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Conserved domains on  [gi|1316032219|sp|Q9WVJ0|]
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RecName: Full=Potassium voltage-gated channel subfamily H member 3; AltName: Full=Ether-a-go-go-like potassium channel 2; Short=ELK channel 2; Short=mElk2; AltName: Full=Voltage-gated potassium channel subunit Kv12.2

Protein Classification

PAS and CAP_ED domain-containing protein( domain architecture ID 13822764)

protein containing domains PAS, CAP_ED, and cyc_nuc_ocin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 227-662 2.84e-24

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.96  E-value: 2.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  227 WDGFILLATLYVAVTVPYSVcvstAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQV-VFAPKSICLHYVTT 305
Cdd:PLN03192    64 WETLMVVLVAYSAWVYPFEV----AFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLST 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  306 WFLLDVIAALPFDLLHAF-----KVNV---YVGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACV 377
Cdd:PLN03192   140 WFLMDVASTIPFQALAYLitgtvKLNLsysLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCL 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  378 wfyigqqeiesseselpeigwlqelarrletpYYLVS-RSPDGGNSsgqsencsssssssgsgggrgseANGTGLELLGG 456
Cdd:PLN03192   220 --------------------------------YYLIAdRYPHQGKT-----------------------WIGAVIPNFRE 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  457 PSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYI 536
Cdd:PLN03192   245 TSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFV 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  537 RIHRIPKPLKQRMLEYFQATWAVNNgIDTTELLQSLPDELRADIAMHLHKEVLQ-LPLFEAASRGCLRALSLALRPAFCT 615
Cdd:PLN03192   325 GRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEkVYLFKGVSREILLLLVTKMKAEYIP 403

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316032219  616 PGEYLIHQGDALQALYFVCSGSMEVL----KGGTVLAILGKGDLIG-----CELPQ 662
Cdd:PLN03192   404 PREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGevgalCCRPQ 459
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-135 1.16e-18

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


:

Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 81.74  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   40 FPVVYCSDGFCDLTGFSRAEVMQRGCACsFLYGPDTSELvrqqIRKALDEHKEFKA-ELILYRKSGLPFWCLLDVIPIKN 118
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITD-LFAEPEDSER----LREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 1316032219  119 EKGEVALFLVSHKDISE 135
Cdd:pfam13426   77 DGGELVGIIAILRDITE 93
cyc_nuc_ocin super family cl28242
bacteriocin-type transport-associated protein; Members of this protein family are ...
 617-712 1.98e-06

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


The actual alignment was detected with superfamily member TIGR03896:

Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 51.05  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  617 GEYLIHQGDALQALYFVCSGSMEVL----KGGTVLAILGKGDLIGcELPQREQVVKANADVKGLTYCVLQCLQLAGLHES 692
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLSispdGPGREVGSSRRGEILG-ETPFLNGSLPGTATVKAIENSVLLAIDKQQLAAK 247

                           90       100
                   ....*....|....*....|
gi 1316032219  693 LALYPEFAPRFSRGLRGELS 712
Cdd:TIGR03896  248 LQQDVGFASRFYRVIASLLS 267
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 227-662 2.84e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.96  E-value: 2.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  227 WDGFILLATLYVAVTVPYSVcvstAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQV-VFAPKSICLHYVTT 305
Cdd:PLN03192    64 WETLMVVLVAYSAWVYPFEV----AFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLST 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  306 WFLLDVIAALPFDLLHAF-----KVNV---YVGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACV 377
Cdd:PLN03192   140 WFLMDVASTIPFQALAYLitgtvKLNLsysLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCL 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  378 wfyigqqeiesseselpeigwlqelarrletpYYLVS-RSPDGGNSsgqsencsssssssgsgggrgseANGTGLELLGG 456
Cdd:PLN03192   220 --------------------------------YYLIAdRYPHQGKT-----------------------WIGAVIPNFRE 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  457 PSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYI 536
Cdd:PLN03192   245 TSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFV 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  537 RIHRIPKPLKQRMLEYFQATWAVNNgIDTTELLQSLPDELRADIAMHLHKEVLQ-LPLFEAASRGCLRALSLALRPAFCT 615
Cdd:PLN03192   325 GRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEkVYLFKGVSREILLLLVTKMKAEYIP 403

