ID A0A158Q832_9BILA Unreviewed; 838 AA.
AC A0A158Q832;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Potassium voltage-gated channel protein eag {ECO:0000313|WBParaSite:EEL_0000631401-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000631401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000631401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A158Q832; -.
DR STRING; 1147741.A0A158Q832; -.
DR WBParaSite; EEL_0000631401-mRNA-1; EEL_0000631401-mRNA-1; EEL_0000631401.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1200.260; -; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR10217:SF435; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN EAG; 1.
DR PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01464; EAGCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 218..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..73
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 558..658
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 838 AA; 96437 MW; 4E43E88C24FE161A CRC64;
MPVVKRGLVA PQNTFLENVI RRCNNSDTNF ILANAQIVEY PIVYCNDGFA KMVGYSRAEI
MQKPCSLSFM HADYSGPEAV RKIQNALDMC QHEQTEIGLR KKNRSLLWLL MHIAPIKNDH
NQVVLYLCQF RDITPLKQPL DDENNKGFSR ILQIAKIAKS RQQFNQIETK DLHKTTSATS
SNFNQVMNLG GDLLPQYRQE TPKTSPHIIL HYSTFKTIWD WSILALTFYT AFIVPYNIAF
KTREHPPRGT IDMVALMDSI VDVIFFADIL LNFHTTFVGP GGEVVIDPNI IRYNYFKSWF
LIDLLSCLPY DIFYMFKHND ERMGSLLSAL KVVRLLRLGR VARKLDNYLE YGAATLLLLL
CAYVLAAHWL ACVWFSIGEY EVKIRFLVPS MPEGWLTKLS KELNLPFNYT FKDRLRLIGG
PQRSSAYISA LYFTMSCLST VGFGNIASTT DNEKVFGVCM MIIAALLYAA IFGHMTNIIQ
QMTSATIRYH DMIANVREFI KLQEVPNELA ERVMDYVIST WAMTKGIDTS KVLSYCPKDM
KADICVHLNR KVFNEHACFR LASDGCLRQF AVHLESNHAA PGDLIYHTGE SVDALWFVVS
GSLEVIQDDE VVAILGKGDV FGDEFWKQLG TGQSAANVRA LTYTDLHSIK KNKLMEVLDF
YKAFANSFAR NMVLTYNLTR RLKFRKVVDV KREKELDERR KNEKLTVPAE HPVRKLLFRM
RERYSTRILP SQIFADLERQ AKMRPPIIVR TTAASVDDSH EVRWSVDVQR NTDIKLPPEL
KMCFERIEEK LHTVNYISHK LENLEKLVFE LYHSMKGTSN YAFSHQISRY SSKKQRNA
//
