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Conserved domains on  [gi|442616380|ref|NP_001259558|]
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ether a go-go, isoform G [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 ...
221-482 3.18e-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: 146.26  E-value: 3.18e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   221 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 299
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   300 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 377
Cdd:pfam00520   70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   378 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 450
Cdd:pfam00520  148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205
                          250       260       270
                   ....*....|....*....|....*....|..
gi 442616380   451 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 482
Cdd:pfam00520  206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
40-138 1.54e-20

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: 87.52  E-value: 1.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGfmygeltDKETVGRLEYTLEN-QQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA-------EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAP 73
                           90       100
                   ....*....|....*....|
gi 442616380   119 IRNERDLVVLFLLTFRDITA 138
Cdd:pfam13426   74 IRDDGGELVGIIAILRDITE 93
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
554-665 2.82e-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: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  554 AFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQFWKDsaVG 628
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLG--NG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 442616380  629 QSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFA 665
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
221-482 3.18e-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: 146.26  E-value: 3.18e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   221 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 299
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   300 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 377
Cdd:pfam00520   70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   378 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 450
Cdd:pfam00520  148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205
                          250       260       270
                   ....*....|....*....|....*....|..
gi 442616380   451 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 482
Cdd:pfam00520  206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
222-619 1.33e-36

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 149.63  E-value: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  222 WDWVILCLTFYTAIMVPYNVAFKNkTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEV-VSDPKVIRMNYLKSWFI 300
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLN-ASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  301 IDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRyLE------YGAAMLILLLCFYMLVAHWLACIWY 374
Cdd:PLN03192  143 MDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTR-LEkdirfsYFWIRCARLLSVTLFLVHCAGCLYY 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  375 SIgrsdADNGIQYSWLWKLANVTQSPYSYIWSNdtgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEKVFTI 454
Cdd:PLN03192  222 LI----ADRYPHQGKTWIGAVIPNFRETSLWIR---------------YISAIYWSITTMTTVGYGDLHAVNTIEMIFII 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  455 CMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYVVSTWAmTKGLDTEKVLNYCPK 534
Cdd:PLN03192  283 FYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPK 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  535 DMKADICVHLNRKVFNEHPAFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVI----QDDEVVAI 610
Cdd:PLN03192  362 SICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGT 441

                  ....*....
gi 442616380  611 LGKGDVFGD 619
Cdd:PLN03192  442 LGCGDIFGE 450
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
40-138 1.54e-20

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: 87.52  E-value: 1.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGfmygeltDKETVGRLEYTLEN-QQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA-------EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAP 73
                           90       100
                   ....*....|....*....|
gi 442616380   119 IRNERDLVVLFLLTFRDITA 138
Cdd:pfam13426   74 IRDDGGELVGIIAILRDITE 93
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
554-665 2.82e-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: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  554 AFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQFWKDsaVG 628
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLG--NG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 442616380  629 QSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFA 665
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-141 1.13e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 84.31  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKTLR----DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105
                          90       100
                  ....*....|....*....|..
gi 442616380  120 RNERDLVVLFLLTFRDITALKQ 141
Cdd:COG2202   106 RDEDGEITGFVGIARDITERKR 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
555-719 9.19e-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: 9.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  555 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDqfwkDSAVGQ 629
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGE----LSLLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  630 --SAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSF----ARNLVLTYNLRHRLIFRKVAD--VKREKELAERRKNEPQ 701
Cdd:COG0664    77 epSPATAEALEDSELLRIPREDLEELLERNPELARALlrllARRLRQLQERLVSLAFLSAEErlARFLLELADRLDGRID 156
                         170       180
                  ....*....|....*....|....*...
gi 442616380  702 LPQNQDHL----------VRKIFSKFRR 719
Cdd:COG0664   157 LPLTQEEIasylgltretVSRILKKLEK 184
PRK13558 PRK13558
bacterio-opsin activator; Provisional
33-141 1.37e-13

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 75.26  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWL 112
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCR----FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWN 238
                          90       100       110
                  ....*....|....*....|....*....|
gi 442616380  113 LLQVAPIRNErDLVVLFLLTFR-DITALKQ 141
Cdd:PRK13558  239 QVDIAPIRDE-DGTVTHYVGFQtDVTERKE 267
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
576-655 3.60e-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: 3.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   576 APGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQfwkdSAVGQ--SAANVRALTYCDLHAIKRD 648
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGepRSATVVALTDSELLVIPRE 80

                   ....*..
gi 442616380   649 KLLEVLD 655
Cdd:pfam00027   81 DFLELLE 87
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
555-668 5.75e-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: 5.75e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    555 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGdqfwkDSAV-- 627
Cdd:smart00100    2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFG-----ELALlt 76
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 442616380    628 -GQSAANVRALTYCdLHAIKRDKLLEVLDFYSAFANSFARNL 668
Cdd:smart00100   77 nSRRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELL 117
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
40-136 1.29e-09

