARLFTISVIIlgitvfatsISAIFGPVIRGNLKRLVKGRISHMHRKDHFI 244
 
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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