ID J9J2S8_9SPIT Unreviewed; 1419 AA.
AC J9J2S8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cation channel family protein {ECO:0000313|EMBL:EJY87094.1};
GN ORFNames=OXYTRI_06346 {ECO:0000313|EMBL:EJY87094.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY87094.1};
RN [1] {ECO:0000313|EMBL:EJY87094.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY87094.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY87094.1}.
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DR EMBL; AMCR01001580; EJY87094.1; -; Genomic_DNA.
DR EnsemblProtists; EJY87094; EJY87094; OXYTRI_06346.
DR OrthoDB; 38039at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR47823; ION_TRANS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47823:SF9; K+-CHANNEL ERG AND RELATED PROTEINS; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 503..607
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 870..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 595..660
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 870..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 166412 MW; 923974758FB33FBC CRC64;
MVIKMRSDSL RQGISSQKPL KIIQLIGINI VKPCSERLRQ AKDLLHLNRN GTFGTANENQ
KSLHYDNNLK PQDTLPFSEH SIHKQNSFQP HKNPSMLRMQ TKRFQNDFMQ SPLLDVDENI
VASSQSPGLR PSIQPELQQN ADGYKLIDTN QANSFQKYWI NPNSKLYEKW IFFLLFCNLV
WIQFTTPLRM SFEDKRYVYL PIAVGDLIVD ICFLIDSILT FFIPRTNTDG DYIFNRKLIA
KRYLLTYFIV DNIANIPYSI FKHYQRHQLK EDMQNFLIFN FAYTPRLFIA MLGIKLIRIR
KAKPQLRRFL KWIGLSVDKR NLLITVWSLI LMLHLVGCFW GAVGTFNYDS NESWIFEQKL
QDEDPLLQYI TSLYFAATTI MTVGYGDILP ITYWEKLFSS MIFIIGVAVF SFTLSTLASQ
FSDLNRSMSK RQSRDNQVQE LNSKFGLDKN IVRKIAYYFS HSESIISISQ EYEINKILKV
LPPFLKTNLA LFLYKEAIRE IPFLQNRDQN FYLDFLDLLI PLKFEKDTVI LKKKSKPEEI
LFILSGEVIN EQSNRVFTVG SIIGETDVYF NKRERIESFK AETNVYILMF DIDTVEQMVS
QYQDIRNDIE MIAKEREKDR LNRMNQKGQL EEQELKMKIL EELQNLLNRD LNRIKQNQTN
NALMKKVTMK IQDKNGMTSD EIFTQKLLAN TQMQSSFQKP KKYQQQEISL KESMRQSSEV
ISELKSQMLT QVQQDQEFER KSNVNQASFS FGEKSSKASP TYNFETIKKT FSQTKEKIKE
IELRKSLILT QNNILTFDRS SNLSSNQKQI DDLLLNDQEE YKEPITTQDG NLPFQMQISS
PVPQVLNNQK YFVTQFPIKQ LEIIEEFQEE KFSNSQQSDK QFKENDSDDY NPFANQHEQV
DDTSPPTLNF QRNETFTRNN SHESLSKKNS LHASRNYQNN KKSTTLSKIL GENHQLNFQQ
DFLNNQRRES DQNSNIYSSI DQQIGRNIQR FNQIVFIIKR SKLILNEYMK LFTNFIENIS
RKYNPKYNKI LSTIENKLLS PRIFLELIND IRTKMSDQNS NLDMIEGSLN VLEEKFGGKT
SSVRELEELL KRQIHLMSID EEEDSIQDSQ NSQPREDDDS FRGVNNHIIE ENMYLKAEIT
QEDDIYITLQ QNDTPSRKSK QRKMEKQIFI NQIDDSSLHQ YSDLYKLDDS QYYKALTSFK
HNDQLRMQNQ SYNRNYAIDI SSQGLTNSSS RQTHLDLTNI DFGLNSEKTL RNQAFNKFES
QQSNAVLKQE SGLLSYFNQK KYSVDNGIQR HADYFTSHQK FKTGQEDDQS LNNDNIKSSG
QTISNLTFQS QNVPFQINQN QIAQFKSAEE NNVKHIQAER QKFENQQNSN NQKAPKIKYS
QKKQKVNKIK ANIQSQLGIY SNKIGKKLTL LSRQPNMDF
//
