ID   SEC18_CANAX             Reviewed;         794 AA.
AC   P34732;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Vesicular-fusion protein SEC18;
GN   Name=SEC18;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26555;
RX   PubMed=8212895; DOI=10.1002/yea.320090808;
RA   Nieto A., Sanz P., Sentandreu R., del Castilo Agudo L.;
RT   "Cloning and characterization of the SEC18 gene from Candida albicans.";
RL   Yeast 9:875-887(1993).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; X66467; CAA47077.1; -; Genomic_DNA.
DR   PIR; S37606; S37606.
DR   AlphaFoldDB; P34732; -.
DR   SMR; P34732; -.
DR   PRIDE; P34732; -.
DR   VEuPathDB; FungiDB:C1_13580W_A; -.
DR   VEuPathDB; FungiDB:CAWG_00094; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.300; -; 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; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039812; Vesicle-fus_ATPase.
DR   PANTHER; PTHR23078; PTHR23078; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54585; SSF54585; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; ER-Golgi transport; Nucleotide-binding;
KW   Protein transport; Repeat; Transport.
FT   CHAIN           1..794
FT                   /note="Vesicular-fusion protein SEC18"
FT                   /id="PRO_0000084569"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         317..324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         600..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   794 AA;  88926 MW;  35A22E62C196F67D CRC64;
     MEKLGFHKVS NSPSSPSQPK ITHNRPIPHP QSPPLPQRPL SEPLKKQLLV DNSPGNDVVI
     ANCVAVNAQD FQNIPDRAPV ILDGVFVYSI AKDDRVRPGT IGLAGNMRTW GKWSLGQPVN
     VENYNIFHNG QQQQYLGAID LSIDFRAKAR ANSNPINHDE LVALFLKNYE NQILQPTQVI
     YMEYTGIYFQ IRVNNVQIID VNTKDQLPSF KDSDDINTKG ILIKSTDVGF YPYEGSIINL
     TKPKTLKQRM FGGSTPHRTS RRKQIINPDF KLEDLGIGGL DAEFQDIFRR AFNSRILPPE
     LAEKLDYKHC KGLLLYGPPG TGKTLIARKL SKMLNGKEPK IVNGPEMLSK YVGASEENIR
     NLFKDAEAEY KLKGEDSDLH VIIFDELDSV FKQRGSGKSD GTGVGDNVVN QLLSKMDGVD
     QLNNILVIGM TNRLDLIDTA LLRPGRFEIQ IEISLPDEKG RKDIFLIHTK KLTENGILSS
     DVNFDELSTL TKNFTGAEIE GLCNSAKSYA ISRHTKKGAL AQIDPESIAK MKITRDDFLL
     ALNDIRPAFG TDEEDLSQQA QHGIIQFNQT IRNIFEKGQS IIDVVRSSET EHLRSILLYG
     PPGVGKTSIA TTLALNSDFP FIKMLSAETL VGMGELRKIQ EIDNVFRDVH KSPLNVLVID
     KIENIINYNP IGPRFSNDIL QVLMVYLTKK PPKGRRLLII GTTSQYQVFK HMNLIDSFND
     AIAVPPIKHI EEVGKVLDKL GFMNKSEREE ILSQLSRYDI NIGIKSLIDV LMVSKYSRDT
     VDEVVNNIVE KMSG