|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
259-645 |
4.63e-31 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 131.14 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192 64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYG-------AAV 400
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWircarllSVT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 401 LFLLM---CTFALIAH--------WLAC---------------------ICSLTSVGFGNVSPNTNSEKVFSICVMLIGS 448
Cdd:PLN03192 210 LFLVHcagCLYYLIADryphqgktWIGAvipnfretslwiryisaiywsITTMTTVGYGDLHAVNTIEMIFIIFYMLFNL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 449 LMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNAVLKGFPECLQADIC 528
Cdd:PLN03192 290 GLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSIC 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 529 LHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----RDDVVVAILGKNDIF 604
Cdd:PLN03192 369 QHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIF 448
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767996066 605 GEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 645
Cdd:PLN03192 449 GEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
258-467 |
3.78e-25 |
|
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: 105.04 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesrrgacsyTCSPLTVVDLIVDIMFVVDIVINFRTTYvntndevvshprrI 337
Cdd:pfam00520 3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 338 AVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520 60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 415 LACICS-------------------------------------LTSVGFGNVSPNTNSEK-------VFSICVMLIGSLM 450
Cdd:pfam00520 139 FLFIFAiigyqlfggklktwenpdngrtnfdnfpnaflwlfqtMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLL 218
|
250
....*....|....*..
gi 767996066 451 YASIFGNVSAIIQRLYS 467
Cdd:pfam00520 219 LNLFIAVIIDNFQELTE 235
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
541-652 |
4.33e-23 |
|
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: 95.09 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 541 AFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPg 615
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 767996066 616 kSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFW 652
Cdd:cd00038 80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
542-641 |
4.44e-19 |
|
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: 83.60 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 542 FSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPVSLHAQPGK 616
Cdd:smart00100 2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81
|
90 100
....*....|....*....|....*
gi 767996066 617 SSADVRALTYCDLHKIQRADLLEVL 641
Cdd:smart00100 82 ASAAAVALELATLLRIDFRDFLQLL 106
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
38-132 |
6.99e-19 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 82.12 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
|
90
....*....|....*.
gi 767996066 117 NEDGAVIMFILNFEDL 132
Cdd:pfam13426 76 DDGGELVGIIAILRDI 91
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
550-656 |
7.40e-16 |
|
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: 77.33 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 550 LRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRAL 624
Cdd:COG0664 9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
|
90 100 110
....*....|....*....|....*....|..
gi 767996066 625 TYCDLHKIQRADLLEVLDMYPAFAESFWSKLE 656
Cdd:COG0664 87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
31-125 |
1.73e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 79.09 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559 58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135
|
90
....*....|....*
gi 767996066 111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559 136 HLGPVYGEDGRLLYF 150
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
41-131 |
6.05e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
|
90
....*....|.
gi 767996066 121 AVIMFILNFED 131
Cdd:COG2202 111 EITGFVGIARD 121
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
41-132 |
1.37e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 53.41 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130 14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
|
90
....*....|..
gi 767996066 121 AVIMFILNFEDL 132
Cdd:cd00130 92 EVIGLLGVVRDI 103
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
37-63 |
5.21e-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: 36.22 E-value: 5.21e-03
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
259-645 |
4.63e-31 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 131.14 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192 64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYG-------AAV 400
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWircarllSVT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 401 LFLLM---CTFALIAH--------WLAC---------------------ICSLTSVGFGNVSPNTNSEKVFSICVMLIGS 448
Cdd:PLN03192 210 LFLVHcagCLYYLIADryphqgktWIGAvipnfretslwiryisaiywsITTMTTVGYGDLHAVNTIEMIFIIFYMLFNL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 449 LMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNAVLKGFPECLQADIC 528
Cdd:PLN03192 290 GLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSIC 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 529 LHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----RDDVVVAILGKNDIF 604
Cdd:PLN03192 369 QHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIF 448
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767996066 605 GEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 645
Cdd:PLN03192 449 GEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
258-467 |
3.78e-25 |
|
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: 105.04 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesrrgacsyTCSPLTVVDLIVDIMFVVDIVINFRTTYvntndevvshprrI 337
Cdd:pfam00520 3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 338 AVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520 60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 415 LACICS-------------------------------------LTSVGFGNVSPNTNSEK-------VFSICVMLIGSLM 450
Cdd:pfam00520 139 FLFIFAiigyqlfggklktwenpdngrtnfdnfpnaflwlfqtMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLL 218
|
250
....*....|....*..
