NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958656115|ref|XP_038940983|]
View 

potassium voltage-gated channel subfamily H member 6 isoform X2 [Rattus norvegicus]

Protein Classification

PAS domain-containing protein( domain architecture ID 13822714)

PAS domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 259-698 5.42e-39

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 155.41  E-value: 5.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesqrgtcgytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192  130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 408 FALIaHWLACIWYAIGNverPYLEPKIGWLDSLGAQLGKQyngsdpasgpSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192  210 LFLV-HCAGCLYYLIAD---RYPHQGKTWIGAVIPNFRET----------SLWIRYISAIYWSITTMTTVGYGDLHAVNT 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192  276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 568 VLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192  355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958656115 644 DDVVVAILGKNDIFGEPASLHARPgkSSADVRALTYCDLHKIHRADLLEVLDMYP 698
Cdd:PLN03192  435 KERVVGTLGCGDIFGEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 38-132 7.67e-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: 81.74  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  38 NCAIIYCNDGFCELFGYSRVEVMQRPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*.
gi 1958656115 117 NEDGAVIMFILNFEDL 132
Cdd:pfam13426  76 DDGGELVGIIAILRDI 91
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 259-698 5.42e-39

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 155.41  E-value: 5.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesqrgtcgytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192  130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 408 FALIaHWLACIWYAIGNverPYLEPKIGWLDSLGAQLGKQyngsdpasgpSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192  210 LFLV-HCAGCLYYLIAD---RYPHQGKTWIGAVIPNFRET----------SLWIRYISAIYWSITTMTTVGYGDLHAVNT 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192  276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 568 VLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192  355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958656115 644 DDVVVAILGKNDIFGEPASLHARPgkSSADVRALTYCDLHKIHRADLLEVLDMYP 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 1.38e-31

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: 123.53  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesqrgtcgyTCSPLTVVDLIVDIMFVVDIVINFRTTYVNtndevvshprri 337
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 338 aVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520  61 -KRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 415 LACIWYAIGNverpylepkigwldslgaQL--GKQYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEK-- 490
Cdd:pfam00520 139 FLFIFAIIGY------------------QLfgGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958656115 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 3.60e-24

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: 97.78  E-value: 3.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 594 AFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPASLHARPg 668
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958656115 669 kSSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFW 705
Cdd:cd00038    80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 595-694 2.74e-21

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: 89.77  E-value: 2.74e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  595 FRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPASLHARPGK 669
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81

                           90       100
                   ....*....|....*....|....*
gi 1958656115  670 SSADVRALTYCDLHKIHRADLLEVL 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 7.67e-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: 81.74  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  38 NCAIIYCNDGFCELFGYSRVEVMQRPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*.
gi 1958656115 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 ...
 595-709 5.44e-17

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: 80.03  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 595 FRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPASLHARPgk 669
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958656115 670 SSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFWNKLE 709
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLRLLA 118
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 31-151 9.88e-17

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 84.50  E-value: 9.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958656115 111 DVVPVKNEDGAVIMFILNFEDL-----AQLLAKSSSRSLtQRLLSH 151
Cdd:PRK13558  241 DIAPIRDEDGTVTHYVGFQTDVterkeAELALQRERRKL-QRLLER 285
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-131 4.78e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 72.75  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202    33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                          90
                  ....*....|.
gi 1958656115 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 2.57e-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: 52.25  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130    14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                          90
                  ....*....|..
gi 1958656115 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 4.54e-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: 4.54e-03
                           10        20
                   ....*....|....*....|....*..
gi 1958656115   37 ENCAIIYCNDGFCELFGYSRVEVMQRP 63
Cdd:smart00091  19 LDGRILYANPAAEELLGYSPEELIGKS 45
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 37-132 8.90e-03

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: 36.89  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  37 ENCAIIYCNDGFCELFGYSRVEVMQRPCTcDFLTGPNtpsSAVSRLAQALLGAEECKVDIL---YYRKDASSFRCLVDVV 113
Cdd:TIGR00229  21 LEGNILYVNPAFEEIFGYSAEELIGRNVL-ELIPEED---REEVRERIERRLEGEPEPVSEerrVRRKDGSEIWVEVSVS 96

                          90
                  ....*....|....*....
gi 1958656115 114 PVkNEDGAVIMFILNFEDL 132
Cdd:TIGR00229  97 PI-RTNGGELGVVGIVRDI 114
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 259-698 5.42e-39

