ID A0A1I8GQM8_9PLAT Unreviewed; 759 AA.
AC A0A1I8GQM8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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_0002688-snap-gene-0.4-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0002688-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; A0A1I8GQM8; -.
DR WBParaSite; maker-uti_cns_0002688-snap-gene-0.4-mRNA-1; maker-uti_cns_0002688-snap-gene-0.4-mRNA-1; maker-uti_cns_0002688-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 Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR041569; AAA_lid_3.
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 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|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 2..51
FT /note="ATPase AAA-type core"
FT /evidence="ECO:0000259|Pfam:PF00004"
FT DOMAIN 78..116
FT /note="AAA ATPase AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17862"
FT DOMAIN 199..313
FT /note="ATPase AAA-type core"
FT /evidence="ECO:0000259|Pfam:PF00004"
FT REGION 573..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..520
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 664..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 84044 MW; 1215897076C55999 CRC64;
VHDTVVNQLL SKIDGVETLN NILVIGMTNR KDMIDEALLR PGRFEVQMEI SLPDEHGRHQ
ILSIHTSKIR DNGKLSPDVD VRELAAKTKN FSGAELAGLV RAATVTAMNR LVQASEKVQV
DPDAIEKLCV TRHDFLHALE YDIRPSFGAQ EEELDRYVTG GLVQWGNPVN HVIEHGLLAT
RAARAEAEAG ADSGRPVALL LEGPRNSGKT ALAVHIARQA GFSYVRLATS KNMVGFNEVA
KCMAVKKFFD DAHKAKQAVV ILDGLEGLID YSPVGPRYSN YVLQALRDLI TAPLPRNKCL
LLLGTTSCRD ALEELGLVQC FTAGKIHVSN LTQPEHLVTA LNQLDAAKFT EKEVRQIYKS
VSGCRLNIGI KELLDVARMT NRVEEGDRVR YFLDRLNEDG RLTDDNQSVK TATAFVITDV
TDTTNCNGND TEDAQMHDAT TTQVVEAETV GTATTALPDR LRKRLLSERK CRPTNEQLDQ
KLARAEQRRQ KQFAKRAASA REAEARCRRV AEAMETLHAR RPQSRAEVVQ RYVRLRHDLQ
EVLGRFNSEV ERTNCALFAG PPLLAFGGGL GYSPSTSSRT STSTTAATAS APTATTSTSS
SWQHRPATAF VVGQTNGNDA PAAAASAADA SISVEMPARL RQRLAAYPRR RGRHELKMAL
EKKLADAQRR KERYEQRRAE SIKETEERCR RISETMEEIS LQAPGPENQS EPQQPQEQPQ
EQRPEQQQTG NGEVCSSAGS RVFYRRVAKL QVDLDCLFT
//