ID M9MDR2_PSEA3 Unreviewed; 879 AA.
AC M9MDR2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Vesicular-fusion protein SEC18 {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN ORFNames=PANT_12c00073 {ECO:0000313|EMBL:GAC74643.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC74643.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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 -!- 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 EMBL; DF196778; GAC74643.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MDR2; -.
DR STRING; 1151754.M9MDR2; -.
DR OrthoDB; 553800at2759; -.
DR Proteomes; UP000011976; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR CDD; cd00009; AAA; 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; IPR004201; Cdc48_dom2.
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 Pfam; PF02933; CDC48_2; 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 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:UP000011976};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 377..525
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 659..795
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 93166 MW; F216105062CBF0CB CRC64;
MAGFLRGGGS GGAGYGRVGD GSDPYRDGRN PYTSSSASSG RSAAPSGYGG GGAGYGGAGF
AGAGAGGAGR SAGAAGFRAG GAGFAGGAGG AGFSGGAGGA GGAGGGAPYA SEKSSAMPRR
GGGHLVVKCP EQLILSNCLI VNGQEWGSTQ YVLVEGMYVF TAQADPTGAI QPGTLGTAKL
QRQWAGLSAQ GQSVEAVPYD PFAFGNSVYL GSIDIEVAFI RKGEVAAQAY DTAEMAKVFA
RAFENHIFTT GQLLVFEFKG MNLIATIRGV EVVELHEIQQ RSQSAPQGGN TGSHPSRSDR
GILIAQTQIN FSATPDGGVK LKASGNRPPP NAILQPNFKF EDMGVGGLDK EFANIFRRAF
ASRIFPPALV EKLGIQHVKG MVLYGPPGTG KTLLARQIGK MLNAREPKIV NGPEVFNKYV
GGSEENVRKL FADAEKEQKD KGDESQLHII ILDELDAMVR QRGSGGAGAT SAGDNVVNTL
LAKLDGVEQL NNILVIGMTN RLDMIDEALL RPGRLEVHVE VSLPDEFGRR QILNIHTSKM
RTNGVMDGDV NIDELAALTK NFSGAEIAGL IKSATSFAFN RHVKVGTMAG ISNDVEDMKV
MHQDFLNALE EVKPAFGVAE EELSQVVQNG IMHFAPHIDV ILRDGHLRVE QVRTSQRTPL
VTVLLHGPPG SGKTALAATI AIASDYPFIK LISPESMIGM GDAQKINYLN KVFNDAYKSP
LSIVVIDNIE KIVEWVRIGP RFSNSVLQAL AVLLGKRPPK DKRLLVLATT SNRRMLHEME
MLNAFIAEIR VPNITSLRSV DHVVRQMQLF EHDGEAQRCQ QLLAQAGLGE EGKLNIGIKK
LLSEIEMARL DNDPADRLAS SLSSVQSTAI DVDIDVDLN
//
