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Database: UniProt
Entry: A0C309_PARTE
LinkDB: A0C309_PARTE
Original site: A0C309_PARTE 
ID   A0C309_PARTE            Unreviewed;      1142 AA.
AC   A0C309;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=Chromosome undetermined scaffold_146, whole genome shotgun sequence {ECO:0000313|EMBL:CAK65176.1};
GN   ORFNames=GSPATT00034654001 {ECO:0000313|EMBL:CAK65176.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK65176.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK65176.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK65176.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR   EMBL; CT868037; CAK65176.1; -; Genomic_DNA.
DR   RefSeq; XP_001432573.1; XM_001432536.1.
DR   AlphaFoldDB; A0C309; -.
DR   STRING; 5888.A0C309; -.
DR   EnsemblProtists; CAK65176; CAK65176; GSPATT00034654001.
DR   GeneID; 5018359; -.
DR   KEGG; ptm:GSPATT00034654001; -.
DR   eggNOG; KOG0208; Eukaryota.
DR   HOGENOM; CLU_001828_0_0_1; -.
DR   InParanoid; A0C309; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006544; P-type_TPase_V.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   NCBIfam; TIGR01657; P-ATPase-V; 1.
DR   PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        103..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1039..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1069..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1108..1130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1142 AA;  130296 MW;  AC1A4CDB538B8A16 CRC64;
     MFKFSQNPYA IYFTPFMEQS LKCMTIQNLP NKKQMQLKIY NYQFLHQCCN FVILFIREYV
     IKIKTQLFGQ QYISMPFPVQ NSFVEGQHPL SQIQPIRISK ARIFLAILLS ISTAFLFALA
     LKYFKKLYQL FLFIDCSDES IATHYRIVAT SGEEFVCKKK IMFDKPYFVF KMLKYSFNSA
     GQFYQPIEFE IKGKTLTDII NLSSKQTREH NIKYFGTCQL KIPIESIFIY SLHAFTGPFN
     ILQYFAVAIW FAEKTVLQPV LILIFTVLTV YLNYFLYVRS RRRLQQLANI HQEVSIKEND
     QIKVINGADL LPGDLLILKD NQTLNCDCAI IQGDVIVNEA TLTGEGIPIP KSALPNQNSL
     FELEKMSQHC LFEGTKLIQV NNAQQNIAIV LRTGFTSLRG QYFRNVLFPE PPSMRFYIQA
     AKFIIEIAFI TSIIYGFLLI EYIPMEFKSS LLVLRFLDNI VWSIPPSMPI FFQICKTASL
     VRLEAKGVIG NNADKVESAG RIDTCCFDKT GTLTTLGFKA IKAFPEEEKP ILDAIMGCCH
     HLIKINGQLL GDPLEIEMLN FVGWQCNFNN NPLTIDGNGK TYTIHKIFDF SSSKSMMSVI
     VTDGSKYYLY AKGSPESINS ISIKKRDDLI EEFNLNAIKG YRVLGLAYKE LQSNQIDQQR
     EQLESQLNFV GLLVMENPLK SDTNEIITTL KESGLDIKVI SGDNPLTTIQ CGKLAGIINS
     DNEITFLDYN QQNQEIILQC NNNQQIIKEQ QPNSIQELES FIQTQQELAL TGKFLEFMTN
     KGNFFVEPKY SSSTFVKSQS KEKIFTEINQ IDIDDGSFGQ LTISIIKKTK VFARQKPEQK
     KLIIQIIQSF GRQVLMCGDG ANDCSAISQA QVGISFSEAD ASYTAPFSSK STSLDCVVKV
     LLQGKAATMT IIEVFQYQIS VNTLKFVAVL FTFLEAETFA DFQFTYTSII SNIPLLIFLC
     LSGPCDTLAK YNPLDDQFAI YNQIQIFNNL IWGVAGLIVN YFISTAVRDV HTCEIDEPID
     NCIPKPIEEL KKFGDIQSVM FMSLMFFFMT FAINLYISNP FKQRYYRNYL LLLWTILGFI
     LFFVSAIFPK GGKWAKLINV NDNAFKGYNW IMIAVVVIAS LIGFFTQAIL QKYLPSKKKI
     EF
//
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