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316032219  616 PGEYLIHQGDALQALYFVCSGSMEVL----KGGTVLAILGKGDLIG-----CELPQ 662
Cdd:PLN03192   404 PREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGevgalCCRPQ 459
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 593-703 1.28e-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: 85.46  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  593 LFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLKGG-----TVLAILGKGDLIGCELPQREQVv 667
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1316032219  668 kANADVKGLTYCVLQCLQLAGLHESLALYPEFAPRF 703
Cdd:cd00038     80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-135 1.16e-18

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 81.74  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   40 FPVVYCSDGFCDLTGFSRAEVMQRGCACsFLYGPDTSELvrqqIRKALDEHKEFKA-ELILYRKSGLPFWCLLDVIPIKN 118
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITD-LFAEPEDSER----LREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 1316032219  119 EKGEVALFLVSHKDISE 135
Cdd:pfam13426   77 DGGELVGIIAILRDITE 93
PRK13557 PRK13557
histidine kinase; Provisional
 41-134 5.98e-18

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 88.57  E-value: 5.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   41 PVVYCSDGFCDLTGFSRAEVMqrGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:PRK13557    54 PIVFANRAFLEMTGYAAEEII--GNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131

                           90
                   ....*....|....
gi 1316032219  121 GEVALFLVSHKDIS 134
Cdd:PRK13557   132 GDLVYFFGSQLDVS 145
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-137 1.17e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.22  E-value: 1.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCacSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKG 121
Cdd:COG2202     33 ILYVNPAFERLTGYSAEELLGKTL--RDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                           90
                   ....*....|....*.
gi 1316032219  122 EVALFLVSHKDISETK 137
Cdd:COG2202    111 EITGFVGIARDITERK 126
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 593-707 1.74e-16

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: 76.67  E-value: 1.74e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   593 LFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLK-----GGTVLAILGKGDLIGcELP-QREQV 666
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFG-ELAlLTNSR 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1316032219   667 VKANADVKGLTYCVLQCLQLAGLHESLALYPEFAPRFSRGL 707
Cdd:smart00100   80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 227-522 4.91e-13

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: 69.99  E-value: 4.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  227 WDGFILLATLYVAVTVPYSVCVstaREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFvsksgqvvfapksICLHYVTT- 305
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYF---QPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSp 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  306 WFLLDVIAALPFDLlhAFKVNVYVGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAV-----FALLAHWVACVWFY 380
Cdd:pfam00520   68 WNILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLkslgnLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  381 IGQQeiesseselpeigwlqelarrLETPYYLVSRSPDGGNSSGQSencsssssssgsgggrgseangtglellggpslr 460
Cdd:pfam00520  146 IGYQ---------------------LFGGKLKTWENPDNGRTNFDN---------------------------------- 170

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316032219  461 saYITSLYFALSSLTSVGFGNVSANTDTEK-------IFSICTMLIGALMHAVVFGNVTAIIQRMYARR 522
Cdd:pfam00520  171 --FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-133 1.21e-11

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 62.27  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCacSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKG 121
Cdd:cd00130     14 ILYANPAAEQLLGYSPEELIGKSL--LDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                           90
                   ....*....|..
gi 1316032219  122 EVALFLVSHKDI 133
Cdd:cd00130     92 EVIGLLGVVRDI 103
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 602-711 2.85e-08

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: 55.38  E-value: 2.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  602 LRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLK---GGT--VLAILGKGDLIGCELPQREQVVKANADVkgL 676
Cdd:COG0664      9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRiseDGReqILGFLGPGDFFGELSLLGGEPSPATAEA--L 86

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1316032219  677 TYCVLQCLQLAGLHESLALYPEFAPRFSRGLRGEL 711
Cdd:COG0664     87 EDSELLRIPREDLEELLERNPELARALLRLLARRL 121
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 42-138 2.91e-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: 50.37  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGcaCSFLYGPDTSELVRQQIRKALD-EHKEFKAELILYRKSGLPFWCLLDVIPIkNEK 120
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRN--VLELIPEEDREEVRERIERRLEgEPEPVSEERRVRRKDGSEIWVEVSVSPI-RTN 101