gi 767996066 451 YASIFGNVSAIIQRLYS 467
Cdd:pfam00520 219 LNLFIAVIIDNFQELTE 235
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
541-652 |
4.33e-23 |
|
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: 95.09 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 541 AFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPg 615
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 767996066 616 kSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFW 652
Cdd:cd00038 80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
542-641 |
4.44e-19 |
|
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: 83.60 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 542 FSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPVSLHAQPGK 616
Cdd:smart00100 2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81
|
90 100
....*....|....*....|....*
gi 767996066 617 SSADVRALTYCDLHKIQRADLLEVL 641
Cdd:smart00100 82 ASAAAVALELATLLRIDFRDFLQLL 106
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
38-132 |
6.99e-19 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 82.12 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
|
90
....*....|....*.
gi 767996066 117 NEDGAVIMFILNFEDL 132
Cdd:pfam13426 76 DDGGELVGIIAILRDI 91
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
550-656 |
7.40e-16 |
|
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: 77.33 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 550 LRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRAL 624
Cdd:COG0664 9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
|
90 100 110
....*....|....*....|....*....|..
gi 767996066 625 TYCDLHKIQRADLLEVLDMYPAFAESFWSKLE 656
Cdd:COG0664 87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
31-125 |
1.73e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 79.09 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559 58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135
|
90
....*....|....*
gi 767996066 111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559 136 HLGPVYGEDGRLLYF 150
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
31-149 |
4.43e-15 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 79.50 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767996066 111 DVVPVKNEDGAVIMFILNFEDL-----AQLLAKCSSRSLsQRLL 149
Cdd:PRK13558 241 DIAPIRDEDGTVTHYVGFQTDVterkeAELALQRERRKL-QRLL 283
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
41-131 |
6.05e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
|
90
....*....|.
gi 767996066 121 AVIMFILNFED 131
Cdd:COG2202 111 EITGFVGIARD 121
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
561-644 |
2.68e-13 |
|
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 459637 [Multi-domain] Cd Length: 89 Bit Score: 66.09 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 561 HAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRA 635
Cdd:pfam00027 3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80
|
....*....
gi 767996066 636 DLLEVLDMY 644
Cdd:pfam00027 81 DFLELLERD 89
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
41-125 |
1.28e-10 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 65.08 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:PRK13557 55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132
|
....*
gi 767996066 121 AVIMF 125
Cdd:PRK13557 133 DLVYF 137
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
41-131 |
4.58e-09 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. 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: 55.12 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQPcTCDFLTgPNTPSSAVSRLAQALLGAEECK-VDILYYRKDASSFRCLVDVVPVKNED 119
Cdd:pfam00989 23 ILYVNAAAEELLGLSREEVIGKS-LLDLIP-EEDDAEVAELLRQALLQGEESRgFEVSFRVPDGRPRHVEVRASPVRDAG 100
|
90
....*....|..
gi 767996066 120 GAVIMFILNFED 131
Cdd:pfam00989 101 GEILGFLGVLRD 112
|
|
| PRK11753 |
PRK11753 |
cAMP-activated global transcriptional regulator CRP; |
563-645 |
5.55e-09 |
|
cAMP-activated global transcriptional regulator CRP;
Pssm-ID: 236969 [Multi-domain] Cd Length: 211 Bit Score: 57.30 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 563 PPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEpVSLHAQPGKSSADVRALTYCDLHKIQRADL 637
Cdd:PRK11753 26 PAKSTLIHAGEKAETLYYIVKGSVAVLIKDeegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKF 104
|
....*...
