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Conserved domains on  [gi|27886667|ref|NP_653234|]
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potassium voltage-gated channel subfamily H member 8 [Homo sapiens]

Protein Classification

PAS and CAP_ED domain-containing protein( domain architecture ID 13822798)

protein containing domains PAS, CAP_ED, and PRK11753

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
 175-615 2.70e-31

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 132.68  E-value: 2.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   175 SGHLQRREKNKLKINNNVFVDKPAF--PEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIgndDLS 252
Cdd:PLN03192   13 KGTGEEDDSGSLSLRNLSKVILPPLgvPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFL---NAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   253 TTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIF-EARSICIHYVTTWFIIDLIAALPFDLLYAF---------NVT 322
Cdd:PLN03192   90 PKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLitgtvklnlSYS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   323 VVSLVHLLKTVRLLRLLRLLQKLDRYSqHSTIVLTLLMSMFALLAHWMACIWYVIGkmEREDNSLLKWevgwlheLGKRL 402
Cdd:PLN03192  170 LLGLLRFWRLRRVKQLFTRLEKDIRFS-YFWIRCARLLSVTLFLVHCAGCLYYLIA--DRYPHQGKTW-------IGAVI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   403 esPYYGNNTLGgpsIRsaYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSL 482
Cdd:PLN03192  240 --PNFRETSLW---IR--YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTME 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   483 YHTRTKDLKDFIRVHHLPQQLKQRMLEYFQTTWSVNNgIDSNELLKDFPDELRSDITMHLNKEILQ-LSLFECASRGCLR 561
Cdd:PLN03192  313 FRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEkVYLFKGVSREILL 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27886667   562 SLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVL----KDSMVLAILGKGDLIG 615
Cdd:PLN03192  392 LLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFG 449
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-135 1.71e-20

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 87.13  E-value: 1.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     40 FPIVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLeeKTEFKGEIMFYKKNGSPFWCLLDIVPIKNE 119
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITD--LFAEPEDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                           90
                   ....*....|....*.
gi 27886667    120 KGDVVLFLASFKDITD 135
Cdd:pfam13426   78 GGELVGIIAILRDITE 93
PRK11753 super family cl36052
cAMP-activated global transcriptional regulator CRP;
578-656 2.99e-04

cAMP-activated global transcriptional regulator CRP;


The actual alignment was detected with superfamily member PRK11753:

Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 43.43  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   578 LLRQGDALQAIYFVCSGSMEVL-KDS----MVLAILGKGDLIGAnLSIKDQVIKTNADVKALTYCDLQCIILKGLFEVLD 652
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLiKDEegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                  ....
gi 27886667   653 LYPE 656
Cdd:PRK11753  110 VNPD 113
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 175-615 2.70e-31

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 132.68  E-value: 2.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   175 SGHLQRREKNKLKINNNVFVDKPAF--PEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIgndDLS 252
Cdd:PLN03192   13 KGTGEEDDSGSLSLRNLSKVILPPLgvPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFL---NAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   253 TTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIF-EARSICIHYVTTWFIIDLIAALPFDLLYAF---------NVT 322
Cdd:PLN03192   90 PKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLitgtvklnlSYS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   323 VVSLVHLLKTVRLLRLLRLLQKLDRYSqHSTIVLTLLMSMFALLAHWMACIWYVIGkmEREDNSLLKWevgwlheLGKRL 402
Cdd:PLN03192  170 LLGLLRFWRLRRVKQLFTRLEKDIRFS-YFWIRCARLLSVTLFLVHCAGCLYYLIA--DRYPHQGKTW-------IGAVI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   403 esPYYGNNTLGgpsIRsaYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSL 482
Cdd:PLN03192  240 --PNFRETSLW---IR--YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTME 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   483 YHTRTKDLKDFIRVHHLPQQLKQRMLEYFQTTWSVNNgIDSNELLKDFPDELRSDITMHLNKEILQ-LSLFECASRGCLR 561
Cdd:PLN03192  313 FRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEkVYLFKGVSREILL 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27886667   562 SLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVL----KDSMVLAILGKGDLIG 615
Cdd:PLN03192  392 LLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFG 449
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 224-481 2.22e-22

