ID   A0A395HSK4_ASPHC        Unreviewed;      1026 AA.
AC   A0A395HSK4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Vps52-domain-containing protein {ECO:0000313|EMBL:RAL09838.1};
GN   ORFNames=BO97DRAFT_472141 {ECO:0000313|EMBL:RAL09838.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL09838.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL09838.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL09838.1,
RC   ECO:0000313|Proteomes:UP000248961};
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; KZ824300; RAL09838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HSK4; -.
DR   STRING; 1450537.A0A395HSK4; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_472141; -.
DR   OrthoDB; 2723231at2759; -.
DR   Proteomes; UP000248961; 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:UP000248961};
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          727..984
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  113315 MW;  4F2E3EBDD1345A79 CRC64;
     MWLDRIAGHS TPSGSQIDSR SNSPLPRRTS SRLSPNIQNN RPGSSRQASS LSVLLTPSDS
     TTSLPATAAR DRSPLKQIAA RSRPSDVADP LDVLNGILGK QNGKRDLSPD GDLNVKPSDL
     VEDIDFQGLS LEDFVAQADN RKRITSTDAG AQTVQQFEKE RDKFQDLHSA ITGCDEVSSS
     VETYLNDFQN ELGAVSAEIE TLQSRSIQLT AMLENRRNVE QLLGPAVEEI SISPKTVRLI
     AEGPIDENWV KALNEMETRA ASIEAKVSGS NSTKSIEDVR PLLKDIKNKA VERIRDYLVS
     QIRALRSPNI NAQILQQQRL VKFKDLYSYI SRAHPELTGQ ITQAYINTMR WYYLSHFTRY
     RQALESIKIY PSDRNEILGG DPSAHKTSSA VAGSRAGSAA HDPFSLGRRV DIMRTGAQIA
     ISSYLAEEDN SFHGLEVPFR NFNLAVVDNV SAEYSFMTEM FSTLSFQQIS RKAVEIFEPV
     FSQGQTLTKQ LIEHTTDALG VLICVRLNQH AAFELQRRKV PVADSYINGV NMQLWPRFQV
     IMDTQCESLK RVAANTGRSA VSALSLAGGD DLNKSSAPHF LTQRFGQLLH GILVLSSDAG
     DDEPVANSLK RLTAEFDNLL TKLSRIGGDA KRRERFLFNN YSLVLAIISD THGKLATEQK
     QGTSTILLER HDAPGTETSS RNSEVRIDCI IVPFALFVSA WRSRMMDIDR SRGKKKSSGG
     IQLMNQRAQQ VIHAGLYYGT DTLKKQLCIE GKELLYDLCE RQNIPYRRTG KWLVAQDAAQ
     WEACLRLHET AQRIGVTTRM LSREEIARRE PEVRAQAGVL ESPTTGILDS HALITYLHGD
     FEDRGGDCAF RTRVTGVRYN GQGRGYEITA VTADGSETAI TAETVVNSAG HGACAINNML
     LPADRHRTPL YAKGTYFSYA ASFPRTSVLV YPVVAKAQAG LGVHLTLDMG GQVRFGPDAE
     WVEDSEDLAP NPARLEQALP LIRDASESGS AWAKGSMFQD FVIQEEEGPG LTSSLAIGKM
     VKRILH
//