                           90
                   ....*....|....*...
gi 1316032219  121 GEVALFLVSHKDISETKN 138
Cdd:TIGR00229  102 GGELGVVGIVRDITERKE 119
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 96-135 1.94e-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: 1.94e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1316032219    96 ELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISE 135
Cdd:smart00086    3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 617-712 1.98e-06

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: 51.05  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  617 GEYLIHQGDALQALYFVCSGSMEVL----KGGTVLAILGKGDLIGcELPQREQVVKANADVKGLTYCVLQCLQLAGLHES 692
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLSispdGPGREVGSSRRGEILG-ETPFLNGSLPGTATVKAIENSVLLAIDKQQLAAK 247

                           90       100
                   ....*....|....*....|
gi 1316032219  693 LALYPEFAPRFSRGLRGELS 712
Cdd:TIGR03896  248 LQQDVGFASRFYRVIASLLS 267
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 227-662 2.84e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.96  E-value: 2.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  227 WDGFILLATLYVAVTVPYSVcvstAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQV-VFAPKSICLHYVTT 305
Cdd:PLN03192    64 WETLMVVLVAYSAWVYPFEV----AFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLST 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  306 WFLLDVIAALPFDLLHAF-----KVNV---YVGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACV 377
Cdd:PLN03192   140 WFLMDVASTIPFQALAYLitgtvKLNLsysLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCL 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  378 wfyigqqeiesseselpeigwlqelarrletpYYLVS-RSPDGGNSsgqsencsssssssgsgggrgseANGTGLELLGG 456
Cdd:PLN03192   220 --------------------------------YYLIAdRYPHQGKT-----------------------WIGAVIPNFRE 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  457 PSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYI 536
Cdd:PLN03192   245 TSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFV 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  537 RIHRIPKPLKQRMLEYFQATWAVNNgIDTTELLQSLPDELRADIAMHLHKEVLQ-LPLFEAASRGCLRALSLALRPAFCT 615
Cdd:PLN03192   325 GRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEkVYLFKGVSREILLLLVTKMKAEYIP 403

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316032219  616 PGEYLIHQGDALQALYFVCSGSMEVL----KGGTVLAILGKGDLIG-----CELPQ 662
Cdd:PLN03192   404 PREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGevgalCCRPQ 459
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 593-703 1.28e-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: 85.46  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  593 LFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLKGG-----TVLAILGKGDLIGCELPQREQVv 667
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1316032219  668 kANADVKGLTYCVLQCLQLAGLHESLALYPEFAPRF 703
Cdd:cd00038     80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-135 1.16e-18

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 81.74  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   40 FPVVYCSDGFCDLTGFSRAEVMQRGCACsFLYGPDTSELvrqqIRKALDEHKEFKA-ELILYRKSGLPFWCLLDVIPIKN 118
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITD-LFAEPEDSER----LREALREGKAVREfEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 1316032219  119 EKGEVALFLVSHKDISE 135
Cdd:pfam13426   77 DGGELVGIIAILRDITE 93
PRK13557 PRK13557
histidine kinase; Provisional
 41-134 5.98e-18

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 88.57  E-value: 5.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   41 PVVYCSDGFCDLTGFSRAEVMqrGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:PRK13557    54 PIVFANRAFLEMTGYAAEEII--GNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131

                           90
                   ....*....|....
gi 1316032219  121 GEVALFLVSHKDIS 134
Cdd:PRK13557   132 GDLVYFFGSQLDVS 145
PRK13559 PRK13559
hypothetical protein; Provisional
 41-135 1.48e-17

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 85.64  E-value: 1.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   41 PVVYCSDGFCDLTGFSRAEVMQRGCacSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:PRK13559    67 PIVLANQAFLDLTGYAAEEVVGRNC--RFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGED 144