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: 97.34  E-value: 2.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    224 WDWLILLATFYVAVTVPYNVCFIGNDDLSTTrsTTVSDIAVEILFIIDIILNFRTTYvsksgqvifearsICIHYVTT-W 302
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYFQPEEPLTTV--LEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpW 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    303 FIIDLIAALPFDL-LYAFNVTVVSLVHLLKTVRLLRLLRLLQKLDRYsqhSTIVLTLLMSM-----FALLAHWMACIWYV 376
Cdd:pfam00520   69 NILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGL---RTLVNSLIRSLkslgnLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    377 IGkMEREDNSLLKWevgwlhelgkrlESPYYGNNTLggpsirSAYIAALYFTLSSLTSVGFGNVSANTDAEK-------I 449
Cdd:pfam00520  146 IG-YQLFGGKLKTW------------ENPDNGRTNF------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiY 206

                          250       260       270
                   ....*....|....*....|....*....|..
gi 27886667    450 FSICTMLIGALMHALVFGNVTAIIQRMYSRWS 481
Cdd:pfam00520  207 FVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-135 1.71e-20

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 87.13  E-value: 1.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     40 FPIVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLeeKTEFKGEIMFYKKNGSPFWCLLDIVPIKNE 119
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITD--LFAEPEDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                           90
                   ....*....|....*.
gi 27886667    120 KGDVVLFLASFKDITD 135
Cdd:pfam13426   78 GGELVGIIAILRDITE 93
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 551-662 2.04e-20

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: 87.77  E-value: 2.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667  551 LFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQVi 625
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 27886667  626 kTNADVKALTYCDLQCIILKGLFEVLDLYPEYAHKFV 662
Cdd:cd00038   80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 551-666 7.13e-17

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: 77.83  E-value: 7.13e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     551 LFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQVI 625
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeeQIVGTLGPGDFFGELALLTNSRR 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 27886667     626 KTNADVKALTYCDLQCIILKglfEVLDLYPEYAHKFVEDIQ 666
Cdd:smart00100   81 AASAAAVALELATLLRIDFR---DFLQLLPELPQLLLELLL 118
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-137 1.36e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG2202   33 ILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                         90
                 ....*....|....*.
gi 27886667  122 DVVLFLASFKDITDTK 137
Cdd:COG2202  111 EITGFVGIARDITERK 126
PRK13557 PRK13557
histidine kinase; Provisional
 41-134 1.16e-15

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 81.64  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13557   54 PIVFANRAFLEMTGYAAEEIIGNNC--RFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131

                          90
                  ....*....|....
gi 27886667   121 GDVVLFLASFKDIT 134
Cdd:PRK13557  132 GDLVYFFGSQLDVS 145
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 560-670 1.52e-11

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: 65.01  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667  560 LRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQviKTNADVKAL 634
Cdd:COG0664    9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGE--PSPATAEAL 86

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 27886667  635 TYCDLQCIILKGLFEVLDLYPEYAHKFVEDIQHDLT 670
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLARRLR 122
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-133 1.16e-10

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: 59.57  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLL--DLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                         90
                 ....*....|..
gi 27886667  122 DVVLFLASFKDI 133
Cdd:cd00130   92 EVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 94-135 4.13e-09

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: 52.96  E-value: 4.13e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 27886667      94 KGEIMFYKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITD 135
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 42-137 8.95e-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: 48.83  E-value: 8.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKG-EIMFYKKNGSPFWCLLDIVPIkNEK 120
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRNVL--ELIPEEDREEVRERIERRLEGEPEPVSeERRVRRKDGSEIWVEVSVSPI-RTN 101