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: 56.49  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   40 DFPIVYCNESFCKISGYNRAEVMQKSCryvcgFMYGELTDKETVG-RLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKSL-----LDLIHPEDREELReRLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTP 85
                          90
                  ....*....|....*...
gi 442616380  119 IRNERDLVVLFLLTFRDI 136
Cdd:cd00130    86 IRDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
43-141 6.42e-07

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: 49.60  E-value: 6.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    43 IVYCNESFCKISGYNRAEVMQKSCRYvcgFMYGELTDkETVGRLEYTLENQQQDQFEILLYK-KNKTPLWLLLQVAPIRN 121
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRNVLE---LIPEEDRE-EVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEVSVSPIRT 100
                           90       100
                   ....*....|....*....|
gi 442616380   122 ERDlVVLFLLTFRDITALKQ 141
Cdd:TIGR00229  101 NGG-ELGVVGIVRDITERKE 119
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
581-685 1.34e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  581 LYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQ--FWKDSavgQSAANVRALTYCDLHAIKRDKLLEV 653
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELglFEEGQ---ERSAWVRAKTACEVAEISYKKFRQL 107
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 442616380  654 L----DFYSAFANSFARNLVLTYNLRHRLIFRKVAD 685
Cdd:PRK11753  108 IqvnpDILMALSAQMARRLQNTSRKVGDLAFLDVTG 143
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
97-139 1.83e-06

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 45.64  E-value: 1.83e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 442616380     97 QFEILLYKKNKTPLWLLLQVAPIRNERDLVVLFLLTFRDITAL 139
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
578-677 7.49e-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: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   578 GDLLYHTGESIDSLCFIVTGSLEV-IQDDE---VVAILGKGDVFGDQFWKDSAVgQSAANVRALTYCDLHAIKRDKLLEV 653
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILGETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAAK 247
                           90       100
                   ....*....|....*....|....
gi 442616380   654 LDFYSAFANSFARNLVLTYNLRHR 677
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 ...
221-482 3.18e-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: 146.26  E-value: 3.18e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   221 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 299
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   300 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 377
Cdd:pfam00520   70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   378 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 450
Cdd:pfam00520  148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205
                          250       260       270
                   ....*....|....*....|....*....|..
gi 442616380   451 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 482
Cdd:pfam00520  206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
222-619 1.33e-36

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 149.63  E-value: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  222 WDWVILCLTFYTAIMVPYNVAFKNkTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEV-VSDPKVIRMNYLKSWFI 300
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLN-ASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  301 IDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRyLE------YGAAMLILLLCFYMLVAHWLACIWY 374
Cdd:PLN03192  143 MDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTR-LEkdirfsYFWIRCARLLSVTLFLVHCAGCLYY 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  375 SIgrsdADNGIQYSWLWKLANVTQSPYSYIWSNdtgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEKVFTI 454
Cdd:PLN03192  222 LI----ADRYPHQGKTWIGAVIPNFRETSLWIR---------------YISAIYWSITTMTTVGYGDLHAVNTIEMIFII 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  455 CMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYVVSTWAmTKGLDTEKVLNYCPK 534
Cdd:PLN03192  283 FYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPK 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  535 DMKADICVHLNRKVFNEHPAFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVI----QDDEVVAI 610
Cdd:PLN03192  362 SICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGT 441

                  ....*....
gi 442616380  611 LGKGDVFGD 619
Cdd:PLN03192  442 LGCGDIFGE 450
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
40-138 1.54e-20

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: 87.52  E-value: 1.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGfmygeltDKETVGRLEYTLEN-QQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA-------EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAP 73
                           90       100
                   ....*....|....*....|
gi 442616380   119 IRNERDLVVLFLLTFRDITA 138
Cdd:pfam13426   74 IRDDGGELVGIIAILRDITE 93
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
554-665 2.82e-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: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  554 AFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQFWKDsaVG 628
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLG--NG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 442616380  629 QSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFA 665
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-141 1.13e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 84.31  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKTLR----DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105
                          90       100
                  ....*....|....*....|..
gi 442616380  120 RNERDLVVLFLLTFRDITALKQ 141
Cdd:COG2202   106 RDEDGEITGFVGIARDITERKR 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
555-719 9.19e-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: 9.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  555 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDqfwkDSAVGQ 629
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGE----LSLLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  630 --SAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSF----ARNLVLTYNLRHRLIFRKVAD--VKREKELAERRKNEPQ 701
Cdd:COG0664    77 epSPATAEALEDSELLRIPREDLEELLERNPELARALlrllARRLRQLQERLVSLAFLSAEErlARFLLELADRLDGRID 156
                         170       180
                  ....*....|....*....|....*...
gi 442616380  702 LPQNQDHL----------VRKIFSKFRR 719
Cdd:COG0664   157 LPLTQEEIasylgltretVSRILKKLEK 184
PRK13558 PRK13558
bacterio-opsin activator; Provisional
33-141 1.37e-13