                           90
                   ....*....|....*
gi 1316032219  121 GEVALFLVSHKDISE 135
Cdd:PRK13559   145 GRLLYFFGSQWDVTD 159
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-137 1.17e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.22  E-value: 1.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCacSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKG 121
Cdd:COG2202     33 ILYVNPAFERLTGYSAEELLGKTL--RDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                           90
                   ....*....|....*.
gi 1316032219  122 EVALFLVSHKDISETK 137
Cdd:COG2202    111 EITGFVGIARDITERK 126
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 593-707 1.74e-16

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: 76.67  E-value: 1.74e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   593 LFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLK-----GGTVLAILGKGDLIGcELP-QREQV 666
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFG-ELAlLTNSR 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1316032219   667 VKANADVKGLTYCVLQCLQLAGLHESLALYPEFAPRFSRGL 707
Cdd:smart00100   80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 41-137 2.55e-16

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 84.12  E-value: 2.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   41 PVVYCSDGFCDLTGFSRAEVMqrGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:PRK13558   172 PLIYINDAFERITGYSPDEVL--GRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDED 249

                           90
                   ....*....|....*..
gi 1316032219  121 GEVALFLVSHKDISETK 137
Cdd:PRK13558   250 GTVTHYVGFQTDVTERK 266
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 227-522 4.91e-13

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: 69.99  E-value: 4.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  227 WDGFILLATLYVAVTVPYSVCVstaREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFvsksgqvvfapksICLHYVTT- 305
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYF---QPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSp 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  306 WFLLDVIAALPFDLlhAFKVNVYVGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAV-----FALLAHWVACVWFY 380
Cdd:pfam00520   68 WNILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLkslgnLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  381 IGQQeiesseselpeigwlqelarrLETPYYLVSRSPDGGNSSGQSencsssssssgsgggrgseangtglellggpslr 460
Cdd:pfam00520  146 IGYQ---------------------LFGGKLKTWENPDNGRTNFDN---------------------------------- 170

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316032219  461 saYITSLYFALSSLTSVGFGNVSANTDTEK-------IFSICTMLIGALMHAVVFGNVTAIIQRMYARR 522
Cdd:pfam00520  171 --FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-133 1.21e-11

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 62.27  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCacSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKG 121
Cdd:cd00130     14 ILYANPAAEQLLGYSPEELIGKSL--LDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                           90
                   ....*....|..
gi 1316032219  122 EVALFLVSHKDI 133
Cdd:cd00130     92 EVIGLLGVVRDI 103
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 463-517 1.89e-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: 1.89e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316032219  463 YITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQR 517
Cdd:pfam07885   24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 602-711 2.85e-08

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: 55.38  E-value: 2.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  602 LRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLK---GGT--VLAILGKGDLIGCELPQREQVVKANADVkgL 676
Cdd:COG0664      9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRiseDGReqILGFLGPGDFFGELSLLGGEPSPATAEA--L 86

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1316032219  677 TYCVLQCLQLAGLHESLALYPEFAPRFSRGLRGEL 711
Cdd:COG0664     87 EDSELLRIPREDLEELLERNPELARALLRLLARRL 121
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
42-137 4.03e-08

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 56.78  E-value: 4.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCACSFlygPDTSELvRQQIRKALDEHKEFKA-ELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:COG3852     29 ITYVNPAAERLLGLSAEELLGRPLAELF---PEDSPL-RELLERALAEGQPVTErEVTLRRKDGEERPVDVSVSPLRDAE 104

                           90
                   ....*....|....*..
gi 1316032219  121 GEVALFLVSHkDISETK 137
Cdd:COG3852    105 GEGGVLLVLR-DITERK 120
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 42-138 2.91e-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: 50.37  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGcaCSFLYGPDTSELVRQQIRKALD-EHKEFKAELILYRKSGLPFWCLLDVIPIkNEK 120
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRN--VLELIPEEDREEVRERIERRLEgEPEPVSEERRVRRKDGSEIWVEVSVSPI-RTN 101

                           90
                   ....*....|....*...
gi 1316032219  121 GEVALFLVSHKDISETKN 138
Cdd:TIGR00229  102 GGELGVVGIVRDITERKE 119
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-133 3.69e-07