                           90
                   ....*....|....*..
gi 27886667    121 GDVVLFLASFKDITDTK 137
Cdd:TIGR00229  102 GGELGVVGIVRDITERK 118
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
578-656 2.99e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 43.43  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   578 LLRQGDALQAIYFVCSGSMEVL-KDS----MVLAILGKGDLIGAnLSIKDQVIKTNADVKALTYCDLQCIILKGLFEVLD 652
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLiKDEegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                  ....
gi 27886667   653 LYPE 656
Cdd:PRK11753  110 VNPD 113
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 175-615 2.70e-31

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 132.68  E-value: 2.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   175 SGHLQRREKNKLKINNNVFVDKPAF--PEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIgndDLS 252
Cdd:PLN03192   13 KGTGEEDDSGSLSLRNLSKVILPPLgvPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFL---NAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   253 TTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIF-EARSICIHYVTTWFIIDLIAALPFDLLYAF---------NVT 322
Cdd:PLN03192   90 PKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLitgtvklnlSYS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   323 VVSLVHLLKTVRLLRLLRLLQKLDRYSqHSTIVLTLLMSMFALLAHWMACIWYVIGkmEREDNSLLKWevgwlheLGKRL 402
Cdd:PLN03192  170 LLGLLRFWRLRRVKQLFTRLEKDIRFS-YFWIRCARLLSVTLFLVHCAGCLYYLIA--DRYPHQGKTW-------IGAVI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   403 esPYYGNNTLGgpsIRsaYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSL 482
Cdd:PLN03192  240 --PNFRETSLW---IR--YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTME 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   483 YHTRTKDLKDFIRVHHLPQQLKQRMLEYFQTTWSVNNgIDSNELLKDFPDELRSDITMHLNKEILQ-LSLFECASRGCLR 561
Cdd:PLN03192  313 FRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEkVYLFKGVSREILL 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27886667   562 SLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVL----KDSMVLAILGKGDLIG 615
Cdd:PLN03192  392 LLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFG 449
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 224-481 2.22e-22

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: 97.34  E-value: 2.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    224 WDWLILLATFYVAVTVPYNVCFIGNDDLSTTrsTTVSDIAVEILFIIDIILNFRTTYvsksgqvifearsICIHYVTT-W 302
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYFQPEEPLTTV--LEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpW 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    303 FIIDLIAALPFDL-LYAFNVTVVSLVHLLKTVRLLRLLRLLQKLDRYsqhSTIVLTLLMSM-----FALLAHWMACIWYV 376
Cdd:pfam00520   69 NILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGL---RTLVNSLIRSLkslgnLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    377 IGkMEREDNSLLKWevgwlhelgkrlESPYYGNNTLggpsirSAYIAALYFTLSSLTSVGFGNVSANTDAEK-------I 449
Cdd:pfam00520  146 IG-YQLFGGKLKTW------------ENPDNGRTNF------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiY 206

                          250       260       270
                   ....*....|....*....|....*....|..
gi 27886667    450 FSICTMLIGALMHALVFGNVTAIIQRMYSRWS 481
Cdd:pfam00520  207 FVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-135 1.71e-20

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 87.13  E-value: 1.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     40 FPIVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLeeKTEFKGEIMFYKKNGSPFWCLLDIVPIKNE 119
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITD--LFAEPEDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                           90
                   ....*....|....*.
gi 27886667    120 KGDVVLFLASFKDITD 135
Cdd:pfam13426   78 GGELVGIIAILRDITE 93
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 551-662 2.04e-20

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: 87.77  E-value: 2.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667  551 LFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQVi 625
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 27886667  626 kTNADVKALTYCDLQCIILKGLFEVLDLYPEYAHKFV 662
Cdd:cd00038   80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 551-666 7.13e-17

