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Database: UniProt
Entry: A0A067JN78_JATCU
LinkDB: A0A067JN78_JATCU
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ID   A0A067JN78_JATCU        Unreviewed;       740 AA.
AC   A0A067JN78;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Vesicle-fusing ATPase {ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN   ORFNames=JCGZ_21445 {ECO:0000313|EMBL:KDP20974.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP20974.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP20974.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP20974.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
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|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU367045}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU367045}.
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DR   EMBL; KK915662; KDP20974.1; -; Genomic_DNA.
DR   RefSeq; XP_012091606.1; XM_012236216.1.
DR   AlphaFoldDB; A0A067JN78; -.
DR   STRING; 180498.A0A067JN78; -.
DR   GeneID; 105649544; -.
DR   KEGG; jcu:105649544; -.
DR   OrthoDB; 553800at2759; -.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
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   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 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; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
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   Pfam; PF02933; CDC48_2; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-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|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367045};
KW   ER-Golgi transport {ECO:0000256|RuleBase:RU367045};
KW   Hydrolase {ECO:0000256|RuleBase:RU367045};
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:UP000027138};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          11..94
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          249..396
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          529..667
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   740 AA;  81448 MW;  1B24D54CA164C10C CRC64;
     MAGRSGSAPT AMIVTNTPSP DLALTNLAYC SATDLHNFAV PGTKLFMALI GDSFVLSLSP
     HENIRPGHIA LNAIQRRHAR VSSGDSISVS RFIPPDDFNL ALLTLELEFV KKGTKNEQVD
     AILLANQLRK RFINQVMTTG QRVSFEYHGN NYIFTVNQAA VEGRERSNDL ERGMITSDTY
     FIFEASNSSG IKIVNQREAA SSNIFRHKEF NLQSLGIGGL SAEFADIFRR AFASRVFPPH
     VTSKLGIKHV KGMLLYGPPG TGKTLMARQI GKMLNGKEPK IVNGPEVLSK FVGETEKNVR
     DLFADAENDQ RARGDQSDLH VIIFDEIDAI CKSRGSTRDG TGVHDSIVNQ LLTKIDGVES
     LNNVLLIGMT NRKDLLDEAL LRPGRLEVQV EISLPDENGR LQILQIHTNK MKENSFLAPD
     VNLQELAART KNYSGAELEG VVKSAVSFAL NRQLSMDDLT KPVDEESIKV TMEDFLHALQ
     EIIPAFGAST DDLERCRLNG MVDCGDRHKH IYQRAMLLVE QVKVSKGSPL VTCLLEGPSG
     SGKTAMSATV GIDSDFPYVK IVSAESMIGL HESTKCAQIV KVFEDAYKSP LSIIVLDDIE
     RLLEYVAIGP RFSNLISQTL LVLLKRLPPK GKKLLVIGTT SEVGFLDSIG ICDSFSVTYH
     VPRLKADDAK KVLKQLNVFA EEDIDAAAEA LNDMPIKKLY MLIEMAAQGE HGGSAEAIYS
     GRQKIKIAHF YDCLQDVVRY
//
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