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Database: UniProt
Entry: A0A1V6PKT1_PENDC
LinkDB: A0A1V6PKT1_PENDC
Original site: A0A1V6PKT1_PENDC 
ID   A0A1V6PKT1_PENDC        Unreviewed;       838 AA.
AC   A0A1V6PKT1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Vesicular-fusion protein SEC18 {ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN   ORFNames=PENDEC_c002G06870 {ECO:0000313|EMBL:OQD77611.1};
OS   Penicillium decumbens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD77611.1, ECO:0000313|Proteomes:UP000191522};
RN   [1] {ECO:0000313|Proteomes:UP000191522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD77611.1}.
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DR   EMBL; MDYL01000002; OQD77611.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PKT1; -.
DR   STRING; 69771.A0A1V6PKT1; -.
DR   OMA; CFDNEIA; -.
DR   OrthoDB; 553800at2759; -.
DR   Proteomes; UP000191522; 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; 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:UP000191522};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          96..178
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          205..279
FT                   /note="CDC48"
FT                   /evidence="ECO:0000259|SMART:SM01072"
FT   DOMAIN          347..495
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          629..755
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  91712 MW;  A80B262CAB42369A CRC64;
     MFNRHNLPSV PNPFSSGGQH PSAQGYSNPN QAPARYDNIL APVTSTGDFR DDQDVPMTDA
     SIVTRGYGAP PPSMGRPSQM PARPPTGRPA GGPSWMLNPS KSPNENYTFG NLVAVSPQDI
     PPSRDGSDVL LLINDLYVLS ARPLEGLPPG LIGMSDPQRT WANIGMRDAV KVQLYDPFSQ
     GGQAYLGSAD IEVSFASVKK RVETPYDQDE LANAVIRNFE NQLFAPGQRI LMDHRSIPLL
     LHVKTVQRVD LTSEKADLSS GEVETNPLAR GIVTRHTQLN FFKDSQSGIN VKPSNRRPAA
     NSIIQPGFKF ENMGIGGLDS EFSTIFRRAF ASRIFPPGLV EKLGIHHVKG LLLYGPPGTG
     KTLIARQIGK MLNAREPKII NGPEVLNKYV GQSEENIRKM FADAEKEFKE KGDESGLHII
     IFDELDAVCK QRGSGAGGGT GVGDSVVNQL LSKLDGVDQL NNILLIGMTN RMDMIDEALL
     RPGRLEVHME ISLPDEHGRS QILKIHTEKM RTNNVMEDDV DLAELAHLTK NFSGAEIAGL
     VKSASSFAFS RHVKVGTMAS INDDVVNMKV NRADFHHALD EVKPAFGVSE EELSSRIQYG
     VIHYSNVIKE IMREGELFVK QVGQAEATPL FSVLLHGPPG SGKTALAARI AIDSGFPFIK
     LISPEDMVGF SEPAKIQHIS RIFDSAYKSQ TSIVVVDNIE RIIDWVPIGP RFSNSVLQAL
     MVFLRKQPTH GRRLLVLATT TERALMKQLD IYNSFNSDIM VPNVSSFGEL RYVMEQSGAF
     DAREIAQALE GVGGLADDGR VSVGIKKVLL GIETAKQDVD KVGRFVRVIN RAIEEAFS
//
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