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Database: UniProt
Entry: D0NJX2_PHYIT
LinkDB: D0NJX2_PHYIT
Original site: D0NJX2_PHYIT 
ID   D0NJX2_PHYIT            Unreviewed;      1019 AA.
AC   D0NJX2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=PITG_12940 {ECO:0000313|EMBL:EEY59809.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY59809.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC         Evidence={ECO:0000256|RuleBase:RU361146};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; DS028142; EEY59809.1; -; Genomic_DNA.
DR   RefSeq; XP_002900494.1; XM_002900448.1.
DR   AlphaFoldDB; D0NJX2; -.
DR   STRING; 403677.D0NJX2; -.
DR   EnsemblProtists; PITG_12940T0; PITG_12940T0; PITG_12940.
DR   GeneID; 9478450; -.
DR   KEGG; pif:PITG_12940; -.
DR   VEuPathDB; FungiDB:PITG_12940; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_0_1; -.
DR   InParanoid; D0NJX2; -.
DR   OMA; IQHCKRA; -.
DR   OrthoDB; 847at2759; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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; 3.
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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
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; 2.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Ion transport {ECO:0000256|RuleBase:RU361146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        112..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        283..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        329..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        765..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        825..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        905..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        937..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          27..102
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1019 AA;  112089 MW;  7EC802AA156CD8B9 CRC64;
     MAFTLVTGDL IRLVETAHEK VGEQLESVGG LDGVATALHV DLRQGLDAND ADDLRRREDS
     FGRNYIPPPK AKSFFALMWD AFQDITIIIL TISGIFSIVL SSTVGDHKET GWVEGACIIL
     AVVVVTLVTA VNDYQKEQQF RSLNAVKEDE KIKVIRNGAP TEVGKWNLLV GDIVRVDLGD
     IIPADGMVFD EKELKMDESA MTGESDLLPK NRENPFLLSG TKVMEGLSKM LVVCVGENSQ
     AGIIKSLING TASKKTPKED KNKNSADGRQ ETDEIYSPLE GKLYNLTIFI GKLGTIVALL
     VFVIMAIRFS IDKFAVDDKP WKNGYISDYL NFFIIAITVL VVAIPEGLPL AVTIALAYSV
     KKMLVDNNLV RHLDACETMG SATTICSDKT GTLTTNRMTV MKIWIGDAEF SSATDSKGAV
     SDETKEALCH GVAINSTAEI LPPKVENGLP EHTGNKTECA LLQFIRDGGV EYADIRATNE
     IVHMLTFSSA KKRMSVVVRR GESKCRVYTK GATEVVLGLC KQMQRTDGAI EALSTARKSE
     IGSTVIDKYA SQGYRTLCLS YRDLDVPAVE LNTWADEDVE KDLTCIAIVG IEDPVRPEVP
     GAIQHCKRAG ITVRMVTGDN ITTARSIAGK CGIISQGDGS LVMDGQTFRS RVLDAQGNII
     QEQFDQIWPM LRVLARSSPK DKYTLVTGLM QSSLMPHGPQ VVAVTGDGTN DAPALKKANV
     GFAMGISGTA VAKDASDIIL MDDNFNSIVN AIKWGRNVYD SISKFLQFQL TVNVVAVLLA
     FIGAVVLEQS PLSAVQMLWP TQALLERKPY PKTQPLISKK MSKHILGQSI FQLALLLAIV
     FTGEKWFNVR SGRLNDLGED HKNDSTKHMT IVFNTFVWMQ LFNELNCRKI HDELNIFQGI
     TKNRVFLYVC VLQIAMQVVM VQLTGDWFNC TPLEIDQWLA CIAMGFISLP LGLVLRSIST
     KNAPSWMALC REVDVEQVRE ATSARGQQLW LQSFALIRAH IRVVKAFKKG LETKDLLQT
//
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