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Database: UniProt
Entry: F0UNT2_AJEC8
LinkDB: F0UNT2_AJEC8
Original site: F0UNT2_AJEC8 
ID   F0UNT2_AJEC8            Unreviewed;       948 AA.
AC   F0UNT2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE            EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN   ORFNames=HCEG_06059 {ECO:0000313|EMBL:EGC46844.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|PIRNR:PIRNR007860};
CC   -!- SUBUNIT: Component of the homotypic vacuole fusion and vacuole protein
CC       sorting (HOPS) complex. Component of the class C core vacuole/endosome
CC       tethering (CORVET) complex. {ECO:0000256|PIRNR:PIRNR007860}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|PIRNR:PIRNR007860};
CC       Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007860};
CC       Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007860}.
CC   -!- SIMILARITY: Belongs to the VPS11 family.
CC       {ECO:0000256|ARBA:ARBA00007070, ECO:0000256|PIRNR:PIRNR007860}.
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DR   EMBL; DS990640; EGC46844.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UNT2; -.
DR   STRING; 544711.F0UNT2; -.
DR   VEuPathDB; FungiDB:I7I53_00120; -.
DR   HOGENOM; CLU_001287_0_0_1; -.
DR   OMA; ENECPAC; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR016528; VPS11.
DR   InterPro; IPR024763; VPS11_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF12451; VPS11_C; 1.
DR   PIRSF; PIRSF007860; VPS11; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|PIRNR:PIRNR007860};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR007860};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW   Transferase {ECO:0000256|PIRNR:PIRNR007860};
KW   Transport {ECO:0000256|PIRNR:PIRNR007860};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR007860};
KW   Vacuole {ECO:0000256|PIRNR:PIRNR007860};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   REPEAT          407..555
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   DOMAIN          865..902
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          569..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  106945 MW;  E95AF4EDF65FF01F CRC64;
     MALTSWKTFN FFDVAPIQFP NDGSSIFNGD ISSICSGSEN LFLGTSDGIV HILSQTFKVL
     RTFKAHDTGS ITHMRQVDST SLIVTISEDL LNDPVLKVWA LDKEEKKTGS PKCLSTVQVH
     NGRRQFPVSA FVVLPDLSQL AVGFANGSVT VIRGDLIHDR GAKQRTVFES EEPVTGLEIQ
     HGPVTTLYIA TTGRILTLVI AGKGQGQPAR ALEDLGCGVG CMTIDHETGD IILAREDAIY
     TYSVSGGRGP SIAFESPKTS INAFRDYIAL VCPPRPALPK SSDALRRLGG SGGGGQVDEI
     LTTSTFTILE PDLKFVAHTE SFPSRVRYVF MEWGDLFIVS VDGMVYRYRE KTLQQKLEIL
     YQRNLYILAI NLAQKAGIDT LQQNIIFRKY GDYLYQKGDY DTAMQQYLRA INNTEPSQVI
     RKFLDTQRIH NLIEYLEELH DHEKATADHT TLLLNCYAKL KDTSKLDSFI KAPGELKFDL
     ETAIAMCRQG GYYEQAAYLA RRHNENDMVI DILIEDSRKY EEALKYIWSL EPDIAYPNLM
     KYARVLLGHC PQETTKLFIE YYTGRFRPRR TTEEEPAERP QTQTGSAIQS LTSFIPLPGS
     QGPKAPAAQP QLAPELESPI QYDIPKARSA FSAFVDQPQK FIEFLEELIK QHNLKEEDRV
     DLYTTLFEMY LDTAMHTRGD GEREEWEGKA KKLIEGKNIP VSTSNVLLLS DLSNFREGTT
     LVREQQGLCS DIFRSYTSAK DTAGVIKALR KYGPHEPQLY IDALAYFSSS PKILEEAGDE
     LHEVLRKIDK DGLMAPLQVI QALSNNAVVT MGMIKKYLSD NIERERKDIA NNRRLISSYT
     ADTEAKQKEI DELATRPFVF QARSCSSCHD RLDLPTVHFL CKHSFHQRCL NRVDEDAECP
     VCAPQNATIR AIRERQIKSA GQHDMFKSEL QRSRDRFGIV KREFNYCN
//
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