ID   A0A395GVD3_9EURO        Unreviewed;      1030 AA.
AC   A0A395GVD3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Vps52-domain-containing protein {ECO:0000313|EMBL:RAK99114.1};
GN   ORFNames=BO80DRAFT_495166 {ECO:0000313|EMBL:RAK99114.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK99114.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAK99114.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK99114.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the VPS52 family.
CC       {ECO:0000256|ARBA:ARBA00008180}.
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DR   EMBL; KZ824449; RAK99114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395GVD3; -.
DR   STRING; 1448316.A0A395GVD3; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_495166; -.
DR   OrthoDB; 2723231at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007258; Vps52.
DR   InterPro; IPR048361; Vps52_C.
DR   InterPro; IPR048319; Vps52_CC.
DR   PANTHER; PTHR14190; SUPPRESSOR OF ACTIN MUTATIONS 2/VACUOLAR PROTEIN SORTING 52; 1.
DR   PANTHER; PTHR14190:SF7; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 52 HOMOLOG; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF20655; Vps52_C; 1.
DR   Pfam; PF04129; Vps52_CC; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          159..330
FT                   /note="Vps52 coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF04129"
FT   DOMAIN          347..661
FT                   /note="Vps52 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20655"
FT   DOMAIN          662..1027
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1030 AA;  112836 MW;  4E2A16AF087AFE82 CRC64;
     MWLDRISGHS TPSGPQFDSR SNSPLPRRTS SRLAPNPPTT RPGSTRPGSS LSLLSTPNDS
     TTSLPATARG ESSTPKPGAA RPRPSDVADP FEVLNGIIGK QSKGGDGSPA SLLETKPSEL
     VEDIDFRGLS LEDFVAENDE PRRSLKSDVG AQTIQQFEKE RDKFQDLHSA ITGCDDVSKS
     VEMYLNDFQN ELGAVSAEIE SLQSRSIQLN AMLENRRNVE QLLGPAVEEI SLSPKTVRLV
     AEGPIDDNWV KALNEIETRT ASIEAKVSGS NSSKSIEDVR PLLGDIKKKA VERIRDYLVS
     QIRALRSPNI NAQIIQQQRL VKFKDLYGYI SRAHPTLTGE ITQAYINTMR WYYLSHFTRY
     HQALEKIKVF PSDRNEVLGG DPSSHKTGNI VPGGRAGSAA HDPFSLGRRV DILRTGNHMA
     ISSYLAEEDT SFHGLEVPFR NFNLALLDNI SAEYSFMTEM FSPLGFKQIS RKAVEIFEPV
     FALGQNMTKH LIEQTTDALG VLICVRLNQQ AAFELQRRKV PVADSYINGI NMQLWPRFQV
     IMDTQCESLK RVAANTGRSA VSALSIAGGD DLNKSSAPHF LTQRFGQLLH GIMVLSSEAG
     DDEPVANSLA RLTAEFDNLL AKLSRIGGDA KRRERFLYNN YSLVLAIISD TQGKLATEQK
     QVIGAGVVGL AVARQLAMKE GTSTILLERH AAPGTETSSR NSEVIHAGLY YGADTLKTHL
     CIKGKELLYA LCHQHNIPHR NTKKWIVAQT PEQWAACLRV HEHAQRIGVP TRILGPEEAR
     RREPEVQALA GVVESPTTGI VDSHSLMTYL QGDFEDRGGD CAFLTRVTGI EPLEGEKGYR
     IRAVSADGTE TTITAETVVN SAGNAACEIS NLLLPESRHR KAYFAKGTYF SYSASKPTTS
     VLVYPATLPG LGGLGTHLTL DMAGRIRFGP DVEWVEDAND LRPSPARLQQ ALPEIRAYLP
     NVDVEAIELD YCGIRPKLGK GGAVNTGKGF QDFVIQEEDG FPGFVNLLGI ESPGLTSSLA
     IGEMVRDILY
//