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Database: UniProt
Entry: L1JH95_GUITC
LinkDB: L1JH95_GUITC
Original site: L1JH95_GUITC 
ID   L1JH95_GUITC            Unreviewed;       996 AA.
AC   L1JH95;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Potassium channel domain-containing protein {ECO:0000259|Pfam:PF07885};
GN   ORFNames=GUITHDRAFT_106691 {ECO:0000313|EMBL:EKX47702.1};
OS   Guillardia theta (strain CCMP2712) (Cryptophyte).
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX47702.1};
RN   [1] {ECO:0000313|EMBL:EKX47702.1, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX47702.1,
RC   ECO:0000313|Proteomes:UP000011087};
RX   PubMed=23201678; DOI=10.1038/nature11681;
RG   DOE Joint Genome Institute;
RA   Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA   Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA   Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA   Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA   Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA   Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT   "Algal genomes reveal evolutionary mosaicism and the fate of
RT   nucleomorphs.";
RL   Nature 492:59-65(2012).
RN   [2] {ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA   Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA   Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA   Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA   Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA   Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA   Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:EKX47702}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
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DR   EMBL; JH992989; EKX47702.1; -; Genomic_DNA.
DR   RefSeq; XP_005834682.1; XM_005834625.1.
DR   AlphaFoldDB; L1JH95; -.
DR   PaxDb; 55529-EKX47702; -.
DR   EnsemblProtists; EKX47702; EKX47702; GUITHDRAFT_106691.
DR   GeneID; 17304318; -.
DR   KEGG; gtt:GUITHDRAFT_106691; -.
DR   eggNOG; KOG3684; Eukaryota.
DR   HOGENOM; CLU_300631_0_0_1; -.
DR   OrthoDB; 4200919at2759; -.
DR   Proteomes; UP000011087; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 2.
DR   InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR10153; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL; 1.
DR   PANTHER; PTHR10153:SF33; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011087};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        125..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        643..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        683..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        823..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        910..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          360..412
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          881..934
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          976..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  113071 MW;  2BAE74AA9B1DC870 CRC64;
     MGYSNRISND EAEQEGPVPQ QRQEEENEQQ QQEQQHLQQQ QQQQQQHSQE QEQEPARRKP
     AKLHPMEIQE QGSISASNVS VRDGRLASET SVTLLSHRPP LHITSNWRRN RAQVDKTMRN
     VRRGAALCGL MGCGFAVACD ELILYGVDAH AAACNLLKAA NTIATCAALS FLVYFYLLNG
     LLQRVNLHLR HLKALDTDFS LSSVALSSSF WAELVVCGLH LPPMTTFELG VWNWNNFILY
     RGETILAVIN TFRLYLLWPV LKDQVLQSLP KRHTISSFTN IPMGSSFVVK KVIRSKFSLL
     FITILWLISV FLFAFCILTA TGQRHRPGRS TSEARRKHEF LLLLAEFVPA EFEKKNDLWY
     QNAVWAMFVT STTIGYGDIL CTTHMSRFVA ILTAGTGLIL VSLMTAAFQN ALQWTEEEIA
     ANLVADREIA RLKAREHAAR LVQIKWKGLR GDRGRAEQRA ASLRAAFMKQ KKRTEVDLDD
     CLADSVKVDQ ISSSSKKIHG ALLDILKKTT PEVEHLSHPR KLFRRNSNLS QFVQGARQRN
     EQRKRRSSLG QEEGMGGSMK LKRKQAREQR RKTFNNILSS QLKVLAEQKR SDFDANLEHS
     ITMMETKTEG ARASFLRVLS FKPDPNKIRD WTSCRKEVET RQLLLRILSC VTSLVGLLAA
     VLTNELVLGG TSPRAPAINA LKWLNSIATV ACCIFLYSSY VFLIRAKRID RHVQLGKKLD
     LRVPFRSVAR RKGLWVELLV CLPHAPPHVA VELELVWMGN VVVYAGETVG CVWNALRMYL
     TWSLVMFLVL REIPMRSVIS HHTRVSFDAL FCLKRLLNRW TGFNVILIAW FVMMIIFGYL
     YRSVEFSFCL LPSATSAACQ QPQATEWEVA GSKFGKQNDV WLTNSFWFIF VTMTTVGYGE
     QVPTTILGRL IALLAATFGI LCASLTTAAL GNLILFTPAE FSAIAIMERE KAREDLRVIA
     ANMIRAWWLR QKGRNKEEEE EEEVTCAAWE READVE
//
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