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Database: UniProt
Entry: A0A1S8VPQ1_9FUNG
LinkDB: A0A1S8VPQ1_9FUNG
Original site: A0A1S8VPQ1_9FUNG 
ID   A0A1S8VPQ1_9FUNG        Unreviewed;       811 AA.
AC   A0A1S8VPQ1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=BSLG_05827 {ECO:0000313|EMBL:OON03979.1};
OS   Batrachochytrium salamandrivorans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON03979.1, ECO:0000313|Proteomes:UP000189906};
RN   [1] {ECO:0000313|EMBL:OON03979.1, ECO:0000313|Proteomes:UP000189906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS {ECO:0000313|EMBL:OON03979.1,
RC   ECO:0000313|Proteomes:UP000189906};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OON03979.1}.
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DR   EMBL; LYON01001180; OON03979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8VPQ1; -.
DR   STRING; 1357716.A0A1S8VPQ1; -.
DR   VEuPathDB; FungiDB:BSLG_05827; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000189906; Unassembled 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   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; 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; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005782; P-type_ATPase_IIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 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; 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|RuleBase:RU361146};
KW   Calcium {ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {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|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
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        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        92..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        567..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        641..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        738..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          591..793
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
SQ   SEQUENCE   811 AA;  88824 MW;  6493769336A30A43 CRC64;
     MVFSGTSITV GKASAIVVFT GVKTAIGQIH DSISSQIEEK TPLKVALDEF GEQLAKIISV
     ICLLVWVINI RHFNDPTFGG NWIKGAVYYF KIAVALAVAA IPEGLAVIIT TCLALGTKKM
     ANQGAIVRKL RSVETLGCTR IICSDKTGTL TTNQMSVRKV MVFKQANAML NIEIQGNTYG
     PEGRVLLDGS PAPANLLVDN PSLNELTHIC AICNDSKIIY DEETDTFQKI GEPTEAALKT
     LVEKMGTDDL AFNKKLPVIP DSAALAALDS KEKMWRVSQV DERIESQYHR ISTMEFSRDR
     KSMSVLADCG PTGKRVHYVK GAPEQILERC NFVRLGASPH TATPMTPQLR SQILQTVSDW
     AESESLRVLA FATVDSPTVP DKPSMSDYIQ YESNMTFVGL VGMLDPPRPE VYDSIQRCYQ
     AGIRVIVITG DNKKTAEAIC RQIGIFDANS SDADLVGQSF TGREFDSMNE DEKRQAALTA
     NLFSRTEPTH KLALVELLKS EGFVVAMTGD GVNDAPALKR ADIGIAMGTG TDVAKLASDM
     VLVDDNFATI VSAVQEGRSI YSNTKQFIRY LISSNIGEVV SIFLTVVLGM PEALIPVQLL
     WVNLVTDGLP ATALGFNPSD AEIMRVGPRD AKEPIVTSWL FVRYMIIGIY VGAATVFGYA
     WWFIYFSAGP HITFYQLSHF HQCATLFPEI GCEMFTNVMS HKATTMSLSI LVVVEMLNAV
     NSLSENQSLL TFPLYKNLYL CAAIVLSMAL HVMILYVPFF TQLFSITPLN SEEWVAVLVI
     SAPVVLIDEI LKAVSRTFVV DASKAKKLKS D
//
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