ID G4VMW9_SCHMA Unreviewed; 743 AA.
AC G4VMW9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Vesicle-fusing ATPase {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_057320.1};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_057320.1}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_057320.1};
RG WormBaseParasite;
RL Submitted (DEC-2018) 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 RefSeq; XP_018653604.1; XM_018798687.1.
DR AlphaFoldDB; G4VMW9; -.
DR STRING; 6183.G4VMW9; -.
DR EnsemblMetazoa; Smp_057320.1; Smp_057320.1; Smp_057320.
DR GeneID; 8345781; -.
DR KEGG; smm:Smp_057320; -.
DR WBParaSite; Smp_057320.1; Smp_057320.1; Smp_057320.
DR CTD; 8345781; -.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; G4VMW9; -.
DR OMA; CFDNEIA; -.
DR OrthoDB; 553800at2759; -.
DR PhylomeDB; G4VMW9; -.
DR Proteomes; UP000008854; 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; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 252..399
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 537..734
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 743 AA; 81790 MW; 14030F651509849B CRC64;
MKFFAAKAPN EEVSLTNRVF FNPKDFNEKL SCVAIHTAAD KYVFRGGSHD HVPQGKVAFG
LAQRKWGNIS VDEPLDVQPY TFNLARECLA SAVLAVDFNN KKMSINEPLD SDRMALEFSM
QFADTPLTVG QHILYRFNKM TLLVEVKKLS TLSMDGGDVD NSKIGMLTGN TVIRWMPQPD
SKLLLIGKAA LDDDGASSIG GGGGYHSIIN PNWDFNQMGI GGLDKEFSAI FRRTFASRMF
PPAVAKQLGL KHVRGILLYG PPGTGKTLMA RQIGKMLNAR EPKIVNGPSI LDKYVGESEA
NIRKLFADAE EEEKRMGAKS ALHIIIFDEI DAICKSRGST GGGAGVHDTV VNQLLTNMDG
VNQLNNILVI GMTNRRDMID EALLRPGRFE MQMEISLPDE DGRLQILNIH TSKMQQAGKL
ARDVDLKELA AKTKNFSGAE IEGLCRAAAF TSMYQLISPS GKTQLDPDAF DRLLVKRSDF
LYALEHDVKP AFGASEEELS CYAPRGIMMW GESVSHALDM GRLAVSAVKE PDVETYRPLT
LLLEGPPKAG KTALAVEIAR LSGFPFVKIV TSHKMIGFTE MAKCAAMKKI FDDGAKSPLS
VVIVDNIEGL IEYNPVGPRF SNFIVQAIRD LVSQPLKAGR RMLVLATTSC REALTDQNLT
QAFSWHVHVA MLSRPEHLIA ALEEDGRFTS KEQQIIEKSL SGRRLCIGIK HLLDLIDLVS
KNDPDHRVAA FLAKLEEVGI VDE
//