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 155.41  E-value: 5.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesqrgtcgytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192  130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 408 FALIaHWLACIWYAIGNverPYLEPKIGWLDSLGAQLGKQyngsdpasgpSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192  210 LFLV-HCAGCLYYLIAD---RYPHQGKTWIGAVIPNFRET----------SLWIRYISAIYWSITTMTTVGYGDLHAVNT 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192  276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 568 VLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192  355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958656115 644 DDVVVAILGKNDIFGEPASLHARPgkSSADVRALTYCDLHKIHRADLLEVLDMYP 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 1.38e-31

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: 123.53  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesqrgtcgyTCSPLTVVDLIVDIMFVVDIVINFRTTYVNtndevvshprri 337
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 338 aVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520  61 -KRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 415 LACIWYAIGNverpylepkigwldslgaQL--GKQYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEK-- 490
Cdd:pfam00520 139 FLFIFAIIGY------------------QLfgGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958656115 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 3.60e-24

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: 97.78  E-value: 3.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 594 AFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPASLHARPg 668
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958656115 669 kSSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFW 705
Cdd:cd00038    80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 595-694 2.74e-21

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: 89.77  E-value: 2.74e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  595 FRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPASLHARPGK 669
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81

                           90       100
                   ....*....|....*....|....*
gi 1958656115  670 SSADVRALTYCDLHKIHRADLLEVL 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 7.67e-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: 81.74  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  38 NCAIIYCNDGFCELFGYSRVEVMQRPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*.
gi 1958656115 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 ...
 595-709 5.44e-17

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: 80.03  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 595 FRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPASLHARPgk 669
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958656115 670 SSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFWNKLE 709
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLRLLA 118
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 31-151 9.88e-17

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 84.50  E-value: 9.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958656115 111 DVVPVKNEDGAVIMFILNFEDL-----AQLLAKSSSRSLtQRLLSH 151
Cdd:PRK13558  241 DIAPIRDEDGTVTHYVGFQTDVterkeAELALQRERRKL-QRLLER 285
PRK13559 PRK13559
hypothetical protein; Provisional
 31-125 1.78e-16

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 81.79  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559   58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135

                          90
                  ....*....|....*
gi 1958656115 111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559  136 HLGPVYGEDGRLLYF 150
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-131 4.78e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 72.75  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202    33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                          90
                  ....*....|.
gi 1958656115 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 4.02e-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: 65.32  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 614 HAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPASLHARPgkSSADVRALTYCDLHKIHRA 688
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80


                  ....*....
gi 1958656115 689 DLLEVLDMY 697
Cdd:pfam00027  81 DFLELLERD 89
PRK13557 PRK13557
histidine kinase; Provisional
 41-125 4.64e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.85  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132


                  ....*
gi 1958656115 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 2.32e-09

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: 54.58  E-value: 2.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958656115 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 7.23e-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: 53.96  E-value: 7.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRPcTCDFLTgPNTPSSAVSRLAQALLGAEECK-VDILYYRKDASSFRCLVDVVPVKNED 119
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKS-LLDLIP-EEDDAEVAELLRQALLQGEESRgFEVSFRVPDGRPRHVEVRASPVRDAG 100

                          90
                  ....*....|..
gi 1958656115 120 GAVIMFILNFED 131
Cdd:pfam00989 101 GEILGFLGVLRD 112
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 41-132 2.57e-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: 52.25  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130    14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                          90
                  ....*....|..
gi 1958656115 121 AVIMFILNFEDL 132
Cdd:cd00130    92 EVIGLLGVVRDI 103
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
616-698 2.79e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 54.99  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 616 PPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEpASLHARPGKSSADVRALTYCDLHKIHRADL 690
Cdd:PRK11753   26 PAKSTLIHAGEKAETLYYIVKGSVAVLIKDeegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKF 104


                  ....*...
gi 1958656115 691 LEVLDMYP 698
Cdd:PRK11753  105 RQLIQVNP 112
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
37-150 2.12e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 50.62  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  37 ENCAIIYCNDGFCELFGYSRVEVMQRPCTcDFLTGPNTPSSAVSRLAQAllGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:COG3852    25 ADGRITYVNPAAERLLGLSAEELLGRPLA-ELFPEDSPLRELLERALAE--GQPVTEREVTLRRKDGEERPVDVSVSPLR 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958656115 117 NEDGAvIMFILNFEDLAQLLAKSSSRSLTQRLLS 150
Cdd:COG3852   102 DAEGE-GGVLLVLRDITERKRLERELRRAEKLAA 134
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 41-153 7.41e-05