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 75.26  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWL 112
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCR----FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWN 238
                          90       100       110
                  ....*....|....*....|....*....|
gi 442616380  113 LLQVAPIRNErDLVVLFLLTFR-DITALKQ 141
Cdd:PRK13558  239 QVDIAPIRDE-DGTVTHYVGFQtDVTERKE 267
PRK13559 PRK13559
hypothetical protein; Provisional
33-137 8.59e-13

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 71.39  E-value: 8.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWL 112
Cdd:PRK13559   58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCR----FLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWN 133
                          90       100
                  ....*....|....*....|....*
gi 442616380  113 LLQVAPIRNERDLVVLFLLTFRDIT 137
Cdd:PRK13559  134 ALHLGPVYGEDGRLLYFFGSQWDVT 158
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
576-655 3.60e-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: 3.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   576 APGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQfwkdSAVGQ--SAANVRALTYCDLHAIKRD 648
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGepRSATVVALTDSELLVIPRE 80

                   ....*..
gi 442616380   649 KLLEVLD 655
Cdd:pfam00027   81 DFLELLE 87
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
555-668 5.75e-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: 5.75e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    555 FRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGdqfwkDSAV-- 627
Cdd:smart00100    2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFG-----ELALlt 76
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 442616380    628 -GQSAANVRALTYCdLHAIKRDKLLEVLDFYSAFANSFARNL 668
Cdd:smart00100   77 nSRRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELL 117
PRK13557 PRK13557
histidine kinase; Provisional
40-129 3.39e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 64.31  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:PRK13557   52 DNPIVFANRAFLEMTGYAAEEIIGNNCR----FLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPV 127
                          90
                  ....*....|.
gi 442616380  120 RNER-DLVVLF 129
Cdd:PRK13557  128 YNDAgDLVYFF 138
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
43-136 7.07e-10

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 57.81  E-value: 7.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    43 IVYCNESFCKISGYNRAEVMQKScryvcgfMYGEL---TDKETVGRLEYTLENQQQDQ-FEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam00989   23 ILYVNAAAEELLGLSREEVIGKS-------LLDLIpeeDDAEVAELLRQALLQGEESRgFEVSFRVPDGRPRHVEVRASP 95
                           90
                   ....*....|....*...
gi 442616380   119 IRNERDLVVLFLLTFRDI 136
Cdd:pfam00989   96 VRDAGGEILGFLGVLRDI 113
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
40-136 1.29e-09

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: 56.49  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   40 DFPIVYCNESFCKISGYNRAEVMQKSCryvcgFMYGELTDKETVG-RLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKSL-----LDLIHPEDREELReRLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTP 85
                          90
                  ....*....|....*...
gi 442616380  119 IRNERDLVVLFLLTFRDI 136
Cdd:cd00130    86 IRDEGGEVIGLLGVVRDI 103
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
43-175 5.05e-09

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: 60.37  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   43 IVYCNESFCKISGYNRAEVMQKSCRYVCGFMYgeltDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPIRNE 122
Cdd:COG5809    37 ILKVNPAAERIFGYTEDELLGTNILDFLHPDD----EKELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQ 112
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442616380  123 RDLVVLFLLTFRDITALKqpiDSEdtkgvlglskfAKLARSVTRSRQFSAHLP 175
Cdd:COG5809   113 NGDIEGMLAISRDITERK---RME-----------EALRESEEKFRLIFNHSP 151
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
43-141 5.89e-09

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 59.47  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   43 IVYCNESFCKISGYNRAEVMQKSCRYVCGFmygeltDKETVGRLEYTLENQQQ-DQFEILLYKKNKTPLWLLLQVAPIRN 121
Cdd:COG3852    29 ITYVNPAAERLLGLSAEELLGRPLAELFPE------DSPLRELLERALAEGQPvTEREVTLRRKDGEERPVDVSVSPLRD 102
                          90       100
                  ....*....|....*....|
gi 442616380  122 ErDLVVLFLLTFRDITALKQ 141
Cdd:COG3852   103 A-EGEGGVLLVLRDITERKR 121
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
423-477 3.60e-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: 51.50  E-value: 3.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442616380   423 YVTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYATIFGHVTTIIQQ 477
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 ...
43-141 6.42e-07