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: 77.83  E-value: 7.13e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     551 LFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQVI 625
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeeQIVGTLGPGDFFGELALLTNSRR 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 27886667     626 KTNADVKALTYCDLQCIILKglfEVLDLYPEYAHKFVEDIQ 666
Cdd:smart00100   81 AASAAAVALELATLLRIDFR---DFLQLLPELPQLLLELLL 118
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-137 1.36e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG2202   33 ILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                         90
                 ....*....|....*.
gi 27886667  122 DVVLFLASFKDITDTK 137
Cdd:COG2202  111 EITGFVGIARDITERK 126
PRK13557 PRK13557
histidine kinase; Provisional
 41-134 1.16e-15

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 81.64  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13557   54 PIVFANRAFLEMTGYAAEEIIGNNC--RFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131

                          90
                  ....*....|....
gi 27886667   121 GDVVLFLASFKDIT 134
Cdd:PRK13557  132 GDLVYFFGSQLDVS 145
PRK13559 PRK13559
hypothetical protein; Provisional
 41-135 3.75e-14

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 75.24  E-value: 3.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13559   67 PIVLANQAFLDLTGYAAEEVVGRNC--RFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGED 144

                          90
                  ....*....|....*
gi 27886667   121 GDVVLFLASFKDITD 135
Cdd:PRK13559  145 GRLLYFFGSQWDVTD 159
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 41-180 4.46e-14

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 76.80  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13558  172 PLIYINDAFERITGYSPDEVLGRNC--RFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDED 249

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   121 GDVVLFLASFKDITDTKvkitpedKKEDKVKGRsragthfdsaRRRSRAVLYHISGHLQR 180
Cdd:PRK13558  250 GTVTHYVGFQTDVTERK-------EAELALQRE----------RRKLQRLLERVEGLVND 292
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 560-670 1.52e-11

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: 65.01  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667  560 LRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQviKTNADVKAL 634
Cdd:COG0664    9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGE--PSPATAEAL 86

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 27886667  635 TYCDLQCIILKGLFEVLDLYPEYAHKFVEDIQHDLT 670
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLARRLR 122
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 42-133 1.16e-10

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: 59.57  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLL--DLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                         90
                 ....*....|..
gi 27886667  122 DVVLFLASFKDI 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.
 421-475 3.86e-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: 57.28  E-value: 3.86e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 27886667    421 YIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQR 475
Cdd:pfam07885   24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 573-652 3.52e-09

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: 54.92  E-value: 3.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    573 APGEYLLRQGDALQAIYFVCSGSMEVLKDS-----MVLAILGKGDLIGANLSIKDQviKTNADVKALTYCDLQCIILKGL 647
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGE--PRSATVVALTDSELLVIPREDF 82


                   ....*
gi 27886667    648 FEVLD 652
Cdd:pfam00027   83 LELLE 87
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 94-135 4.13e-09

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: 52.96  E-value: 4.13e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 27886667      94 KGEIMFYKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITD 135
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-128 3.56e-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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 48.87  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     42 IVYCSDGFCELAGFARTEVMQKSCSCKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                   ....*..
gi 27886667    122 DVVLFLA 128
Cdd:pfam08447   81 KPVRVIG 87
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 4-137 3.66e-07

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: 54.21  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667    4 MKGLLAPQ--NTFLDTIATRFDGTHSNFILANAQvakGFpIVYCSDGFCELAGFARTEVMQKscscKFLFGVETNEQLML 81
Cdd:COG5809    1 MKSSKMELqlRKSEQRFRSLFENAPDAILILDLE---GK-ILKVNPAAERIFGYTEDELLGT----NILDFLHPDDEKEL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 27886667   82 QIEKSLEEKTEFKGEIMF--YKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITDTK 137
Cdd:COG5809   73 REILKLLKEGESRDELEFelRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERK 130
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 42-137 8.95e-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: 48.83  E-value: 8.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKG-EIMFYKKNGSPFWCLLDIVPIkNEK 120
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRNVL--ELIPEEDREEVRERIERRLEGEPEPVSeERRVRRKDGSEIWVEVSVSPI-RTN 101

