ID Q0UMU2_PHANO Unreviewed; 991 AA.
AC Q0UMU2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=SNOG_06922 {ECO:0000313|EMBL:EAT85573.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT85573.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH445334; EAT85573.2; -; Genomic_DNA.
DR RefSeq; XP_001797283.1; XM_001797231.1.
DR AlphaFoldDB; Q0UMU2; -.
DR STRING; 321614.Q0UMU2; -.
DR EnsemblFungi; SNOT_06922; SNOT_06922; SNOG_06922.
DR GeneID; 5974173; -.
DR KEGG; pno:SNOG_06922; -.
DR VEuPathDB; FungiDB:JI435_069220; -.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001287_0_0_1; -.
DR InParanoid; Q0UMU2; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
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 Pfam; PF13923; zf-C3HC4_2; 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:UP000001055};
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 880..922
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 991 AA; 111042 MW; 6F598C60A4FE0F70 CRC64;
MAKLTREQWQ FKFFDVAQVK LPDEESSFLS EVCHCLSGSE SIFFGSADGI VRIVSQAFKV
VRAFKAHDTG AINYMKQIEG TSLLVTIAED LSDEPVLKVW ALDKLEKKTG IPRCQSTLTI
HNGRKQFPIS AFAALDDLSQ LAVGFANGAV TVVRGDLIHD RGARQRTVFE SEEPITGIEF
REGSITTLYI ATTNRIMTLV ISGRGQGQPA KSLDEYGCGV DCMAVDKTTR EVVVGRSDAI
YYYGQHGRGP PYTYEGEKKK VSVYKDYVVI VAPPKSNAMP RSNPLRAFGI GATDDVFNTS
SFTLLNTELR FVAHQEQLTS QVKAVISEWG DLFVFTMDGK IFRYHEKPFA QKLDILYQRN
LYVLAINLAQ KAGLDAAQQN VILRKFGDHL YSKQDYDTAM QQYLKAIDNT EPSQVIRKFL
DTQRIHNLIE YLEELHDHHK ATSDHTTLLL NCYAKLKDVE KLEEFIKSPD DLKFDLDTAI
SMCRQGGYYD QAAYLARKHG EHELVVDVLI EDSKRYAEAL AYIWRLEPEV AYFNLMKYAT
VLLQHTAKDT TQLFIDYYTG NFCPKKDAIV IPNAPATPGG IGMGLGVASS AVQNLAALLP
LPYMNTSSVA STPLSEQKST MSQAQIVETT TDEPAPEYTV PKPRTAFSAF VDHSQEFIVF
LEACIASENL REDDKVDLYT TLFEMYLHTA SSKKDGERQE WENKAKKLVE GRDIPIDTSN
VLLLSHLSNF RDGAILVREQ QGLHFDIFRS YTAANDTQGA IRALRKYGPE EPALYPAALA
YFTSSPDVLA EAGDELDSVL KKIDEDGLMA PLQVIQTLST NGVATMGMIK SYLSTTIERE
RSEIASNRRT IETFRSDTET KKNELQKLNT KPEVFQASRC QVCMKTLELP VVHFLCKHSY
HRSCLSTDED VEDAEVECPV CSGQNATVKA IRRAQIESAE RHDLFQDALK RGRDGFAVIS
EWFGRRCYGC SKCGLEQSMS TKLSCCLPLL P
//