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: 49.60  E-value: 6.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    43 IVYCNESFCKISGYNRAEVMQKSCRYvcgFMYGELTDkETVGRLEYTLENQQQDQFEILLYK-KNKTPLWLLLQVAPIRN 121
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRNVLE---LIPEEDRE-EVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEVSVSPIRT 100
                           90       100
                   ....*....|....*....|
gi 442616380   122 ERDlVVLFLLTFRDITALKQ 141
Cdd:TIGR00229  101 NGG-ELGVVGIVRDITERKE 119
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
581-685 1.34e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380  581 LYHTGESIDSLCFIVTGSLEVIQDDE-----VVAILGKGDVFGDQ--FWKDSavgQSAANVRALTYCDLHAIKRDKLLEV 653
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELglFEEGQ---ERSAWVRAKTACEVAEISYKKFRQL 107
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 442616380  654 L----DFYSAFANSFARNLVLTYNLRHRLIFRKVAD 685
Cdd:PRK11753  108 IqvnpDILMALSAQMARRLQNTSRKVGDLAFLDVTG 143
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
97-139 1.83e-06

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 45.64  E-value: 1.83e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 442616380     97 QFEILLYKKNKTPLWLLLQVAPIRNERDLVVLFLLTFRDITAL 139
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-141 6.31e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 49.25  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   16 LENIIRRSNSQPDSSFLLANAQIV----DFPIVYCNESFCKISGYNRAEVMQKSCRYVcgfmYGELTDKETVGRLEYTLE 91
Cdd:COG2202   128 AEEALRESEERLRLLVENAPDGIFvldlDGRILYVNPAAEELLGYSPEELLGKSLLDL----LHPEDRERLLELLRRLLE 203
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442616380   92 NQQQdQFEILLYKKNKTPLWLLLQVAPIRNE-RDLVVLFLLTFRDITALKQ 141
Cdd:COG2202   204 GGRE-SYELELRLKDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKR 253
PRK10537 PRK10537
voltage-gated potassium channel protein;
424-471 2.70e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 45.01  E-value: 2.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442616380  424 VTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYAT----IFGHV 471
Cdd:PRK10537  170 STAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
40-141 3.83e-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: 41.25  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380    40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgfmygELTDKETVGRLEYTL-----ENQQQDQFEILLYkkNKTPLWLLL 114
Cdd:pfam08448   14 DGRVRYANAAAAELFGLPPEELLGKTLA--------ELLPPEDAARLERALrraleGEEPIDFLEELLL--NGEERHYEL 83
                           90       100
                   ....*....|....*....|....*..
gi 442616380   115 QVAPIRNERDLVVLFLLTFRDITALKQ 141
Cdd:pfam08448   84 RLTPLRDPDGEVIGVLVISRDITERRR 110
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
43-141 5.93e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 44.38  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   43 IVYCNESFCKISGYNRAEVMQKScryVCGFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPIRNE 122
Cdd:PRK11359  158 IVQCNRAFTEMFGYCISEASGMQ---PDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDV 234
                          90
                  ....*....|....*....
gi 442616380  123 RDLVVLFLLTFRDITALKQ 141
Cdd:PRK11359  235 LAHLQNLVMTFSDITEERQ 253
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
40-141 7.86e-04

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: 43.42  E-value: 7.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGFMYGELTDKetvgRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:COG5809   160 DGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAA----FISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI 235
                          90       100
                  ....*....|....*....|..
gi 442616380  120 rNERDLVVLFLLTFRDITALKQ 141
Cdd:COG5809   236 -KKNGEVDGIVIIFRDITERKK 256
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
578-677 7.49e-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: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   578 GDLLYHTGESIDSLCFIVTGSLEV-IQDDE---VVAILGKGDVFGDQFWKDSAVgQSAANVRALTYCDLHAIKRDKLLEV 653
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLsISPDGpgrEVGSSRRGEILGETPFLNGSL-PGTATVKAIENSVLLAIDKQQLAAK 247
                           90       100
                   ....*....|....*....|....
gi 442616380   654 LDFYSAFANSFARNLVLTYNLRHR 677
Cdd:TIGR03896  248 LQQDVGFASRFYRVIASLLSQRSR 271
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
43-141 9.66e-03

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: 40.14  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616380   43 IVYCNESFCKISGYNRAEVMQKSCRYVcgfmYGELTDKETVgrleytlenQQQDQFEILLYKKNKTPLWLLLQVAPIRnE 122
Cdd:COG3829    33 ITYVNRAAERILGLPREEVIGKNVTEL----IPNSPLLEVL---------KTGKPVTGVIQKTGGKGKTVIVTAIPIF-E 98
                          90
                  ....*....|....*....
gi 442616380  123 RDLVVLFLLTFRDITALKQ 141
Cdd:COG3829    99 DGEVIGAVETFRDITELKR 117
 
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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