                           90
                   ....*....|....*..
gi 27886667    121 GDVVLFLASFKDITDTK 137
Cdd:TIGR00229  102 GGELGVVGIVRDITERK 118
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-133 4.18e-06

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: 46.64  E-value: 4.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     42 IVYCSDGFCELAGFARTEVMQKScsckfLFGVETNEQ------LMLQIEKSLEEKTEFkgEIMFYKKNGSPFWCLLDIVP 115
Cdd:pfam00989   23 ILYVNAAAEELLGLSREEVIGKS-----LLDLIPEEDdaevaeLLRQALLQGEESRGF--EVSFRVPDGRPRHVEVRASP 95

                           90
                   ....*....|....*...
gi 27886667    116 IKNEKGDVVLFLASFKDI 133
Cdd:pfam00989   96 VRDAGGEILGFLGVLRDI 113
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 42-137 5.34e-06

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: 50.36  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIkNEKG 121
Cdd:COG5809  163 IIYANPAACKLLGISIEELIGKSILE--LIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNG 239

                         90
                 ....*....|....*.
gi 27886667  122 DVVLFLASFKDITDTK 137
Cdd:COG5809  240 EVDGIVIIFRDITERK 255
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
42-137 1.48e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 48.69  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSCKFLFGvetnEQLMLQIEKSLEEKTEFK-GEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:COG3852   29 ITYVNPAAERLLGLSAEELLGRPLAELFPED----SPLRELLERALAEGQPVTeREVTLRRKDGEERPVDVSVSPLRDAE 104

                         90
                 ....*....|....*..
gi 27886667  121 GDvVLFLASFKDITDTK 137
Cdd:COG3852  105 GE-GGVLLVLRDITERK 120
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-137 6.98e-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. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 43.17  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667     42 IVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLEEKTEFKGEImFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:pfam08448   17 VRYANAAAAELFGLPPEELLGKTLAE--LLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEERHYELRLTPLRDPDG 93

                           90
                   ....*....|....*.
gi 27886667    122 DVVLFLASFKDITDTK 137
Cdd:pfam08448   94 EVIGVLVISRDITERR 109
PAS COG2202
PAS domain [Signal transduction mechanisms];
42-137 1.43e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.02  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFkGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG2202  159 ILYVNPAAEELLGYSPEELLGKSLL--DLLHPEDRERLLELLRRLLEGGRES-YELELRLKDGDGRWVWVEASAVPLRDG 235

                         90
                 ....*....|....*..
gi 27886667  122 D-VVLFLASFKDITDTK 137
Cdd:COG2202  236 GeVIGVLGIVRDITERK 252
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 548-645 1.72e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 45.48  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   548 QLSLFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLK----DSMVLAILGKGDLIGANLSikDQ 623
Cdd:PLN02868   12 SVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGpaeeESRPEFLLKRYDYFGYGLS--GS 89

                          90       100
                  ....*....|....*....|..
gi 27886667   624 VIKtnADVKALTycDLQCIILK 645
Cdd:PLN02868   90 VHS--ADVVAVS--ELTCLVLP 107
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 42-137 2.48e-04

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 45.11  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG5805  179 ILFINESIERLFGAPREELIGKNLL--ELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDG 256

                         90
                 ....*....|....*.
gi 27886667  122 DVVLFLASFKDITDTK 137
Cdd:COG5805  257 SVKGILVILRDITEKK 272
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
578-656 2.99e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 43.43  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886667   578 LLRQGDALQAIYFVCSGSMEVL-KDS----MVLAILGKGDLIGAnLSIKDQVIKTNADVKALTYCDLQCIILKGLFEVLD 652
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLiKDEegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                  ....
gi 27886667   653 LYPE 656
Cdd:PRK11753  110 VNPD 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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