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Conserved domains on  [gi|320542083|ref|NP_001188592|]
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ether a go-go, isoform D [Drosophila melanogaster]

Protein Classification

potassium voltage-gated channel protein( domain architecture ID 12140963)

potassium voltage-gated channel protein is the pore-forming (alpha) subunit of a voltage-gated potassium channel that mediates the potassium permeability of membranes and may be modulated by cAMP and subunit assembly

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
236-497 2.15e-39

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: 146.64  E-value: 2.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   236 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 314
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   315 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 392
Cdd:pfam00520   70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   393 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 465
Cdd:pfam00520  148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205
                          250       260       270
                   ....*....|....*....|....*....|..
gi 320542083   466 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 497
Cdd:pfam00520  206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
569-680 2.86e-19

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: 84.68  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  569 AFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQFWKDsaVG 643
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLG--NG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542083  644 QSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFA 680
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 ...
40-153 3.56e-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: 77.89  E-value: 3.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083    40 DFPIVYCNESFCKISGYNRAEVMQKSCRCGFmygelTDKETVGRLEYTLEN-QQQDQFEILLYKKNNlqcgcalsqfgka 118
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALREgKAVREFEVVLYRKDG------------- 62
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320542083   119 qtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDITA 153
Cdd:pfam13426   63 ----EPFPVLVSLAPIRDDGGELVGIIAILRDITE 93
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
236-497 2.15e-39

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: 146.64  E-value: 2.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   236 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 314
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   315 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 392
Cdd:pfam00520   70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   393 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 465
Cdd:pfam00520  148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205
                          250       260       270
                   ....*....|....*....|....*....|..
gi 320542083   466 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 497
Cdd:pfam00520  206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
237-634 1.09e-36

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 150.02  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  237 WDWVILCLTFYTAIMVPYNVAFKNkTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEV-VSDPKVIRMNYLKSWFI 315
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLN-ASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  316 IDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRyLE------YGAAMLILLLCFYMLVAHWLACIWY 389
Cdd:PLN03192  143 MDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTR-LEkdirfsYFWIRCARLLSVTLFLVHCAGCLYY 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  390 SIgrsdADNGIQYSWLWKLANVTQSPYSYIWSNdtgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEKVFTI 469
Cdd:PLN03192  222 LI----ADRYPHQGKTWIGAVIPNFRETSLWIR---------------YISAIYWSITTMTTVGYGDLHAVNTIEMIFII 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  470 CMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYVVSTWAmTKGLDTEKVLNYCPK 549
Cdd:PLN03192  283 FYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPK 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  550 DMKADICVHLNRKVFNEHPAFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVI----QDDEVVAI 625
Cdd:PLN03192  362 SICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGT 441

                  ....*....
gi 320542083  626 LGKGDVFGD 634
Cdd:PLN03192  442 LGCGDIFGE 450
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
569-680 2.86e-19

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: 84.68  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  569 AFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQFWKDsaVG 643
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLG--NG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542083  644 QSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFA 680
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 ...
40-153 3.56e-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: 77.89  E-value: 3.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083    40 DFPIVYCNESFCKISGYNRAEVMQKSCRCGFmygelTDKETVGRLEYTLEN-QQQDQFEILLYKKNNlqcgcalsqfgka 118
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALREgKAVREFEVVLYRKDG------------- 62
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320542083   119 qtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDITA 153
Cdd:pfam13426   63 ----EPFPVLVSLAPIRDDGGELVGIIAILRDITE 93
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
570-734 8.95e-15

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: 74.64  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  570 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDqfwkDSAVGQ 644
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGE----LSLLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  645 --SAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSF----ARNLVLTYNLRHRLIFRKVAD--VKREKELAERRKNEPQ 716
Cdd:COG0664    77 epSPATAEALEDSELLRIPREDLEELLERNPELARALlrllARRLRQLQERLVSLAFLSAEErlARFLLELADRLDGRID 156
                         170       180
                  ....*....|....*....|....*...
gi 320542083  717 LPQNQDHL----------VRKIFSKFRR 734
Cdd:COG0664   157 LPLTQEEIasylgltretVSRILKKLEK 184
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-156 2.16e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.68  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   40 DFPIVYCNESFCKISGYNRAEVMQKSCRcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNlqcgcalsqfgkaq 119
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG-------------- 93
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542083  120 tqeTPLWLLLQVAPIRNERDLVVLFLLTFRDITALKQ 156
Cdd:COG2202    94 ---SLFWVELSISPVRDEDGEITGFVGIARDITERKR 127
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
591-670 3.64e-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: 60.70  E-value: 3.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   591 APGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQfwkdSAVGQ--SAANVRALTYCDLHAIKRD 663
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGepRSATVVALTDSELLVIPRE 80

                   ....*..
gi 320542083   664 KLLEVLD 670
Cdd:pfam00027   81 DFLELLE 87
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
570-683 6.11e-11

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: 60.88  E-value: 6.11e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083    570 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGdqfwkDSAV-- 642
Cdd:smart00100    2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFG-----ELALlt 76
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 320542083    643 -GQSAANVRALTYCdLHAIKRDKLLEVLDFYSAFANSFARNL 683
Cdd:smart00100   77 nSRRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELL 117
PRK13558 PRK13558
bacterio-opsin activator; Provisional
33-156 1.18e-10

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 66.01  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNlqcgcal 112
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCR--FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDG------- 233
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 320542083  113 sqfgkaqtqeTPLWLLLQVAPIRNErDLVVLFLLTFR-DITALKQ 156
Cdd:PRK13558  234 ----------STFWNQVDIAPIRDE-DGTVTHYVGFQtDVTERKE 267
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
596-700 1.35e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  596 LYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQ--FWKDSavgQSAANVRALTYCDLHAIKRDKLLEV 668
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELglFEEGQ---ERSAWVRAKTACEVAEISYKKFRQL 107
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 320542083  669 L----DFYSAFANSFARNLVLTYNLRHRLIFRKVAD 700
Cdd:PRK11753  108 IqvnpDILMALSAQMARRLQNTSRKVGDLAFLDVTG 143
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
40-151 2.09e-06

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 47.63  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   40 DFPIVYCNESFCKISGYNRAEVMQKSCrcgFMYGELTDKETVG-RLEYTLENQQQDQFEILLYKKNNlqcgcalsqfgka 118
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKSL---LDLIHPEDREELReRLENLLSGGEPVTLEVRLRRKDG------------- 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 320542083  119 qtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDI 151
Cdd:cd00130    75 ----SVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
123-154 3.91e-03

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: 36.39  E-value: 3.91e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 320542083    123 TPLWLLLQVAPIRNERDLVVLFLLTFRDITAL 154
Cdd:smart00086   12 SYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
593-692 7.52e-03

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: 39.88  E-value: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   593 GDLLYHTGESIDSLCFIVTGSLEV-IQDDE---VVAILGKGDVFGDQFWKDSAVgQSAANVRALTYCDLHAIKRDKLLEV 668
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILGETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAAK 247
                           90       100
                   ....*....|....*....|....
gi 320542083   669 LDFYSAFANSFARNLVLTYNLRHR 692
Cdd:TIGR03896  248 LQQDVGFASRFYRVIASLLSQRSR 271
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
236-497 2.15e-39

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: 146.64  E-value: 2.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   236 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 314
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   315 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 392
Cdd:pfam00520   70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   393 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 465
Cdd:pfam00520  148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205
                          250       260       270
                   ....*....|....*....|....*....|..
gi 320542083   466 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 497
Cdd:pfam00520  206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
237-634 1.09e-36

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 150.02  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  237 WDWVILCLTFYTAIMVPYNVAFKNkTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEV-VSDPKVIRMNYLKSWFI 315
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLN-ASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  316 IDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRyLE------YGAAMLILLLCFYMLVAHWLACIWY 389
Cdd:PLN03192  143 MDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTR-LEkdirfsYFWIRCARLLSVTLFLVHCAGCLYY 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  390 SIgrsdADNGIQYSWLWKLANVTQSPYSYIWSNdtgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEKVFTI 469
Cdd:PLN03192  222 LI----ADRYPHQGKTWIGAVIPNFRETSLWIR---------------YISAIYWSITTMTTVGYGDLHAVNTIEMIFII 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  470 CMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYVVSTWAmTKGLDTEKVLNYCPK 549
Cdd:PLN03192  283 FYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPK 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  550 DMKADICVHLNRKVFNEHPAFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVI----QDDEVVAI 625
Cdd:PLN03192  362 SICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGT 441

