ID K5VFV0_PHACS Unreviewed; 1041 AA.
AC K5VFV0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=PHACADRAFT_205018 {ECO:0000313|EMBL:EKM61891.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM61891.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM61891.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM61891.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(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}.
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DR EMBL; JH930468; EKM61891.1; -; Genomic_DNA.
DR RefSeq; XP_007391283.1; XM_007391221.1.
DR AlphaFoldDB; K5VFV0; -.
DR STRING; 650164.K5VFV0; -.
DR GeneID; 18912327; -.
DR KEGG; pco:PHACADRAFT_205018; -.
DR HOGENOM; CLU_001287_0_0_1; -.
DR InParanoid; K5VFV0; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000008370; 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 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 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 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:UP000008370};
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 951..986
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 632..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 115407 MW; 454381378E3424EF CRC64;
MSTHSATPAA SAWRQFNFFD ITPVKDVHDL ASSPEIFKKT PEISCITSTQ HGTIVADIHG
SVYRLNEDFE TVNAWVAHTG GRVTHMLERS GLLVTIGEED TARHPLLKIW DLQTTEKKSG
APVLLRSAKV QSGNRPHPVS TIALTASLSH LAIGLADGTV LLYRHLDQSI FNGSTSLTAL
PKARVVLEGS SDPVTGLGFR ESNRDNLDIH LFIVTTNRVL MYQVSGKGHG GTPTAVDEVG
CALGCATMDH GAREIVVARD EAIYLCGIEG RGACYAYEGH KSAVYAHRNY LVIVSPPFTP
TASAPSATVR NFVRDNDIGA EISRVVVFDL ENKFVAYSGT YTDGIRDIFA ASGQIYLLSN
DGKLLRLEEK PTPEKLELLY RKSQYLLALS LAKTQGLDEQ NVADIRKQYG DHLYAKGEYD
SAMQQFVQTI SYVQPSYVVR KFLDAQRIHN LVMYLQELHN RGLANADHTT LLLNTYTKLK
DVTRLDSFIK SESRRTSADS DADELPFDLD TAIRVCRQAG YFEHASYLAE KYERHEDYLQ
IMVEDAGNYR EALTYLRRLG TEAAEGNLAR YGRALLDNLP EETTALLIDL CTSLTPLAIN
DEDSPPASAR QSSVGGPSYL SYLALNRGSA ASASSETAQP STASTTTTVK APAPRRQGSV
NVSDASPSSQ PSRTATPTVA KSARHQVIKR PSPRVYFAHF IDHPVNFLNF LEQVALLRWG
RSVNSKEGVP TVVESDLNAD PEVERRDQAA VWNTLLELYL VDTPDKALRV LQRDDLPYDH
THALILCSTR GFTPGLVLLW EKLGMFEDVL RFHMDRERED PTSGGSKDVI HCLDKYGAQQ
PGLYPLVLRF LTSSPELLGR HTDDLGRILE HIESEKIMPP LAVVQVLSRN NVASVGLVKQ
WLLSRIKSAR AEIDMDQKLI DSYRTETKAK LKQVEDLSDP EHPRVFHVTQ CSACGGQLDL
PSLHFMCNHS YHQRCLGEHE TECPNCARQR SIIREIRRNN VRLADQHDVF LSEVKEGGYA
AVAAGFGRGV LNMSRLEEIA S
//
