ID G0VJX6_NAUCC Unreviewed; 758 AA.
AC G0VJX6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Vesicular-fusion protein SEC18 {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN Name=NCAS0I01400 {ECO:0000313|EMBL:CCC71808.1};
GN OrderedLocusNames=NCAS_0I01400 {ECO:0000313|EMBL:CCC71808.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71808.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC71808.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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|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 EMBL; HE576760; CCC71808.1; -; Genomic_DNA.
DR RefSeq; XP_003678152.1; XM_003678104.1.
DR AlphaFoldDB; G0VJX6; -.
DR STRING; 1064592.G0VJX6; -.
DR GeneID; 11525481; -.
DR KEGG; ncs:NCAS_0I01400; -.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; G0VJX6; -.
DR OMA; CFDNEIA; -.
DR OrthoDB; 553800at2759; -.
DR Proteomes; UP000001640; Chromosome 9.
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 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; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
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 Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000001640};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 28..105
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 133..204
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 273..420
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 556..692
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84058 MW; BE2446AA687BA6DF CRC64;
MFKLPAFSKT GGHRVAPDMS NVDPSPRHLQ VTNCPNNSYA LANVAAVSPK DFPDNIYILV
DNLFVFTTKQ ANEVPPGTIG FNGNQRTWGG WSLNQEVQVR AFDLFKYSGK QSYLGTLDLE
ISFRSRGKAV NTPFDQDELA SHFVKCFESQ IFSPTQYLIM DFKGFFFDLK VRNVQAIDLG
DVEPSNSVST GIEVKGILTN KTQINFFKGR DGLVNLKSSN SLRPRSDAVI RSDFKFEDLG
VGGLDKEFTK IFRRAFASRI FPPAVIEKLG ISHVKGLLLF GPPGTGKTLI ARKIGTMLNA
REPKIVNGPE ILSKYVGSSE ENIRNLFKDA EAEYKAKGED SSLHIIIFDE LDSVFKQRGS
RGDGTGVGDN VVNQLLAKMD GVDQLNNILV IGMTNRKDLI DSALLRPGRF EVQVEIHLPD
EKGRLQIFEI QTKKMRENNM MDKDVDLAEL AALSKNFSGA EIEGLVKSAS SFAINKTVNI
GQGATKLNTK DITKLRVTRE DFMNALSEVT PAFGINEEDL KTCVEGGMII YSDRVNSILK
NGARYVRQVR ESDKSRLVSL LIHGPPGSGK TALAAAIALK SQFPFIRLIS PNELSGMSEN
AKIAYIDSTF RDSYKSPLNI LVIDSLETLV DWVPIGPRFS NNILQVLKVA LKRKPPQDRR
LLIMTTTSAY SVLQQMDILS CFDNEIAVPN MSSIDEFNNV MMDSKFLNDA DRVKVINELA
QISPKFNVGI KKALTNIETA RHDDDPVSEI VELMAQSV
//
