ID Q4QED4_LEIMA Unreviewed; 1051 AA.
AC Q4QED4;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=Putative P-type ATPase {ECO:0000313|EMBL:CAJ03586.1};
GN ORFNames=LMJF_17_0600 {ECO:0000313|EMBL:CAJ03586.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03586.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ03586.1, 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:CAJ03586.1, 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).
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DR EMBL; FR796413; CAJ03586.1; -; Genomic_DNA.
DR RefSeq; XP_001682314.1; XM_001682262.1.
DR AlphaFoldDB; Q4QED4; -.
DR STRING; 5664.Q4QED4; -.
DR EnsemblProtists; CAJ03586; CAJ03586; LMJF_17_0600.
DR GeneID; 5650785; -.
DR KEGG; lma:LMJF_17_0600; -.
DR VEuPathDB; TriTrypDB:LmjF.17.0600; -.
DR VEuPathDB; TriTrypDB:LMJFC_170013500; -.
DR VEuPathDB; TriTrypDB:LMJLV39_170011900; -.
DR VEuPathDB; TriTrypDB:LMJSD75_170011600; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR InParanoid; Q4QED4; -.
DR OMA; MINVHDI; -.
DR Proteomes; UP000000542; Chromosome 17.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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 GO; GO:0005388; F:P-type calcium transporter activity; 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; 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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 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}.
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..44
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 811..984
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 113569 MW; 84EEF9F385BBCE49 CRC64;
MAQRRAWFSA NELPEAEETS FMDMIWESLE DRMVQILIVS AVVSLVLGLT VPDQDTGLVD
YAHGWIEGTA ILLSVTIVTL VSSINNYQKE QKFKELSKAT PPVKVQVVRS GTTLDITDKE
LLSGDLLNVA AGDVLTVDGL VLRSTSLKVD ESAATGENDD VAKSAHGDFV LRSGSNVTEG
EGTILVMGVG VHSFAGHIAM HVREAKEETP LQHKLEELAN LIGYMGMVAA GLMFVLLSGK
ELLDTVVYRK HPFGYKKYLD NLMTAVTIVV VAVPEGLPLS VTIALAYSMK QMFKENNLVR
HLAACETMGG ATTICTDKTG TITQNNMSVT DGVTAYGVAY VVPRRPSTFA GEDEKGSSGT
LAPLSPLLQA STSMNVSEAL GGAQAAGVRR LLMECIVMNT KATWVRVESL DAKQATVRLT
GSKTEQALLN FVDALGEDPM QLRSERLSRL NEEAMRTPSS PFSLVPWPTG LEGTSSNVVA
AAATFTKDLR IYPFTSARKR MATALVLRPE KLVRYYVKGA SELILAACTH TYDAQGERVG
LSHEVRMRLE EAIMAMARRQ LRTLAIAYTD YSLSADCSAT PQGSSDSDEG GAAPSSPFLE
DDTQLTGLTL VGIVGIRDPV RLEVPGAVAQ CRRAGVVVRM ITGDNKATAV SIAKEVGIYG
KVWSGPAEGE QGLALEGPQF RELAKSARKL NAILPRLQVI SRASPMDKHI LVSALMTRGE
VVAVTGDGTN DAPALKGANV GFSMNSGTEV AKLASDVVIL DDNFSTIVTA MKWGRNVHDN
ICKFLQFQMT VNVAAVVVSF TGALLDRNGD SPLKPVQLLW VNLIMDTLAA LALATETPSD
EVLLRPPKPK AAPLITRRMW LNIAGQSLYQ ILIQQYLLLG GANTLGLAVR DSEELHTLIF
NVFVLMQLSN EFNARILDNS VGFWHNLGNA PMFITVVGTM FLIQIVSVQY GGTLMQCVPL
PLASWVTSLA LGVVPLLLGF VLRRIGVVER EIPPPPPVVD TEEEAALQLA LKQHVCPTLQ
DTARKVRMQL RVLRAFRTNA QEQKASRTQS S
//
