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
//