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Database: UniProt
Entry: E9AF31_LEIMA
LinkDB: E9AF31_LEIMA
Original site: E9AF31_LEIMA 
ID   E9AF31_LEIMA            Unreviewed;      1109 AA.
AC   E9AF31;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Putative calcium motive p-type ATPase {ECO:0000313|EMBL:CBZ12835.1};
DE            EC=3.6.3.- {ECO:0000313|EMBL:CBZ12835.1};
GN   ORFNames=LMJF_35_2080 {ECO:0000313|EMBL:CBZ12835.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CBZ12835.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CBZ12835.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CBZ12835.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FR796431; CBZ12835.1; -; Genomic_DNA.
DR   RefSeq; XP_003722601.1; XM_003722553.1.
DR   AlphaFoldDB; E9AF31; -.
DR   STRING; 5664.E9AF31; -.
DR   EnsemblProtists; CBZ12835; CBZ12835; LMJF_35_2080.
DR   GeneID; 12982505; -.
DR   KEGG; lma:LMJF_35_2080; -.
DR   VEuPathDB; TriTrypDB:LmjF.35.2080; -.
DR   VEuPathDB; TriTrypDB:LMJFC_350028200; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_350027300; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_350026600; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   HOGENOM; CLU_002360_3_0_1; -.
DR   InParanoid; E9AF31; -.
DR   OMA; FGIDDYI; -.
DR   Proteomes; UP000000542; Chromosome 35.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008554; F:P-type sodium transporter activity; IBA:GO_Central.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; IBA:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF14; SODIUM TRANSPORT ATPASE 1-RELATED; 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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:CBZ12835.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT   TRANSMEM        138..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        356..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        885..906
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        926..944
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        965..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1000..1020
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          83..158
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1109 AA;  122083 MW;  72EF8414628DBB07 CRC64;
     MTIEMTKKSI SLSADLAAKG LEESDDSQHL PVFSGEKLNG RALGDGAENG TAVVADAKEH
     HAMNFGDEQG DEPTPEAYDA RDKFWALALE NVFNLVQLED PLAGIDATDA PRHAKELGDN
     VIPIKGGPSW IVILASQFKN AITIVLLIVI IISGVFGDWA EFGVVLFILF FNAFLGFYQE
     YGAERSLASL KQMTAGVAKV IRNGIPEIIF IDEVVVGDVI VLEQGASVPA DCRIFESNGL
     EVDEALLTGE ALPVVKHANV IRDPENRLAL GDRKNMVYRN TQVTQGRGKA VVVAGGLNTE
     MGKLAKRLND SKGSGKTALM KKLDYMMYFL FLCCAIAAVI VFAANKMRYT PATLSYATAV
     AIAILPESLC AVITVAMTFS VKRMAQQKCI VRKLPVLEVL GNVTDICSDK TGTLTENKMV
     VKKAVIGIDD MYSVGGAPYD THGDFFPAMR NGQEQQPVIM AHQQEVRYVY QFFKCAALCS
     TTVLHVSEED MDSLAGNGNP TEIAIQVMTW KAGLNRDKLE DEGWECITEY SFDSKIKRMS
     TAWENKAKRE LYLCTKGAPE RVVELCTYKI SEDGKLVSLT QQDREQVEWH IRDLAAQGLR
     TICFAYREDA TKIFPIPADE PFIDAYDRDQ VERDLVFLGI VGIYDPPRPE SRPSVVACQH
     AGICVRMLTG DHTSTAGSIA SMLNIIRRRD LDDPVKLQAG PDFDKVDPET IDGWADLPVV
     VGRCSPESKV KMIESLHRRK KVVAMTGDGF NDSPSIKIAD IGCAMGSGVD VTKGVADLVI
     TDDNFATIVK AVAEGRRISQ CIRKFVVHLL SSNVAEVIAL ICGLPISHGG ESVFILSPIE
     ILWLNMFTSA PPATGLSLDR ATDDILQVPP NTQGFFTIEL IADTVVYGFW LGAITLCGFA
     VVLYGFKSGP EGTDCNRHNG VGCDNIWTAR STAFGILYFG LLIHSYTVRH PRVSIFRMRW
     LDNKWICGSC VLGGALFVPI VYINAIAHGL FVHSMITWEW GVIAVGVMTF LAACETYKVI
     KNLIFPIRKV LVEVDEEEAE DVEEQRQREY NTFTRTMPDD RNVERIANEN LRMSFASLAG
     SVGTANTGSF RMPAQREKKK RIGLFRKRE
//
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