ID A0A074X2B3_9PEZI Unreviewed; 968 AA.
AC A0A074X2B3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=M436DRAFT_86154 {ECO:0000313|EMBL:KEQ68781.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ68781.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ68781.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ68781.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584726; KEQ68781.1; -; Genomic_DNA.
DR RefSeq; XP_013422978.1; XM_013567524.1.
DR AlphaFoldDB; A0A074X2B3; -.
DR STRING; 1043004.A0A074X2B3; -.
DR GeneID; 25417663; -.
DR HOGENOM; CLU_001287_0_0_1; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000027730; 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 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 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 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:UP000027730};
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 872..914
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 968 AA; 108250 MW; 33FA8617B18F4003 CRC64;
MALTSWKAFR FFDVSPIKLP DADKSILEQG NVSCIIASPD HVYVGSPDGH LRILDQTFKT
TQSWKAHESG ALTNIRQIPH SSLLVTLAED LPHEPVLKVW ALDRPDKKTG IPRCLTTISV
TNGRKPFPVS AFAVLRDLSQ VAVGFANGAV TVIRGDFIHD RGTKQRTVLE TDEPITGLEF
REANVTTLFI STTSRISTLI ISGKGQGQPA RTLDEHGCAV GCLTKDLRSN DIIVARDDAV
YAYNPRGRVA SYAYEGSKKL TETYKDYILL VSPPKSMTNA PTRSFGGGQA DDLFSTSNFT
ILNPDLKLIA HTEALPSQVN ALFSAWGQVY IVTLDGKVLR YTEKTFQQKL EILYQREFFV
LAINLAQKEK VDVVQQNLIF RKYGDYLYRK GDYDTAMQQY LRAIDNTEPS QIIRKFLDNQ
RIRNLIEYLE ELHEHHKASS DHTTLLLNCY AKLKDVEKLE DFIKSPGDLK FDLDTAITMC
RQSGYSDQAA FLARKHNEHG LVVDILIEDL KRYAEALAYI WRLEPEQAYD SLTKYGTVLL
EHSSEDTKQL FIDYFTGNFR PKKDAVVEQE ITPEQQQSGG IGKMATSAVQ NLAALIPLPY
MSADVPRTPG GTKTTQQVIE TTVEDEYVEY KVPKPRAAFS SFVDHPDEFI SFLEACIASS
GLKDEDKTDL YTTLFEMYLQ IASKKTSDDK TKWESKARQL VEEQNTRMGT SNILLLSHLS
NFRDGTTLVR EQRGLYFDIF RSYTSANDTP SAIKALRKYG PLEPQLYPAA LAYFTSTSAV
LAEASSELDS VLKKIDDDGL MAPLQVIQTL SQSQVATMGL VKTYLSRTIE RERAEIASNR
KLISSYRNDT AAKANELETL ASKPVSFSAT RCSACGAPLD LPTVHFLCKH SFHERCLYVG
AGDEESDVEC PKCSGDNATV KAIRRAQEES ADRHELFVDA LGRSRDKFAT VSEWFGRGVM
GRGVSVVE
//