gi 767996066 638 LEVLDMYP 645
Cdd:PRK11753 105 RQLIQVNP 112
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
41-132 |
1.37e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 53.41 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130 14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
|
90
....*....|..
gi 767996066 121 AVIMFILNFEDL 132
Cdd:cd00130 92 EVIGLLGVVRDI 103
|
|
| Ion_trans_2 |
pfam07885 |
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
397-464 |
1.65e-06 |
|
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: 46.49 E-value: 1.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996066 397 GAAVLFLLMCTFA---LIAHWLACICsLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQR 464
Cdd:pfam07885 9 FGTVYYLLEEGWEwsfLDALYFSFVT-LTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
37-136 |
6.34e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 49.46 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 37 ENCAIIYCNDGFCELFGYSRVEVMQQPCTcDFLTGPNTPSSAVSRLAQAllGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:COG3852 25 ADGRITYVNPAAERLLGLSAEELLGRPLA-ELFPEDSPLRELLERALAE--GQPVTEREVTLRRKDGEERPVDVSVSPLR 101
|
90 100
....*....|....*....|
gi 767996066 117 NEDGAvIMFILNFEDLAQLL 136
Cdd:COG3852 102 DAEGE-GGVLLVLRDITERK 120
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
37-146 |
1.29e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 45.92 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 37 ENCAIIYCNDGFCELFGYSRVEVM-QQPCTcdFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPV 115
Cdd:PRK11359 154 PERRIVQCNRAFTEMFGYCISEASgMQPDT--LLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767996066 116 KNEDGAVIMFILNFEDLAQ-----------LLAKCSSRSLSQ 146
Cdd:PRK11359 232 YDVLAHLQNLVMTFSDITEerqirqlegniLAAMCSSPPFHE 273
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
41-135 |
3.16e-04 |
|
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: 44.38 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQPCTcDFLTGpntpssavSRLAQALlgAEECKVDILYYRKDASSFRCLVDVVPVKnEDG 120
Cdd:COG3829 33 ITYVNRAAERILGLPREEVIGKNVT-ELIPN--------SPLLEVL--KTGKPVTGVIQKTGGKGKTVIVTAIPIF-EDG 100
|
90
....*....|....*
gi 767996066 121 AVIMFILNFEDLAQL 135
Cdd:COG3829 101 EVIGAVETFRDITEL 115
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
41-132 |
2.11e-03 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 40.78 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEEcKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRE-SYELELRLKDGDGRWVWVEASAVPLRDG 235
|
90
....*....|...
gi 767996066 121 A-VIMFILNFEDL 132
Cdd:COG2202 236 GeVIGVLGIVRDI 248
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
535-639 |
2.18e-03 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 41.63 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 535 LLQHCPAFSgagkgcLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR----DDVVVAILGKNDIFGEPV-- 608
Cdd:PLN02868 15 LLQRLPSSS------LKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGpaeeESRPEFLLKRYDYFGYGLsg 88
|
90 100 110
....*....|....*....|....*....|...
gi 767996066 609 SLHaqpgksSADVRALT--YCDLHKIQRADLLE 639
Cdd:PLN02868 89 SVH------SADVVAVSelTCLVLPHEHCHLLS 115
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
37-63 |
5.21e-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: 36.22 E-value: 5.21e-03
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
19-132 |
6.70e-03 |
|
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: 39.96 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996066 19 IRKFEGQSRKflIANAQMENCA-------IIYCNDGFCELFGYSRVEVMQQPCTcDFLtGPNTPSSAVSRLAQALLGAEE 91
Cdd:COG5809 136 LRESEEKFRL--IFNHSPDGIIvtdldgrIIYANPAACKLLGISIEELIGKSIL-ELI-HSDDQENVAAFISQLLKDGGI 211
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767996066 92 CKVDILYYRKDASSFRCLVDVVPVkNEDGAVIMFILNFEDL 132
Cdd:COG5809 212 AQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDI 251
|
|
|