ID A0A0G2FLF6_9PEZI Unreviewed; 973 AA.
AC A0A0G2FLF6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=UCDDA912_g05143 {ECO:0000313|EMBL:KKY34871.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY34871.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY34871.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34871.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY34871.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34871.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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}.
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:KKY34871.1}.
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DR EMBL; LCUC01000180; KKY34871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FLF6; -.
DR STRING; 1214573.A0A0G2FLF6; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000034680; 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 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|PIRNR:PIRNR007860};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR007860};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
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 REPEAT 404..549
FT /note="CHCR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT DOMAIN 881..919
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 973 AA; 108389 MW; FCC08F196739C7F1 CRC64;
MALSWKSFDF FDVSQVKLAD DDETRAFFDS NEISSVCSGS DSLFLGSSDG HVRIVGPSWR
IVRSFQAHDN VRISHMRQVE GTSLLVTVGE DLSGEPVLKV WALDKPVKKT GMPTCLSSVT
ISNGRKQFPV SAFAATEDLS QIAVGFANGA VTVIRGDLVN DRGTKQRIVY ESEEPITGVE
LRVDERLTTL FVSTVSRILK LTISGKGQGQ PPKTVEDQGC GVGCMAVDKR DGSIVVARDD
AIYYYTADGR GPPKAYDSPK ELVTVYQKYV AIVSPPKSAQ DPNALRRRFG GNAADAIFNA
STFSLLEPDL KVIAHTETLI SKVLAVFELW GDLYTLTQDG KVHRYHEKTL QQRLEMLYQR
NLYPFAISLA QTAGLDTQQQ NVIFRRYGDH LYQKGEYDQA MAQYIKAIDN TEPSQVIRKF
LDTQRIHNLI EYLEQLHEHG KATSDHTTLL LNCYAKLKDI EKLEAFIKQP GELKFDLDTA
ITMCRQGGYF EQAAYLAKKH GENDLVVDIL IEDLKDYKEA LAFIWHLDPQ TAYPCLMKYA
RVLIEHCPKG STQLFIDYYT GNYRPRARHA DTIETPASGG GFAAGAVSAV QNLSNLLPLP
YMNSSAVASP PTQGNIEPTV SDAAVLLDPD DVPPPKYTAP QPRTAFSSFI DHPDEFIVFL
EACLADESIS DENKADLYTT LFEMYLHKST EVKSEHDREQ WEQKAKKLIE GRGAPIENSN
VLLLSHLSEF QDGTTLVKEQ AGLLSDIFRS YTSAKDTRGA MKALRKYGPQ EPSLYPAALA
YLTSDSRVLD EAGLDELAKV LSTIDKDGLM APLQVVQMLS KNAVATMGMI KPYLHETIER
ERKDIASNRR RVAGFRTETE QRRAEIADLG AKPAVFQATR CPVCTQVLDL PAVHFLCKHS
FHQRCLRGGD GVEGECPLCA QSNATIRAIK RGQEENADRH ELFKDELGRS EDRFATVAEW
YGRGVMNVQQ NLE
//