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Database: UniProt
Entry: A0A915PMN9_9BILA
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ID   A0A915PMN9_9BILA        Unreviewed;       746 AA.
AC   A0A915PMN9;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JAN-2026, entry version 14.
DE   RecName: Full=Vesicle-fusing ATPase {ECO:0000256|ARBA:ARBA00012674, ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674, ECO:0000256|RuleBase:RU367045};
OS   Setaria digitata.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Setariidae; Setaria.
OX   NCBI_TaxID=48799 {ECO:0000313|Proteomes:UP000887581, ECO:0000313|WBParaSite:sdigi.contig145.g5203.t1};
RN   [1] {ECO:0000313|WBParaSite:sdigi.contig145.g5203.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) 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|ARBA:ARBA00056429, ECO:0000256|RuleBase:RU367045}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); 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|ARBA:ARBA00048883,
CC         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   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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   AlphaFoldDB; A0A915PMN9; -.
DR   WBParaSite; sdigi.contig145.g5203.t1; sdigi.contig145.g5203.t1; sdigi.contig145.g5203.
DR   Proteomes; UP000887581; Unplaced.
DR   GO; GO:0005795; C:Golgi stack; IEA:TreeGrafter.
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:0043001; P:Golgi to plasma membrane protein transport; IEA:TreeGrafter.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:TreeGrafter.
DR   GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR   FunFam; 1.10.8.60:FF:000026; vesicle-fusing ATPase isoform X1; 1.
DR   FunFam; 3.40.50.300:FF:000166; vesicle-fusing ATPase isoform X1; 1.
DR   FunFam; 2.40.40.20:FF:000012; Vesicle-fusing ATPase protein; 1.
DR   FunFam; 3.40.50.300:FF:000187; Vesicular-fusion ATPase SEC18; 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; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR054419; NSF_ATPase_lid.
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; PF02359; CDC48_N; 1.
DR   Pfam; PF21964; NSF_ATPase_lid; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367045};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU367045}; Hydrolase {ECO:0000256|RuleBase:RU367045};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, 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:UP000887581};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          1..82
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          255..402
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          538..674
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          680..707
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   746 AA;  82552 MW;  6301B7DE5DCD34C6 CRC64;
     MRVRKCPTDD LALTNCAILN ISALNGKEIK HILVKTGPAH HFVFSIRNHP SLKADEIAFA
     LSQRKWAKLS LDQEVEVQQF IFNNNQFIGS ITVAADFQSK KNQTPEPLNT DHMAREFSIQ
     FAGHAFTRGE LLVFKFDDDK GKSHTLALTV TSILGIDLSL ATNPQAVSHL KPAEIDSGQL
     LPNSVIIFDK AEDSLLNLIG KSKGKSAYRS IINPDWDFQK MGIGGLDKEF SGIFRRAFAS
     RVFPPEFIEQ LGMKHVRGIL LYGPPGTGKT LMARQIGKML NAREPKIING PQILDKYVGE
     SESNIRKLFA DAEEEWKRCG ASSGLHIIIF DEIDAICKQR GSVAGSTAVH DTVVNQLLAK
     MDGVDQLNNI LVIGMTNRKD MIDEALLRPG RMEVQMEISL PDEAGRLQIL KIHTARMREY
     DKLDPNVDLI ELAKKTKNFS GAELEGLVRA AQSSAMNRLV KAGGKVQLDA DAVEKLMINV
     DDFNYALEND VKPAFGHSNE ELEKYLIGGF ISWSAQVAQI LEQGALLVKQ VRSPDTKGFA
     SVLLAGSPNS GKTCFAAMIA KASDYPFIKV ISAEDMVGYT ETAKCATLRK VFDDAYRSPL
     SCVIVDGVER LLDFSPIGPR YSNLVLQALF LLVKKLPPQN RRLLVIATSS NRSFLRELGL
     LSAFCTIIDV PALTTVQHIM AVIEDTNALS RQECEEIRNE LSRANKEYFI GIKKLLNVVD
     MARECEPVDR VSVVVQSLMS ETFSNS
//
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