ID A4H9S2_LEIBR Unreviewed; 463 AA.
AC A4H9S2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=P-type H+-ATPase, putative {ECO:0000313|EMBL:CAM38148.1};
DE EC=3.6.3.6 {ECO:0000313|EMBL:CAM38148.1};
GN Name=H1A-2 {ECO:0000313|EMBL:CAM38148.1};
GN ORFNames=LbrM_18_1740 {ECO:0000313|EMBL:CAM38148.1};
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM38148.1, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM38148.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM38148.1,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:CAM38148.1}.
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DR EMBL; CADA01000013; CAM38148.1; -; Genomic_DNA.
DR AlphaFoldDB; A4H9S2; -.
DR STRING; 5660.A4H9S2; -.
DR VEuPathDB; TriTrypDB:LbrM.18.1740; -.
DR VEuPathDB; TriTrypDB:LBRM2903_180021700; -.
DR InParanoid; A4H9S2; -.
DR OMA; WSESAVI; -.
DR Proteomes; UP000007258; Unassembled WGS sequence.
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 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; 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; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF48; PLASMA MEMBRANE ATPASE; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
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; 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 Hydrolase {ECO:0000313|EMBL:CAM38148.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 261..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..114
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50227 MW; D87AF42A297E69D1 CRC64;
MGLNGSEKDA AAFEEKPTSP LGAEMPPQKP QRRQSVLSKA VSEHDVNATG PMGELLPPSK
GLTTEEAEEL LAKYGRNELP EKRTPSWLIY VRGLWGPMPA ALWIAIIIEF ALENWPDGAI
LLVIQIANAT IGWFETIKAG DAVAALKNSL KPTATVYRDS KWQQIDAALL VPGDLVKLAS
GSAVPADCSI NEGVIDVDEA ALTGESLPVT MGPEHMPKMG SNVVRGEVEG TVQYTGTLTF
FGKTAALLQS VESDLGNIHV ILARVMIALC AISFVLCMCC FIYLLARFYE SFRRALQFAV
VVLVVSIPIA LEIVVTTTLA VGSKHLSKHK IIVTKLSAIE TMSGVNMLCS DKTGTLTLNK
MEIQEQCFTF EEGSDLHSTL VLAALAAKWR EPPRDALDTM VLGAADLDEC DNYEQLSFLP
FDPTTKRTAA TLGDRPTGVI FYWTKAAPHR ILQNGSSRFD FTA
//
