ID A0A0D2WVV7_CAPO3 Unreviewed; 946 AA.
AC A0A0D2WVV7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=CAOG_006786 {ECO:0000313|EMBL:KJE96463.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE96463.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) 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|ARBA:ARBA00038148, ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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; KE346371; KJE96463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2WVV7; -.
DR EnsemblProtists; KJE96463; KJE96463; CAOG_006786.
DR Proteomes; UP000008743; 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 CDD; cd02083; P-type_ATPase_SERCA; 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; 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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF102; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC/ENDOPLASMIC RETICULUM TYPE; 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 PRINTS; PR00121; NAKATPASE.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
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 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 257..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 726..747
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 799..823
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 8..40
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 750..917
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
SQ SEQUENCE 946 AA; 102518 MW; 8E4BD56BB2BF89D1 CRC64;
MFALLLTELP AEEGTPLWKL VLEQFDDLLV QILLAAAVIS FVLAIFDNEE GVSAFVEPLV
IILILIANAV VGVWQERNAE DAIEALKAYE PEIAKVVRNG ELTNIKAKQI VPGDIVEVAV
GDKIPADLRV IRIKSTTIRV DQAILTGESV SVIKQVEACG DARSVNQDKL SIMFSGTAVA
SGSAVGVVVG TGLNTAIGRI SKAMAETEEQ RSPLQKKLDE FGELLSKVIG VICILVWLIN
IGHFSDPAHG GSWFKGAIYY FKIAVALAVA AIPEGLPAVI TTCLALGSLR MAKKNAIVRN
LPSVETLGCT SVICSDKTGT LTTNQMSVSK MVVFRAGRAA GSTAPMEFSV SGTTFEPKGE
FTLGSKRVNP LAEAPNAVRE LAAIASLCNE ARISYDQGSK TYQKLGEATE AALAVLSEKL
AIDDARATLS AADLASSSRK VFESTYDKAF TLEFSRDRKS MSVYCVPKAG KKNVMFVKGA
PEGVIERCSF VRLADGSKVP LVPGDETHET IHKILLSYGT GSDTLRCLAL ATVDEPLAAN
KFDFTNAEKF KTYESNMTLV GIVGMLDPPR PEVRDSIQKC REAGIRVIVI TGDNKNTAEA
ICRRIGVFGE DEDLKGKSYT GREFDDLSPA EQKKAVLRAS LFSRTEPTHK SRLVELLQEH
GEISAMTGDG VNDAPALKKA EIGVAMGSGT EVAKSASKMV LADDNFSTIV SAVEEGRAIY
NNTKQFIRYL ISSNIGEVVC IFLTAALGMP EALVPVQLLW VNLVTDGLPA TALSFNPADS
DIMRKPPRKA DESMIDGWLF FRYMVIGTYV GVATVFAAAW WFLFYHAGPQ LSWEQLTDHL
GCDASVPGNY CHVFEDPHPA TMALSVLVTI EMFNALNSLS ENQSLFSMPP WTNRILLGAI
AMSMILHFAI LYIPFMSVSI VWGFVFFRFR LFLFGMVSLL LHHPDC
//