                  ....*....
gi 320542083  626 LGKGDVFGD 634
Cdd:PLN03192  442 LGCGDIFGE 450
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
569-680 2.86e-19

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: 84.68  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  569 AFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQFWKDsaVG 643
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLG--NG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542083  644 QSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFA 680
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 ...
40-153 3.56e-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: 77.89  E-value: 3.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083    40 DFPIVYCNESFCKISGYNRAEVMQKSCRCGFmygelTDKETVGRLEYTLEN-QQQDQFEILLYKKNNlqcgcalsqfgka 118
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALREgKAVREFEVVLYRKDG------------- 62
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320542083   119 qtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDITA 153
Cdd:pfam13426   63 ----EPFPVLVSLAPIRDDGGELVGIIAILRDITE 93
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
570-734 8.95e-15

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: 74.64  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  570 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDqfwkDSAVGQ 644
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGE----LSLLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  645 --SAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSF----ARNLVLTYNLRHRLIFRKVAD--VKREKELAERRKNEPQ 716
Cdd:COG0664    77 epSPATAEALEDSELLRIPREDLEELLERNPELARALlrllARRLRQLQERLVSLAFLSAEErlARFLLELADRLDGRID 156
                         170       180
                  ....*....|....*....|....*...
gi 320542083  717 LPQNQDHL----------VRKIFSKFRR 734
Cdd:COG0664   157 LPLTQEEIasylgltretVSRILKKLEK 184
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-156 2.16e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.68  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   40 DFPIVYCNESFCKISGYNRAEVMQKSCRcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNlqcgcalsqfgkaq 119
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG-------------- 93
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542083  120 tqeTPLWLLLQVAPIRNERDLVVLFLLTFRDITALKQ 156
Cdd:COG2202    94 ---SLFWVELSISPVRDEDGEITGFVGIARDITERKR 127
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
591-670 3.64e-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: 60.70  E-value: 3.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   591 APGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQfwkdSAVGQ--SAANVRALTYCDLHAIKRD 663
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGepRSATVVALTDSELLVIPRE 80

                   ....*..
gi 320542083   664 KLLEVLD 670
Cdd:pfam00027   81 DFLELLE 87
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
570-683 6.11e-11

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: 60.88  E-value: 6.11e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083    570 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGdqfwkDSAV-- 642
Cdd:smart00100    2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFG-----ELALlt 76
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 320542083    643 -GQSAANVRALTYCdLHAIKRDKLLEVLDFYSAFANSFARNL 683
Cdd:smart00100   77 nSRRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELL 117
PRK13558 PRK13558
bacterio-opsin activator; Provisional
33-156 1.18e-10

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 66.01  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNlqcgcal 112
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCR--FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDG------- 233
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 320542083  113 sqfgkaqtqeTPLWLLLQVAPIRNErDLVVLFLLTFR-DITALKQ 156
Cdd:PRK13558  234 ----------STFWNQVDIAPIRDE-DGTVTHYVGFQtDVTERKE 267
PRK13559 PRK13559
hypothetical protein; Provisional
33-152 1.03e-09

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 61.76  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNlqcgcal 112
Cdd:PRK13559   58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCR--FLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDG------- 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 320542083  113 sqfgkaqtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDIT 152
Cdd:PRK13559  129 ----------EPFWNALHLGPVYGEDGRLLYFFGSQWDVT 158
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
438-492 3.18e-08