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 49.72  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRgcacSF--LYGPDTSELVRQQIRKALDEHKEFKAELILYRKS-GLPFWCLLDVIPIKN 118
Cdd:pfam00989   23 ILYVNAAAEELLGLSREEVIGK----SLldLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPdGRPRHVEVRASPVRD 98

                           90
                   ....*....|....*
gi 1316032219  119 EKGEVALFLVSHKDI 133
Cdd:pfam00989   99 AGGEILGFLGVLRDI 113
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 616-681 5.21e-07

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 48.37  E-value: 5.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316032219  616 PGEYLIHQGDALQALYFVCSGSMEVLKGG-----TVLAILGKGDLIGcELP--QREqvvKANADVKGLTYCVL 681
Cdd:pfam00027    6 AGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFG-ELAllGGE---PRSATVVALTDSEL 74
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 96-135 1.94e-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: 1.94e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1316032219    96 ELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISE 135
Cdd:smart00086    3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 617-712 1.98e-06

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: 51.05  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  617 GEYLIHQGDALQALYFVCSGSMEVL----KGGTVLAILGKGDLIGcELPQREQVVKANADVKGLTYCVLQCLQLAGLHES 692
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLSispdGPGREVGSSRRGEILG-ETPFLNGSLPGTATVKAIENSVLLAIDKQQLAAK 247

                           90       100
                   ....*....|....*....|
gi 1316032219  693 LALYPEFAPRFSRGLRGELS 712
Cdd:TIGR03896  248 LQQDVGFASRFYRVIASLLS 267
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-137 2.03e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.41  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCAcsFLYGPDTSELVRQQIRKALDEHKE-FKAELILYRKSGLPFWCLLDVIPIKNEk 120
Cdd:COG2202    159 ILYVNPAAEELLGYSPEELLGKSLL--DLLHPEDRERLLELLRRLLEGGREsYELELRLKDGDGRWVWVEASAVPLRDG- 235

                           90
                   ....*....|....*..
gi 1316032219  121 GEVALFLVSHKDISETK 137
Cdd:COG2202    236 GEVIGVLGIVRDITERK 252
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-123 2.03e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 44.25  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGCAC-SFLYgPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGESWlDLVH-PDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79


                   ...
gi 1316032219  121 GEV 123
Cdd:pfam08447   80 GKP 82
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-137 1.35e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 42.40  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVmqRGCACSFLYGPDTSELVRQQIRKALDEHkEFKAELILYRKSGLPFWCLLDVIPIKNEKG 121
Cdd:pfam08448   17 VRYANAAAAELFGLPPEEL--LGKTLAELLPPEDAARLERALRRALEGE-EPIDFLEELLLNGEERHYELRLTPLRDPDG 93

                           90
                   ....*....|....*.
gi 1316032219  122 EVALFLVSHKDISETK 137
Cdd:pfam08448   94 EVIGVLVISRDITERR 109
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 42-138 1.36e-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: 45.74  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219   42 VVYCSDGFCDLTGFSRAEVMQRGcACSFLygPDTSELVRQQIRKALDEHKEFKA-ELILYRKSGLPFWCLLDVIPIKNEK 120
Cdd:COG5809     37 ILKVNPAAERIFGYTEDELLGTN-ILDFL--HPDDEKELREILKLLKEGESRDElEFELRHKNGKRLEFSSKLSPIFDQN 113

                           90
                   ....*....|....*...
gi 1316032219  121 GEVALFLVSHKDISETKN 138
Cdd:COG5809    114 GDIEGMLAISRDITERKR 131
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 590-695 4.08e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 40.86  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032219  590 QLPLFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLK----GGTVLAILGKGDLIGCELPQREQ 665
Cdd:PLN02868    12 SVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGpaeeESRPEFLLKRYDYFGYGLSGSVH 91

                           90       100       110
                   ....*....|....*....|....*....|
gi 1316032219  666 vvkaNADVKGLTYcvLQCLQLAglHESLAL 695
Cdd:PLN02868    92 ----SADVVAVSE--LTCLVLP--HEHCHL 113
 
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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