|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
259-698 |
1.77e-36 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 148.48 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192 64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 408 FALIaHWLACIWYAIGNvERPYLEHKigWLDSLGVQLGKryngsdpasgPSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192 210 LFLV-HCAGCLYYLIAD-RYPHQGKT--WIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192 276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 568 VLKGFPECLQADICLHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1034601540 644 DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 698
Cdd:PLN03192 435 KERVVGTLGCGDIFGEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
258-520 |
4.42e-35 |
|
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: 133.93 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesrrgacsyTCSPLTVVDLIVDIMFVVDIVINFRTTYvntndevvshprrI 337
Cdd:pfam00520 3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 338 AVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520 60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 415 LACIWYAIgnverpylehkigwldslGVQL--GKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEK-- 490
Cdd:pfam00520 139 FLFIFAII------------------GYQLfgGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200
|
250 260 270
....*....|....*....|....*....|....*
gi 1034601540 491 -----VFSICVMLIGSLMYASIFGNVSAIIQRLYS 520
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
594-705 |
3.57e-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: 95.47 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 594 AFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPg 668
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034601540 669 kSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFW 705
Cdd:cd00038 80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
595-694 |
3.67e-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: 83.99 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 595 FSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPVSLHAQPGK 669
Cdd:smart00100 2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81
|
90 100
....*....|....*....|....*
gi 1034601540 670 SSADVRALTYCDLHKIQRADLLEVL 694
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 |
7.42e-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: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
|
90
....*....|....*.
gi 1034601540 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 ... |
603-709 |
5.94e-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: 77.72 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 603 LRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRAL 677
Cdd:COG0664 9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
|
90 100 110
....*....|....*....|....*....|..
gi 1034601540 678 TYCDLHKIQRADLLEVLDMYPAFAESFWSKLE 709
Cdd:COG0664 87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
31-125 |
1.87e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 79.09 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559 58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135
|
90
....*....|....*
gi 1034601540 111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559 136 HLGPVYGEDGRLLYF 150
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
41-131 |
6.49e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
|
90
....*....|.
gi 1034601540 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 |
1.35e-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: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130 14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
|
90
....*....|..
gi 1034601540 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 |
5.00e-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: 36.61 E-value: 5.00e-03
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
259-698 |
1.77e-36 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 148.48 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192 64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 408 FALIaHWLACIWYAIGNvERPYLEHKigWLDSLGVQLGKryngsdpasgPSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192 210 LFLV-HCAGCLYYLIAD-RYPHQGKT--WIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192 276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 568 VLKGFPECLQADICLHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1034601540 644 DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 698
Cdd:PLN03192 435 KERVVGTLGCGDIFGEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
258-520 |
4.42e-35 |
|
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: 133.93 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesrrgacsyTCSPLTVVDLIVDIMFVVDIVINFRTTYvntndevvshprrI 337
Cdd:pfam00520 3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 338 AVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520 60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 415 LACIWYAIgnverpylehkigwldslGVQL--GKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEK-- 490
Cdd:pfam00520 139 FLFIFAII------------------GYQLfgGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200
|
250 260 270
....*....|....*....|....*....|....*
gi 1034601540 491 -----VFSICVMLIGSLMYASIFGNVSAIIQRLYS 520
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
594-705 |
3.57e-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: 95.47 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 594 AFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPg 668
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034601540 669 kSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFW 705
Cdd:cd00038 80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
595-694 |
3.67e-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: 83.99 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 595 FSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPVSLHAQPGK 669
Cdd:smart00100 2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81
|
90 100
....*....|....*....|....*
gi 1034601540 670 SSADVRALTYCDLHKIQRADLLEVL 694
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 |
7.42e-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: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
|
90
....*....|....*.
gi 1034601540 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 ... |
603-709 |
5.94e-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: 77.72 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 603 LRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRAL 677
Cdd:COG0664 9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
|
90 100 110
....*....|....*....|....*....|..
gi 1034601540 678 TYCDLHKIQRADLLEVLDMYPAFAESFWSKLE 709
Cdd:COG0664 87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
31-125 |
1.87e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 79.09 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559 58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135
|
90
....*....|....*
gi 1034601540 111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559 136 HLGPVYGEDGRLLYF 150
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
31-149 |
4.84e-15 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 79.50 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034601540 111 DVVPVKNEDGAVIMFILNFEDL-----AQLLAKCSSRSLsQRLL 149
Cdd:PRK13558 241 DIAPIRDEDGTVTHYVGFQTDVterkeAELALQRERRKL-QRLL 283
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
41-131 |
6.49e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
|
90
....*....|.
gi 1034601540 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, ... |
614-697 |
2.84e-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: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 614 HAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRA 688
Cdd:pfam00027 3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80
|
....*....
gi 1034601540 689 DLLEVLDMY 697
Cdd:pfam00027 81 DFLELLERD 89
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
41-125 |
1.39e-10 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 65.08 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:PRK13557 55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132
|
....*
gi 1034601540 121 AVIMF 125
Cdd:PRK13557 133 DLVYF 137
|
|
| Ion_trans_2 |
pfam07885 |
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
463-517 |
1.73e-10 |
|
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: 58.05 E-value: 1.73e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034601540 463 YVTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQR 517
Cdd:pfam07885 24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
41-131 |
4.87e-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: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQPcTCDFLTgPNTPSSAVSRLAQALLGAEECK-VDILYYRKDASSFRCLVDVVPVKNED 119
Cdd:pfam00989 23 ILYVNAAAEELLGLSREEVIGKS-LLDLIP-EEDDAEVAELLRQALLQGEESRgFEVSFRVPDGRPRHVEVRASPVRDAG 100
|
90
....*....|..
