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Database: UniProt
Entry: C6HE57_AJECH
LinkDB: C6HE57_AJECH
Original site: C6HE57_AJECH 
ID   C6HE57_AJECH            Unreviewed;      1070 AA.
AC   C6HE57;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Vps52/Sac2 family protein {ECO:0000313|EMBL:EER41841.1};
GN   ORFNames=HCDG_04488 {ECO:0000313|EMBL:EER41841.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER41841.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the VPS52 family.
CC       {ECO:0000256|ARBA:ARBA00008180}.
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DR   EMBL; GG692423; EER41841.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HE57; -.
DR   STRING; 544712.C6HE57; -.
DR   VEuPathDB; FungiDB:HCDG_04488; -.
DR   HOGENOM; CLU_007605_0_0_1; -.
DR   OMA; HSSCAIS; -.
DR   Proteomes; UP000002624; 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:UP000002624};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          119..290
FT                   /note="Vps52 coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF04129"
FT   DOMAIN          307..656
FT                   /note="Vps52 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20655"
FT   DOMAIN          712..1067
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   1070 AA;  119040 MW;  43E59BF042A2E788 CRC64;
     MRRLLSPIPL GWASGFFLPF DRTARSWTSV LRALRLYAVD HSSAVCIMGN VPGQGLIQTR
     QPSCMRQELS RLLTSRECLV EDIDFGELSL EEFAQQKEER EEGKLKRRVD VQTIEQYERE
     RDRFQDLHSA INGCDDVLKS VESYLSRFRT DLGVVSAEIE SLQSRSAQLN SQLENRRNLE
     RLLGPAVEDV SISPKVVHLI SEGPINQEWV KALSEVETRS ANIEANTSTT SNVRAVEDIK
     PLLSDLKAKA IERIRDYLVA QIKAIRSPNI NAQIIQQQSL IKYKDLYGFL SRNHSALTEE
     ITQAYINTMR WYYLSNFTRY HQALEKLKVH HAERNDLLGG DPSAQKASNI FPSGRNSTYD
     PFALGRRMDI LKSSHTALPS YLAEENASHA TTTNPNAKVN PKTQPSIHGL EVPFRNFNLA
     LIDNISAEYS FVAEMFVTKT QSLRTSSRRV IEMFEPVFAL GHSLTKHLID SSTDCLSILL
     CVRLNQHFAF ELQRRKVPVA DNYINGINML LWPRFQMVMD LHTESIQRIA GNTTGNIGAI
     LSLSETTNPN TSSPAFSSSS APHFLTQRFG QFLQGILALS SEAGDDEPVS NSLARLRVEF
     DALLVKLAKA ANGSDARGRE RFLWSNYSLI GTIISDTRGR LAEEVKEHYT QLIKNSAGRR
     NCRCRKLNPI GLGALPNFSA LLRASSINYQ CTSRRVTEIP LHLLASLQKK EIIGGGIVGL
     SIARHLSLTR PNTTTILLER HPALGTETTS RNSEVIHAGL YYPPSSLKTR LCIRGKHLLY
     DLCASPAHNI PHRRTRKWIL AQDAEQLDRL QRMHEHAARL GVPTRFLARG EMARREPDGA
     GGDVALWTAV SQIEKVGAGG GYRIYTRSAG TGREARDSAR GGEGEGDEDE AVITAEALIN
     AAGHNACAIS NMLLPSDRHV RPAYAKGTYF SYSASSPKPR TLLYPAPKPG LGGLGTHLTL
     DMTGQVRFGP DVEWVDGPED LVPRVGRLEE AVREIQEYLP GVRPEAIGLD YCGVRPKLAV
     KEGEDRGAFR DFVIREEECF EGFVNLLGIE SPGLTSALAI GEMVEELLYG
//
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