ID   A0A059JD21_TRIIM        Unreviewed;      1115 AA.
AC   A0A059JD21;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDB25578.1};
GN   ORFNames=H109_02586 {ECO:0000313|EMBL:KDB25578.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB25578.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB25578.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB25578.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the VPS52 family.
CC       {ECO:0000256|ARBA:ARBA00008180}.
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:KDB25578.1}.
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DR   EMBL; AOKY01000195; KDB25578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059JD21; -.
DR   STRING; 1215338.A0A059JD21; -.
DR   HOGENOM; CLU_007605_0_0_1; -.
DR   OMA; HSSCAIS; -.
DR   Proteomes; UP000024533; 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:UP000024533};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          190..356
FT                   /note="Vps52 coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF04129"
FT   DOMAIN          373..685
FT                   /note="Vps52 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20655"
FT   DOMAIN          743..1110
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1115 AA;  123398 MW;  14B4E7BA229935C3 CRC64;
     MWPDRGAAGQ GGGPVASAST GSRPYSPARR QSQLSAANKP GRPSFSPRSS SLSFSPTPNA
     STTSLPGAAR AANGLSRQPP SAMRNQSYPD PVDVLNGIIG QRRSSSTPGD ETTSLPEKPD
     VLCENIDFGG LSLEEFAHQM ETQPARRSYG QGIQSFEQCE PPMDDISLSI HKSPIVDIWM
     YIDDNDRNIF EELHNSITGC DEILKSVESY LTKFQAELGA ISSKIESLQS RSFRLSSQLE
     NRKNVERILG PAVEKISVSP RTVRSISDRP IDQEWVKALS ELDTLSSTIN ANTSTPENIK
     AIEDVRPLLQ NLQEKAVERI RDFLVTQIKA IRSPNMNSQV IQQQSLLKYK DLYTYLSTHH
     PTLSEEITQA YVNTMRWYYL SNFTRYSQAL DKLKLYSIDR NDLLGGDASS QRTAHGGSGS
     RSPALAAHDP LALGRRMDIL KSSSHMALSS YLAEEDKSTH GLEIVFRNFN LALIDNISAE
     YSFLAEMFAA KTIHYNSQKV TEIFEPTFAS GQALTKQLIE TTTDCIGILL CVRLNQQFAF
     EMQRRKVPVA DPYINGINMQ LWPRFQMIMD MHFESLKRIS TASTRSGLSV LALTSTDAQS
     SAPHFLTQRF GQFLHSILTL CNEAGDDEPI FNSLGRLVNE FDALLTKLSK SSGDTKRRER
     FLFNNYSLIL TIISDTKGKL ATDQKEPSGV TLFYPHLPYA SQTNEPAAPL IGLACETRSW
     SWPLARCRLF SSSSKLHADF THAVVGAGVV GLAVARQLAA REGTSTILVE RHSAVGTETS
     SRNSEVIHAG LYYGVDSLKT KLCIEGKELL YKLCEKQNIP HRNTKKWIVA QDEEQWKECL
     KVFLHAKEIG VPIRFVSAEE AKRREPDVRA EAGILESPTT GIVDAHSLMS YLHGSYEERG
     GDCVLLTEVY KVEPLKNGGG YEVFTRSGER KDEESSFTAE TLINCAGHFA CGINNMILPP
     ERHRTPHFAK GTYFSYAASS PKPSTLLYPA PRPSYGGLGT HLTLDMAGRI KFGPDVEWVD
     SPDDLIPSPK RLTQAIKEIQ AYLPSVNPDA IGLDYCGIRP KLIRGGSVSS GKDFQDFVIQ
     EEKGFPGFIN LLGIESPGLT SSLAIAKMVE NLLYR
//