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Database: UniProt
Entry: G3ANM8_SPAPN
LinkDB: G3ANM8_SPAPN
Original site: G3ANM8_SPAPN 
ID   G3ANM8_SPAPN            Unreviewed;       797 AA.
AC   G3ANM8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Vesicular-fusion protein SEC18 {ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN   ORFNames=SPAPADRAFT_71938 {ECO:0000313|EMBL:EGW32557.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW32557.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996502; EGW32557.1; -; Genomic_DNA.
DR   RefSeq; XP_007375833.1; XM_007375771.1.
DR   AlphaFoldDB; G3ANM8; -.
DR   STRING; 619300.G3ANM8; -.
DR   GeneID; 18875402; -.
DR   KEGG; spaa:SPAPADRAFT_71938; -.
DR   eggNOG; KOG0741; Eukaryota.
DR   HOGENOM; CLU_008037_2_0_1; -.
DR   InParanoid; G3ANM8; -.
DR   OMA; CFDNEIA; -.
DR   OrthoDB; 553800at2759; -.
DR   Proteomes; UP000000709; 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; 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; PF02359; CDC48_N; 1.
DR   SMART; SM00382; AAA; 2.
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|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:UP000000709};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          47..126
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          311..459
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          594..730
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   797 AA;  89115 MW;  B8C2FD7DD4DBD51C CRC64;
     MEKFGFQKVS NNPSQPGQPS ITHNIRIPHP QTPPAQMQPL RESFRKQLMV DNAPGNDVVV
     ANCVAVNPAD FAQVPDRAPV ILDGNFVYSI AKDERTKPGT IGLAGNMRTW GKWSLGQPVT
     IENYNIFQNG QQQQYLGAVD LFIDFKSRSR ANSNPINHDQ LVDLFLKKYE NQILQPTQVI
     YMEFNGAYFS VLVNSVQVID VNTKDHLPSF KDSDDLSTKG ILLKSTDVLF YPAEGSVINL
     TKNKSLKSRI FGGSSNVHHR PHARKQIINP DFKLEDLGIG GLDAEFQDIF RRAFNSRILP
     PDIAEKLDYK HCKGLLLYGP PGTGKTLIAR KLSKMLNGKE PKIVNGPEML SKYVGASEEN
     IRNLFKDAEA EYKQKGEDSD LHVIIFDELD SVFKQRGSAR SDGTGVGDNV VNQLLSKMDG
     VDQLNNILVI GMTNRLDLID TALLRPGRFE IQIEIALPDE KGRKDIFLIH TKKLRENDIL
     TPDVNFDELS ILTKNFTGAE IEGLCNSAKS YAISRHTKKG SLAQIDPETI ANLKITRNDF
     LLALNDIRPA FGTDEEDLSQ QAKHGIIQFN EAIRHVFEKG QSIVDVVRSS ETETLRSILL
     YGAAGVGKTA IATTLALNSD FPFIKMLSAE TLVGMGEARK IQEIDTVFRD VHKSPLNVLV
     IDKIENIINY NPIGPRFSND ILQVLMVYLT KKPPKGRRLL IIGTTSQYSV FKHMNLVDAF
     TDTIPIPPIK KVEEIGRVLE KLGFMTERDR EEILHQLSQY EINIGVKGLI DVLMVSKYSK
     DNVDEVVANI VEKMNAL
//
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