ID A4HYS3_LEIIN Unreviewed; 738 AA.
AC A4HYS3; A0A2K4YSY3; A0A381MGQ9;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=Vesicle-fusing ATPase {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN ORFNames=LINJ_20_0820 {ECO:0000313|EMBL:CAM67461.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM67461.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM67461.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM67461.1,
RC ECO:0000313|Proteomes:UP000008153};
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).
RN [2] {ECO:0000313|EMBL:CAM67461.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM67461.1,
RC ECO:0000313|Proteomes:UP000008153};
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 -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC of transport vesicles within the Golgi cisternae. Is also required for
CC transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC function as a fusion protein required for the delivery of cargo
CC proteins to all compartments of the Golgi stack independent of vesicle
CC origin. {ECO:0000256|RuleBase:RU367045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000256|RuleBase:RU367045};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU367045};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU367045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU367045}.
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; FR796452; CAM67461.1; -; Genomic_DNA.
DR RefSeq; XP_001465214.1; XM_001465177.1.
DR AlphaFoldDB; A4HYS3; -.
DR SMR; A4HYS3; -.
DR STRING; 5671.A4HYS3; -.
DR GeneID; 5068629; -.
DR KEGG; lif:LINJ_20_0820; -.
DR VEuPathDB; TriTrypDB:LINF_200013000; -.
DR eggNOG; KOG0741; Eukaryota.
DR InParanoid; A4HYS3; -.
DR OMA; CFDNEIA; -.
DR OrthoDB; 553800at2759; -.
DR Proteomes; UP000008153; Chromosome 20.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1.
DR PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367045};
KW Cytoplasm {ECO:0000256|RuleBase:RU367045};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU367045};
KW Hydrolase {ECO:0000256|RuleBase:RU367045, ECO:0000313|EMBL:CAM67461.1};
KW Magnesium {ECO:0000256|RuleBase:RU367045};
KW Metal-binding {ECO:0000256|RuleBase:RU367045};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367045};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367045};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 251..398
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 532..668
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 738 AA; 81105 MW; EFBF6DD1F680BDB8 CRC64;
MSRYYSVCSV PTDNDTKTNC IFLNTVDFAE VAGPQAAATG NSFAVLVQGF PFTVCRSDVV
ERGAVAMNSI QRRLLGLSTG ARSTVVLEPF LSRVPNMRIL QIQVEPISAR QAIMLDCQAC
IAYMEKMYSG QYFRVTQQLA IVMDSGERMR ATVMTTELVE SKEVSAASLD IGRFSRGVTQ
VIITASEASG INLMNVSEAQ MDAQQPQLVR NFNLENLGIG GLRAEFGQVF RRAFASRMLK
PSFIKKLALK HVKGVLLYGP PGTGKTLIAR KIGEILNCHE PKIVNGPEVF NKFVGGTEEN
IRKLFADAEK EQAEKGDQSR LHLIIFDEFD AICKQRGAVR DSTGVNDNVV NQLLSKIDGV
NSLNNVLLVG MTNRLDLIDE AILRPGRFEV HVEIGLPDEP GRVEIFRIHT RGMRENNIMS
SDVSLEELGK MTKNYSGAEI EGVVRDATSN AFNRHIDLDH PDKMVDDANV HVTREDFMKA
VEEVTPAFGQ AKEECANLRR GGIIDYGDSW EVVKSRCKRY TDQLNAAGKR IDSLAVLIDG
APGSGKSAVS AYLAEVADFP YVKVVSAEDM VGYGEMQRVN ILRKAFEDAY KSPASCIILD
DLERLIDFSQ LGGRYSNTLL QALLVLTKRP PPEGKKLLVV GTTAQYDIMD SLELGACFSV
KLHLPSVPVS AIPKVCEGLG LAFASQQDMD SCLSLMSHDI PMKQLMLLLE MASEQKGSGR
PLITYHSMSR AKESVGGY
//