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: 45.92  E-value: 7.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRPCTcDFLTGpntpssavSRLAQALlgAEECKVDILYYRKDASSFRCLVDVVPVKnEDG 120
Cdd:COG3829    33 ITYVNRAAERILGLPREEVIGKNVT-ELIPN--------SPLLEVL--KTGKPVTGVIQKTGGKGKTVIVTAIPIF-EDG 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958656115 121 AVIMFILNFEDLAQLlaKSSSRSLTQRLLSHSF 153
Cdd:COG3829   101 EVIGAVETFRDITEL--KRLERKLREEELERGL 131
PRK10537 PRK10537
voltage-gated potassium channel protein;
464-536 3.12e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 43.86  E-value: 3.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656115 464 VTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYA----SIFGNV-SAIIQRLYSGtaRYHTqMLRVKEFI 536
Cdd:PRK10537  170 STAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFAtsisAIFGPViRGNLKRLVKG--RISH-MHRKDHFI 244
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 37-134 5.95e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 43.22  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  37 ENCAIIYCNDGFCELFGYSRVEVM-QRPCTcdFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPV 115
Cdd:PRK11359  154 PERRIVQCNRAFTEMFGYCISEASgMQPDT--LLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231

                          90
                  ....*....|....*....
gi 1958656115 116 KNEDGAVIMFILNFEDLAQ 134
Cdd:PRK11359  232 YDVLAHLQNLVMTFSDITE 250
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-132 1.35e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 41.16  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRpcTCDFLTGPNTPSSAVSRLAQALLGAEEcKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202   159 ILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRE-SYELELRLKDGDGRWVWVEASAVPLRDG 235

                          90
                  ....*....|...
gi 1958656115 121 A-VIMFILNFEDL 132
Cdd:COG2202   236 GeVIGVLGIVRDI 248
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 19-152 2.32e-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: 41.11  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  19 IRKFEGQSRKflIANAQMENCA-------IIYCNDGFCELFGYSRVEVMQRPCTcDFLtGPNTPSSAVSRLAQALLGAEE 91
Cdd:COG5809   136 LRESEEKFRL--IFNHSPDGIIvtdldgrIIYANPAACKLLGISIEELIGKSIL-ELI-HSDDQENVAAFISQLLKDGGI 211

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656115  92 CKVDILYYRKDASSFRCLVDVVPVkNEDGAVIMFILNFEDLaqllaksSSRSLTQRLLSHS 152
Cdd:COG5809   212 AQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDI-------TERKKLEELLRKS 264
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 588-678 3.56e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 40.47  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115 588 LLQHCPAfrgaskGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR----DDVVVAILGKNDIFGEP--A 661
Cdd:PLN02868   15 LLQRLPS------SSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGpaeeESRPEFLLKRYDYFGYGlsG 88

                          90
                  ....*....|....*..
gi 1958656115 662 SLHarpgksSADVRALT 678
Cdd:PLN02868   89 SVH------SADVVAVS 99
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 37-63 4.54e-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: 4.54e-03
                           10        20
                   ....*....|....*....|....*..
gi 1958656115   37 ENCAIIYCNDGFCELFGYSRVEVMQRP 63
Cdd:smart00091  19 LDGRILYANPAAEELLGYSPEELIGKS 45
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 41-126 8.81e-03

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: 36.16  E-value: 8.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  41 IIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                  ....*.
gi 1958656115 121 AVIMFI 126
Cdd:pfam08447  81 KPVRVI 86
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 37-132 8.90e-03

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: 36.89  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656115  37 ENCAIIYCNDGFCELFGYSRVEVMQRPCTcDFLTGPNtpsSAVSRLAQALLGAEECKVDIL---YYRKDASSFRCLVDVV 113
Cdd:TIGR00229  21 LEGNILYVNPAFEEIFGYSAEELIGRNVL-ELIPEED---REEVRERIERRLEGEPEPVSEerrVRRKDGSEIWVEVSVS 96

                          90
                  ....*....|....*....
gi 1958656115 114 PVkNEDGAVIMFILNFEDL 132
Cdd:TIGR00229  97 PI-RTNGGELGVVGIVRDI 114
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH