ID K9G7N8_PEND2 Unreviewed; 1001 AA.
AC K9G7N8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=PDIG_12300 {ECO:0000313|EMBL:EKV17965.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV17965.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV17965.1}.
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DR EMBL; AKCT01000044; EKV17965.1; -; Genomic_DNA.
DR AlphaFoldDB; K9G7N8; -.
DR STRING; 1170229.K9G7N8; -.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001287_0_0_1; -.
DR InParanoid; K9G7N8; -.
DR OMA; ENECPAC; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000009882; 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; IPR019734; TPR_repeat.
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; PF17122; zf-C3H2C3; 1.
DR PIRSF; PIRSF007860; VPS11; 1.
DR SMART; SM00299; CLH; 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; PS50005; TPR; 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:UP000009882};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
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 424..457
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 910..947
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1001 AA; 112476 MW; 8CE92C4789F45737 CRC64;
MSFHLGSKAE ENAVLAAVID VENQVVQAPA GRAPNRIVTF HTFQFMASRD GADITFNFID
VSPVKLPEDS SSIFNSDLSS ICTGSANVFV GTTDGFVHIV SSAFRVVRSF KAHDTGSITH
MRQINDTAML VTVAEDLYNE PVLKVWALDT EKKNGDPRCL STVSVQNARR QFPISAFAAV
DDLSQVAVGF ANGSVTIIRG DLIHDRGARQ RIVFESEEPI TGLETQTGVI TTLYISTTSR
ILTLVIAGRG QGQPARVLED AGCGLGCMTL DREGGEILIA RDEAICTYGP RGRGASYAFE
GPKTSIDAFR DYVALVCPPK AGSSKSDPLR KYTANPAEEI FGTTTFTLLD TDLKFIAHSE
ALMSPMKRVF MEWGDLYLLT TDGKIFRYRE KTLQQKLEIL YERNLYILAI NLGQKIGIDP
LQQNVIYRKY GDFLYQRGDY DTAMQQYLRA IDNTEPSQVI RKYLDTQRIH NLIEYLEELH
DHGRATVDHT TLLLNCYAKL KDTSKLDSFI KAPGELKFDL ETAIAMCRQG GYYEQAAYLA
TKHGENEMVV DILIEDSKKY AEAVEYIWRL DPEVAYQNLM KYARVLLTHC PERTSELFKV
YYSGQFRPRT EVEQPSEPEE QATSTVQSLA ALLPLRYMNV GTSTQLSAGI PEPAIDENKV
EDSLPYYDIP KPRTAFSAFV DHPKEFIDFL ETLVQQPDLK QDAKVDLFTT LFEMYLDTAK
RKKDAGERQE WETKAKKLIE GKDIPISTSN VLLLSDLSNF REGSTLVREQ EGLRLDIFRS
FTSAKDTQGA IKALHRYGPD EPQLYVDALT YFASSPKVLE EAGDELDAVL QHIDQDGILS
PLQVIQALSN NAVVTMGRVK KYLSDNIDRE RKEITTNRRL VTSYKSETEI KKQELDNLST
QPVVFQSRRC QSCGGTLDLP TVHFLCRHSF HERCLNNLDN DAQCPVCAPA NATLRAIRQR
QVDSADQHDL FKSELSRSRD RFGVVSEFFG RGIMRPQSTM E
//
