ID A0A1I8GTJ5_9PLAT Unreviewed; 747 AA.
AC A0A1I8GTJ5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Vesicle-fusing ATPase {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0003093-snap-gene-0.4-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0003093-snap-gene-0.4-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A1I8GTJ5; -.
DR WBParaSite; maker-uti_cns_0003093-snap-gene-0.4-mRNA-1; maker-uti_cns_0003093-snap-gene-0.4-mRNA-1; maker-uti_cns_0003093-snap-gene-0.4.
DR Proteomes; UP000095280; Unplaced.
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; -; 2.
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; IPR029067; CDC48_domain_2-like_sf.
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; 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|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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 250..397
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 538..660
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 747 AA; 83464 MW; 531B6D8E740CE495 CRC64;
MAQSPQTFEA AKCPSDELSL TNQLFFHPED VLHSTTQHLV LQCGKGDFIF MLGTNPKMTR
GQVGFSLIQR RWTNVSIGEK VFIKLSHKFD PRKAAIAHLL VEADFLLKKN ATNDPYNTDD
MRVEFTQCFP QMPLTVGQEL VFKYKDKRHL LLRVKELELL LPDGRTEPAK TGIVSGNTIV
TFEKLSADSP LTLTGKAKGK QVYQSIINPD WNFSMMGIGG LDREFSDIFR RTFASRIFPP
DLVEQLGMNH VRGLLLYGPP GTGKTLMARQ IGKMLNAREP KIVNGPSILD KYVGESESKI
RQLFAEAEEE YKRVGNNSAL HIIIFDEIDA ICKTRGSVGG GTQVHDTVVN QLLTKMEGVE
PLNNILVIGM TNRKDMIDEA LLRPGRFEVQ MEISLPDQHG RLQILEIHTG QLRKNGKLAQ
DVDVQELAKE TKNFSGAELA GLVRAATVTA MNRLVQASDT VRLDPDAVDR LLVQRGDFMH
ALEHDVKPAF GTQEEELDRY ITGGIIDWGE PVQHIVQNGS LATRAARAEA EQSLDSGRPV
ALLLEGPPNS GKTALAVHIA RQSGFSYVRL CTSKRMIGYS EVAKCQAIKQ HFDDAHKAKQ
AVIILDGLEG LIDYSPVGPR YSNYVLQALR DLITAPLPKN RSLLLLGTTS CREALLELGL
VQCFTAGKIH VSNLTNSDEL LEALKKVDSA EFTKEELDRI KKETQNRHLN VGIKELLDVV
RMTNRVEEMD RVRYFLDRLI EDGRLQE
//
