ID E4ZME9_LEPMJ Unreviewed; 978 AA.
AC E4ZME9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=LEMA_P052040.1 {ECO:0000313|EMBL:CBX92498.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929094; CBX92498.1; -; Genomic_DNA.
DR RefSeq; XP_003835863.1; XM_003835815.1.
DR AlphaFoldDB; E4ZME9; -.
DR STRING; 985895.E4ZME9; -.
DR EnsemblFungi; CBX92498; CBX92498; LEMA_P052040.1.
DR GeneID; 13285295; -.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001287_0_0_1; -.
DR InParanoid; E4ZME9; -.
DR OMA; ENECPAC; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000002668; Genome.
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; SM00184; RING; 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:UP000002668};
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 884..926
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 978 AA; 109167 MW; 87DBAA138A518338 CRC64;
MAWLTRDKWQ FKFFDVSQVK LPDDDSSSNT FLSEIGNITC IVSGSESIFS GSADGTVRIV
SQAFKVVRAF KAYDAGAITH MKQIEGTSLL VTIAEDLSDE PVLKVWALDK LEKKTGMPRC
QSTLTVHNGR KQFPISAFAA LDDLSQLAVG FANGAVTVVR GDLIHDRGAR QRTVFESEEP
ITGIELRQGS ITTLYIATTA RILTLVISGR GQGQPAKSLD EYGCSVGCMA VDKTTRDVVV
ARNDAIYYYG QHGRGPPYTY EGEKKLISTY KDYVVIVAPP KTNAMPRSNP LRTFGVGATD
DVFNTSTFTL LNTELRFVAH QEQLTSQVKA IVSEWGDLFV FTIDGKIFKY HEKPFAQKLD
ILYQRNLYVL AINLAQKAGL DSSQQNVILR KFGDYLYSKQ DYDTAMQQYL KAIDNTEPSQ
FLDTQRIHNL IEYLEELHDH HKATSDHTTL LLNCYAKLKD VEKLEEFIKS PDDLKFDLDT
AISMCRQGGY YDQAAFLARK HGEHELVVDV LIEDSHRFAE ALAYIWRLEP EVAYYNLMKY
ATVLLQHVPK DTTQLFIDYY TASFRPKKDA IIIPDAPSSG GGGGIGMGLG VASSAVQNLA
ALLPLPYMNS NALASPPNGE QKGIMSQAQI IETNTDEPAP EYKVPKPRTA FSAFVDHPQE
FIVFLEACIK SENMREDDRV DLYTTLFGMY LHTASSKKDG ERQEWENKAK KLVEGKDKPI
DTSNVLLLSH LSDFRDGAIL VREQQGLYFD IFRSFTAAKD TQGAIRALRK YGPEEPALYP
AALAYFTSSS EILSEAGDEL DSVLKRIDED GLMAPLQVIQ TLSTNGFATM GMIKSYLSAT
IEREREEIAQ NRRTIETFRA DTETKKMELA NLNSKPVIFQ TSRCQICSKP LELPVVHFLC
KHSFHQSCLS TDEDVHDAEV ECPLCSANNA TVKAIRRAQL ESANRHDLFQ DALKRGKDGF
AVISEWFGRG VMGVGGTD
//
