ID A0C2C2_PARTE Unreviewed; 1057 AA.
AC A0C2C2;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Chromosome undetermined scaffold_144, whole genome shotgun sequence {ECO:0000313|EMBL:CAK64939.1};
GN ORFNames=GSPATT00034416001 {ECO:0000313|EMBL:CAK64939.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK64939.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK64939.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK64939.1,
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT868035; CAK64939.1; -; Genomic_DNA.
DR RefSeq; XP_001432336.1; XM_001432299.1.
DR AlphaFoldDB; A0C2C2; -.
DR STRING; 5888.A0C2C2; -.
DR EnsemblProtists; CAK64939; CAK64939; GSPATT00034416001.
DR GeneID; 5018121; -.
DR KEGG; ptm:GSPATT00034416001; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; A0C2C2; -.
DR OMA; RRSQILW; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
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; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 99..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 904..923
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..998
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..110
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 814..996
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1030..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1057 AA; 117431 MW; 43BAD846F7C80BDF CRC64;
MSYKQQKDVE AQIQSQLSID DLTDLFKLNS INDGSSMQKV KQLGDDFGIA RKLNTDLKKG
FQDKSAIEKS KQLYGDNLPV EKEPTTLCEL ILECLEDTML QILLIAALVS TVIGMINEGV
KTGWTEGATI FFAIFLIISI TAGNNYLKER QFRQLRRKLD DGKCQVIRDG KVTEIQTKDI
VVGDLLIFNL GDLFGVDGLM VQGSAVKIDE SPMTGESDEI KKLPYIEMAQ QPHNQLNVNQ
EAARGHVSPF LISGTKCLDG TGQMIVLAVG QNTVSGKLKQ LLIQENPPTP LQQKLEGVAS
DIGKLGVLVS ILTFIALMGH LGYDCYLGKF PFLSIKTLQI IVESFMIAVT IIVVAVPEGL
PLAVTIALAY SVGKMKDEQN LVKNLSSCEI MGGANNICSD KTGTLTQNIM QVVALWTENQ
PFRDQKDTIE LMCESICYNS NAFPEKDPQT NKWVQIGNKT ECALLECADN FGYNFNQFRP
SDKVLRQLPF NSKRKKMSTV IYNQKSQYIR VYTKGASEII LAQCNKYIGN NGIEQMLDPQ
LRKQIYDNII QKFASDSLRT IAIAYRDLDP QSHGSNVRGQ IPQLTKVAQN IPEDDLDKDL
VLIAIAGIKD PIRPDVPNSI KQCHASGVKV RMVTGDNILT ATAIAKECGI LPTNREIGEW
EVVEGKKFRE FVGGLKDEQV DGKTVKVVGN KENFARVSRD MKVMARASPE DKYILVTGLI
AEGNVIAVTG DGTNDAPALK KADVGFAMGI TGSDVAKDAA DIILLDDNFS SIITAMKWGR
NIYDCIRKFI QFQLTVNLVA LFMSFLGAVV LKESPLNTIE MLWVLIMDTF ASLALATEPP
NITVLERQPY KRDDKIVSPT MNRTIVGGSI YQICVLCGIL FVLPQFMDLS IPTELAAQKY
HQNVVQMSIF FQTFVVMQVF NSITCRQLDY KTINPFANAC NNPLFWAVQT FTLVIQCVLI
QYGGKFVKVS HLTLQQHLLC LGFGLGSLIF SILVKIAVPE RWCQFVELFR EQEVQSADMD
TSLTSVLRRK STSRLGNQRK SMDQQGSQVK MSAQRLQ
//