gi 1034601540 120 GAVIMFILNFED 131
Cdd:pfam00989 101 GEILGFLGVLRD 112
|
|
| PRK11753 |
PRK11753 |
cAMP-activated global transcriptional regulator CRP; |
616-698 |
5.93e-09 |
|
cAMP-activated global transcriptional regulator CRP;
Pssm-ID: 236969 [Multi-domain] Cd Length: 211 Bit Score: 57.30 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 616 PPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEpVSLHAQPGKSSADVRALTYCDLHKIQRADL 690
Cdd:PRK11753 26 PAKSTLIHAGEKAETLYYIVKGSVAVLIKDeegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKF 104
|
....*...
gi 1034601540 691 LEVLDMYP 698
Cdd:PRK11753 105 RQLIQVNP 112
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
41-132 |
1.35e-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: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130 14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
|
90
....*....|..
gi 1034601540 121 AVIMFILNFEDL 132
Cdd:cd00130 92 EVIGLLGVVRDI 103
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
37-136 |
5.66e-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: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 37 ENCAIIYCNDGFCELFGYSRVEVMQQPCTcDFLTGPNTPSSAVSRLAQAllGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:COG3852 25 ADGRITYVNPAAERLLGLSAEELLGRPLA-ELFPEDSPLRELLERALAE--GQPVTEREVTLRRKDGEERPVDVSVSPLR 101
|
90 100
....*....|....*....|
gi 1034601540 117 NEDGAvIMFILNFEDLAQLL 136
Cdd:COG3852 102 DAEGE-GGVLLVLRDITERK 120
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
37-146 |
1.33e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 45.92 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 37 ENCAIIYCNDGFCELFGYSRVEVM-QQPCTcdFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPV 115
Cdd:PRK11359 154 PERRIVQCNRAFTEMFGYCISEASgMQPDT--LLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1034601540 116 KNEDGAVIMFILNFEDLAQ-----------LLAKCSSRSLSQ 146
Cdd:PRK11359 232 YDVLAHLQNLVMTFSDITEerqirqlegniLAAMCSSPPFHE 273
|
|
| PRK10537 |
PRK10537 |
voltage-gated potassium channel protein; |
334-536 |
1.47e-04 |
|
voltage-gated potassium channel protein;
Pssm-ID: 236711 [Multi-domain] Cd Length: 393 Bit Score: 45.40 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 334 PRRIAVHYFKGWfLIDMVAAIPFDLLI----FRTGSDETTTLIGLLKTAR-------LLRLVRVARKLDRYSEYGAAVLF 402
Cdd:PRK10537 35 YGMAALNLFDIW-HIKALSALDLSLLAnapqFMLGVFLVLMAIGLLFRARlawaisiLLLLAALAITLHFYPWLKFLIGY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 403 LLMCTFALIAHW-------LAC--IWYAIGnverpylehkIGWLDSLGVqLGKRYNGSDPAsgPSVQDkYVTALYFTFSS 473
Cdd:PRK10537 114 CIVLLVALLIYRrdfdrssLAAgtLFAVIS----------ITSLLFYST-FGALYLGDGFS--PPIES-LSTAFYFSIVT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601540 474 LTSVGFGNVSPNTNSEKVFSICVMLIGSLMYA----SIFGNV-SAIIQRLYSGtaRYHTqMLRVKEFI 536
Cdd:PRK10537 180 MSTVGYGDIVPVSESARLFTISVIILGITVFAtsisAIFGPViRGNLKRLVKG--RISH-MHRKDHFI 244
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
41-135 |
3.38e-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: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQPCTcDFLTGpntpssavSRLAQALlgAEECKVDILYYRKDASSFRCLVDVVPVKnEDG 120
Cdd:COG3829 33 ITYVNRAAERILGLPREEVIGKNVT-ELIPN--------SPLLEVL--KTGKPVTGVIQKTGGKGKTVIVTAIPIF-EDG 100
|
90
....*....|....*
gi 1034601540 121 AVIMFILNFEDLAQL 135
Cdd:COG3829 101 EVIGAVETFRDITEL 115
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
41-132 |
2.25e-03 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 40.78 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEEcKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRE-SYELELRLKDGDGRWVWVEASAVPLRDG 235
|
90
....*....|...
gi 1034601540 121 A-VIMFILNFEDL 132
Cdd:COG2202 236 GeVIGVLGIVRDI 248
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
588-692 |
2.35e-03 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 41.63 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 588 LLQHCPAFSgagkgcLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR----DDVVVAILGKNDIFGEPV-- 661
Cdd:PLN02868 15 LLQRLPSSS------LKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGpaeeESRPEFLLKRYDYFGYGLsg 88
|
90 100 110
....*....|....*....|....*....|...
gi 1034601540 662 SLHaqpgksSADVRALT--YCDLHKIQRADLLE 692
Cdd:PLN02868 89 SVH------SADVVAVSelTCLVLPHEHCHLLS 115
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
37-63 |
5.00e-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: 36.61 E-value: 5.00e-03
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
19-132 |
7.17e-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: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601540 19 IRKFEGQSRKflIANAQMENCA-------IIYCNDGFCELFGYSRVEVMQQPCTcDFLtGPNTPSSAVSRLAQALLGAEE 91
Cdd:COG5809 136 LRESEEKFRL--IFNHSPDGIIvtdldgrIIYANPAACKLLGISIEELIGKSIL-ELI-HSDDQENVAAFISQLLKDGGI 211
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1034601540 92 CKVDILYYRKDASSFRCLVDVVPVkNEDGAVIMFILNFEDL 132
Cdd:COG5809 212 AQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDI 251
|
|
|