ID Q6FK22_CANGA Unreviewed; 758 AA.
AC Q6FK22;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=Vesicular-fusion protein SEC18 {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN OrderedLocusNames=CAGL0M01782g {ECO:0000313|CGD:CAL0136325,
GN ECO:0000313|EMBL:CAG62398.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG62398.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG62398.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380959; CAG62398.1; -; Genomic_DNA.
DR RefSeq; XP_449422.1; XM_449422.1.
DR AlphaFoldDB; Q6FK22; -.
DR STRING; 284593.Q6FK22; -.
DR EnsemblFungi; CAGL0M01782g-T; CAGL0M01782g-T-p1; CAGL0M01782g.
DR GeneID; 2891192; -.
DR KEGG; cgr:CAGL0M01782g; -.
DR CGD; CAL0136325; CAGL0M01782g.
DR VEuPathDB; FungiDB:CAGL0M01782g; -.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; Q6FK22; -.
DR OMA; CFDNEIA; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0070300; F:phosphatidic acid binding; IEA:EnsemblFungi.
DR GO; GO:0000149; F:SNARE binding; IEA:EnsemblFungi.
DR GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:EnsemblFungi.
DR GO; GO:0048219; P:inter-Golgi cisterna vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:EnsemblFungi.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IEA:EnsemblFungi.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:EnsemblFungi.
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 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:UP000002428};
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"
SQ SEQUENCE 758 AA; 83584 MW; A99A7995F0B281ED CRC64;
MFKLPGFGKA SISHSPPDMS NVNIRPVTLC VTNCPNNTYA LANVAAVNPA DLPDNIYIIV
DNLFVFTTRH SNDVPAGTIG FNGNQRTWGG WSLNQDAQVK SFDLFKYAGK ASYLGTIDME
ITFRSRNKAV ATPFDQDELA AQFVANFESQ IFSPTQYMIM EFKGHYFDLK IRNLQAIDLG
DIDSSAPVSS GIEVKGILTK QTQINFFKGR DGLVNLKSPN SLRPRSNAVI RPDFKFEDLG
VGGLDKEFTK IFRRAFASRI FPPAVIEKLG ISHVKGLLLY GPPGTGKTLI ARKIGMMLNA
KEPKIVNGPE ILSKYVGSSE ENIRNLFKDA EAEYKSKGEE SSLHIIIFDE LDSVFKQRGS
RGDGTGVGDN VVNQLLAKMD GVDQLNNILV IGMTNRKDLI DGALLRPGRF EVQVEIHLPD
EAGRVQIFEI QTKKMRENNM MSPDVNLAEL AALTKNFSGA EIEGLVKSAS SFAINKSVNI
GQGATKIDPK NIAQLKVTRA DFLNALSEVT PAFGISEEDL KSCVEGGMFV YSERVNALLK
HGARYVRQVR ESEKSRLVSL LIHGPPGSGK TALSAAIALK SEFPFIRMIS PNELAGMSEA
AKISYIDNTF RDAYKSPMNI LVIDSIESLV DWVPIGPRFS NNILQVLKVA LKRKPPQDRR
LLILTTTSAY SVLQQMDILS CFDNEIAVPN LSTLDEFNNV MKEAQFLDDS GRMQVISQMQ
NAGTKINVGV KKVLTNIETA RHDDDPVNEL VELMTQSI
//
