ID A0A058Z5T6_FONAL Unreviewed; 1293 AA.
AC A0A058Z5T6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=H696_04044 {ECO:0000313|EMBL:KCV69625.1};
OS Fonticula alba (Slime mold).
OC Eukaryota; Rotosphaerida; Fonticulaceae; Fonticula.
OX NCBI_TaxID=691883 {ECO:0000313|EMBL:KCV69625.1};
RN [1] {ECO:0000313|EMBL:KCV69625.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38817 {ECO:0000313|EMBL:KCV69625.1};
RG The Broad Institute Genomics Platform;
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., Brown M., Walker B., Young S.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fonticula alba ATCC 38817.";
RL Submitted (APR-2013) 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}.
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DR EMBL; KB932206; KCV69625.1; -; Genomic_DNA.
DR RefSeq; XP_009496190.1; XM_009497915.1.
DR STRING; 691883.A0A058Z5T6; -.
DR EnsemblProtists; KCV69625; KCV69625; H696_04044.
DR GeneID; 20528769; -.
DR eggNOG; KOG0204; Eukaryota.
DR OMA; QWGYSIV; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000030693; 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; 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; 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; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000030693};
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 207..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 347..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 566..588
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 603..635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1121..1143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1155..1173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1194..1217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1223..1243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 293..362
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1293 AA; 136785 MW; DDE17FA8E52AAFBD CRC64;
MGVPAYEEGT TESAAAAAAG STRVRIAPQV LEQQDLMPSG EAGSASARPT TSSSRPRIRA
QILSTSDPTT DEHTASPSGK SAGSSALPAD RAPSRDLRDL ETVSPAEVGA GAGAGAGAGA
GAAATATMSP GPERMIATGD TDEAGAGAGA GAGAGTVTQA GPRTGIAIGG RNMAGDRTAA
TTTTPATATA LVMATTPRRL AILARNVATG AAVVASAPLM TGLCATITVA AMAATSLVVL
AVGSVALASM MVAAAVLPVV LLLIVVLGIP LAAAVGMWLA LVGRRRDPAA AVVPGPGPGL
LKVDPTRGVP NEDVHARQTV YGTNTIPKPP SVTFLELVWE ALQDPTLIML ICASLVSVAI
GIYEEVTRDR SGGSSGSQDN EYELGSWVEG VAIMVAVVAV VLVSAGNDYQ KERQFRKLNA
KREDRNVTVI RSGERLSISV YEVVVGDILI IDTGDVLCAD GVLLEGHDIQ CDESSLTGES
DAIKKIVCHG RQPGSDKDDA PVSSSKGSGP FLLSGSKVLQ GVGSMVVTCV GEHSMYGSTL
AAMSTGNENT PLQDKLADLS ETIGKIGLAV ALLMLFILIV KYCAIHAINK SWPSGASAIV
QDIVGFIITA VAVVVMAVPE GLPMAVTLAL AYATIQMLRD NNLVRILAAC ETMGGATTIC
SDKTGTLTQN RMTVVQVRAL SFFPGADVPL PLQVHAASFT DIEGSRNIPQ QIGTGLTEIL
AHGICINSNA AETVEDGVTT FLGSKTEVAL LEYIRAAAGF DYSIVRQANP IVRLVPFSSD
RKRMSTVVRL NNGKYRLYCK GAAEMVLANC LSYLSPDPLP GSVSISRSSS IIRSYLVSIE
SFANNALRAI CMAYRDFEAD EIESLTDDEF PSEANMTLIG IVGIQDPLRP EVPHAVRQCQ
QAGIRVRMVT GDNLMTARAI ARECGILSPT GIVMEGQVFR RLNPLQMSRI LPSLEVLARS
SPTDKQLLVR HLKEMGHVVA VTGDGTNDGP ALKLANVGFA MGIAGTEVAK EAAHIILMDD
NFASIVRAVV WGRGVFDAVR KFLQFQLTIN VVAVTLSFVS AISDPDGTAV LSAVQLLWVN
LIMDTLAALA LATEPPTDEL LQRPPHPKTG SLISRQMWKN ILGQSAFQLL VCFILYYLGF
GLFDLDSTSS VDRGVHRTIV FNTFVFMQFF NEVNCRVLDR SVNIFRGLHR HLSFILIMLL
TVAIQVLVVE FGGAAFRTHP LNWYQWLICI GIGFLSWPLG LVVRVIPISE KKVPPIETES
VTRGRLLWET AISDVRTQIR VVNQLRRHRE SYF
//