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: 51.88  E-value: 3.18e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 320542083   438 YVTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYATIFGHVTTIIQQ 492
Cdd:pfam07885   24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK13557 PRK13557
histidine kinase; Provisional
40-144 8.51e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 56.60  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   40 DFPIVYCNESFCKISGYNRAEVMQKSCRcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNlqcgcalSQFgkaq 119
Cdd:PRK13557   52 DNPIVFANRAFLEMTGYAAEEIIGNNCR--FLQGPETDRATVAEVRDAIAERREIATEILNYRKDG-------SSF---- 118
                          90       100
                  ....*....|....*....|....*.
gi 320542083  120 tqetplWLLLQVAPIRNER-DLVVLF 144
Cdd:PRK13557  119 ------WNALFVSPVYNDAgDLVYFF 138
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
596-700 1.35e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083  596 LYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQ--FWKDSavgQSAANVRALTYCDLHAIKRDKLLEV 668
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELglFEEGQ---ERSAWVRAKTACEVAEISYKKFRQL 107
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 320542083  669 L----DFYSAFANSFARNLVLTYNLRHRLIFRKVAD 700
Cdd:PRK11753  108 IqvnpDILMALSAQMARRLQNTSRKVGDLAFLDVTG 143
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
43-151 1.38e-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. 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: 48.18  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083    43 IVYCNESFCKISGYNRAEVMQKScrcgfMYGEL---TDKETVGRLEYTLENQQQDQ-FEILLYKKNNlqcgcalsqfgka 118
Cdd:pfam00989   23 ILYVNAAAEELLGLSREEVIGKS-----LLDLIpeeDDAEVAELLRQALLQGEESRgFEVSFRVPDG------------- 84
                           90       100       110
                   ....*....|....*....|....*....|...
gi 320542083   119 qtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDI 151
Cdd:pfam00989   85 ----RPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
40-151 2.09e-06

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 47.63  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   40 DFPIVYCNESFCKISGYNRAEVMQKSCrcgFMYGELTDKETVG-RLEYTLENQQQDQFEILLYKKNNlqcgcalsqfgka 118
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKSL---LDLIHPEDREELReRLENLLSGGEPVTLEVRLRRKDG------------- 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 320542083  119 qtqeTPLWLLLQVAPIRNERDLVVLFLLTFRDI 151
Cdd:cd00130    75 ----SVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
43-190 5.15e-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: 50.74  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   43 IVYCNESFCKISGYNRAEVMQKscRCGFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNLQcgcalsqfgkaqtqe 122
Cdd:COG5809    37 ILKVNPAAERIFGYTEDELLGT--NILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKR--------------- 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320542083  123 tpLWLLLQVAPIRNERDLVVLFLLTFRDITALKqpiDSEdtkgvlglskfAKLARSVTRSRQFSAHLP 190
Cdd:COG5809   100 --LEFSSKLSPIFDQNGDIEGMLAISRDITERK---RME-----------EALRESEEKFRLIFNHSP 151
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
43-156 2.31e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 48.30  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   43 IVYCNESFCKISGYNRAEVMQKSCRCGFMYgeltDKETVGRLEYTLENQQQ-DQFEILLYKKNNlqcgcalsqfgkaqtq 121
Cdd:COG3852    29 ITYVNPAAERLLGLSAEELLGRPLAELFPE----DSPLRELLERALAEGQPvTEREVTLRRKDG---------------- 88
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 320542083  122 eTPLWLLLQVAPIRNErDLVVLFLLTFRDITALKQ 156
Cdd:COG3852    89 -EERPVDVSVSPLRDA-EGEGGVLLVLRDITERKR 121
PRK10537 PRK10537
voltage-gated potassium channel protein;
439-486 2.53e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 45.01  E-value: 2.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 320542083  439 VTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYAT----IFGHV 486
Cdd:PRK10537  170 STAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
123-154 3.91e-03

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: 36.39  E-value: 3.91e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 320542083    123 TPLWLLLQVAPIRNERDLVVLFLLTFRDITAL 154
Cdd:smart00086   12 SYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
15-93 5.00e-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: 36.99  E-value: 5.00e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320542083     15 FLENIIrrsNSQPDSSFLLANaqivDFPIVYCNESFCKISGYNRAEVMQKScrcgfmYGELTDKETVGRLEYTLENQQQ 93
Cdd:smart00091    2 RLRAIL---ESLPDGIFVLDL----DGRILYANPAAEELLGYSPEELIGKS------LLELIHPEDRERVQEALQRLLS 67
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
593-692 7.52e-03

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: 39.88  E-value: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542083   593 GDLLYHTGESIDSLCFIVTGSLEV-IQDDE---VVAILGKGDVFGDQFWKDSAVgQSAANVRALTYCDLHAIKRDKLLEV 668
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILGETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAAK 247
                           90       100
                   ....*....|....*....|....
gi 320542083   669 LDFYSAFANSFARNLVLTYNLRHR 692
Cdd:TIGR03896  248 LQQDVGFASRFYRVIASLLSQRSR 271
 
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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