ID A0A0D2BNI5_9EURO Unreviewed; 976 AA.
AC A0A0D2BNI5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=PV06_08861 {ECO:0000313|EMBL:KIW39047.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW39047.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW39047.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW39047.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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; KN847340; KIW39047.1; -; Genomic_DNA.
DR RefSeq; XP_016259263.1; XM_016410241.1.
DR AlphaFoldDB; A0A0D2BNI5; -.
DR GeneID; 27360935; -.
DR VEuPathDB; FungiDB:PV06_08861; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000053342; 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; 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; SM00299; CLH; 1.
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|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR007860};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR007860};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
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 DOMAIN 877..923
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 976 AA; 109354 MW; B26DA41891CCD5E1 CRC64;
MKRDRISSRC VLPVSLETCP NSRCQNDIVS IATGSDSLFL GSSNGSVRVL SRALKVVRTF
QASDTSDASI THIKQIPETP FLVTISENLS SEPFLKVWAL DKTEKKTGGP RCLCTIAVQN
GRRQFPVSAL VVLDDMSQVA VGFANGSVTV IRGDFVHDRG TKQRTVFESE DPITGLEIRQ
NATKVLYIAN TAKICSLIIS GKGQGQTART VDNRGCNVGC MTQDRETGDI VIAREDAIHY
YGPGGRGPSY AFEGPKKIVK MYKEYVGLVC PPRVAQVSKS KTFRRLAGDE IHELFSSSSF
TLLDTDLKFI AHTESLPAQV KDVFVEWDEL FLLTSEGKLF RYQEKTLQQK LEILYQRNLY
IYAINLAQKA GADKVQQNII FRKYGDYLYQ KGDYDTAMQQ YLRAIDNTEP SQVIRRFLDT
QRIHNLIDYL EELHEHDKAS PDHTTLLLNC YAKLKDTEKL DAFIRASGTA RFDIETAIAM
CRQGGYYDQA AYLATKHGEN ELVIDILIED SKKYAEALQY IWRLNPDTAY PVLMKYARSL
IEHCPEETTK LFIEYYTGRY APKQDIPAVS EVQAQSGGGA FQTLSALWTL PFMSRASNVN
GIPTGDEQKP LGEETQPTSV VVTPSYLVPR PRSAFSAFIA RPVEFIQFLE ALVRQESLAK
EDRSDLSTTL FEMYLEAANS SRDPGERDNW QVKATSLIAD NKTESLDEST IDTSNVLLLS
SLSKFPTGTT LVRERENLYA DIFRSFTSAK DTSGAISALR KYGEKDPSLY PLALGYFSSS
EGILKEPGVK DELQNVLKKI DQEKLMAPLQ VVKVLSQGGA VSMGMVKAYL SDNIQRERKE
IQTNRRLIDS YRTETASKRS ELTDLETKPV VFQARRCSSC ARNLTLPTVH FMCKHSFHQE
CLNKPGLGLD EDEDDQIECP ICKPGNDTIR AIRRQQVEST EQHDLFKAAL ARSNSRFETV
SEFFGRGVMG TIPAAE
//
