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Database: UniProt
Entry: A0A0G2FLF6_9PEZI
LinkDB: A0A0G2FLF6_9PEZI
Original site: A0A0G2FLF6_9PEZI 
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
//
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