ID U9T678_RHIID Unreviewed; 1010 AA.
AC U9T678;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=GLOIN_2v1764281 {ECO:0000313|EMBL:POG80727.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:POG80727.1, ECO:0000313|Proteomes:UP000018888};
RN [1] {ECO:0000313|EMBL:POG80727.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA Roux C., Martin F.;
RT "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT oldest plant symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN [2] {ECO:0000313|EMBL:POG80727.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=29355972;
RA Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT symbiont Rhizophagus irregularis.";
RL New Phytol. 0:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POG80727.1}.
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DR EMBL; AUPC02000016; POG80727.1; -; Genomic_DNA.
DR AlphaFoldDB; U9T678; -.
DR VEuPathDB; FungiDB:GLOIN_2v1764281; -.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001287_0_0_1; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000018888; 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 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; 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; 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|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:UP000018888};
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}.
SQ SEQUENCE 1010 AA; 114551 MW; 87E80833349C441B CRC64;
MSVKQWRHFT FFDVQQIKDH DSTKPPAIFQ KTDITVRYVH IVDRSFNVQS FIAYEGGRVT
HMKQIKQKNI LLTVGEEDFP IFPIIKIWDL DKQDKSKGIP ICLRTIKVNH GGKPFPVSTI
AVLDNLSQIA VGLANGVVVL IRGDLKERHT KQKVIHESDE PVTGLGFKEN NKNTILFIVT
INKVLTCITP IKSQPIIIDE QGCALGCAVI SDITHEMVVA KDEGIYFYGT EGRGACFAYE
GTKSEVIWFK SNLIIVSPPA QSTRYTSTTH TGSSNQKNTS PFELTKVTIF DTANKFIAYV
GTFSHGIRTI CCEWGGIYIL GMDGKLYRLE EKDTPTKLEI LFKKNLYLLA INLAHSQKYD
DASISEIFKK YGDHLYSKAD YDSAMAQYIR TIGQLEPSYI IRKFLDAQRI HNLVNYLQEL
HSHDLATPDH TTLLLNCYTK LKDVARLDQF IKTDNKLNFD LETAIKVCRQ AGYYEHAVYL
AKLGEEHDLY LKIQIEDTKD YQNALEYIRN LGSLEANRNL QKYGKILLNH LPEPTTKLLI
DLCTGDLYLT AQNPHTPEPV GPTEVSHPGG IPYPSFLQFA HASPAPSLNA ETQANITAVN
TPKEPKTVAY KPPPVRTFMS LFVDQPNYLI QFLEKVSQKR WGGFGSIKPS QPAHNLSLAK
GQYVPIDNIA DEAAESSKSF FESDAEIEEK KAVWNTLLEL YLSEAYLPPV ISTKDAKGRK
NGAPGIFGVT TETERVKEKL IRKDKALQLL MDEDISYDAN QALVLCYLAQ FDEGIIYLYE
KMKMYEDILR FYMAKDNTEK VIQALKKYGP QDQSLYPLTL TYFSSSPATL ATSTTELLKI
LDHIESHNLL PPLQVVQALS RNSVATLGMV KGYLGKRIEL EKKEAQADMK LIQSYREETE
KKRKEIDDLK TTARIFQVTK CTGCRSNLDL PAVHFLCRHS FHQRCLPDSD RECPQCAVQH
RMISEIRRAQ EENAEKHELF FEQLKEAEDG FSVIADYFSK NTMAFAKLID
//
