ID A0A0C9XU82_9AGAR Unreviewed; 1096 AA.
AC A0A0C9XU82;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=K443DRAFT_678533 {ECO:0000313|EMBL:KIK01272.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK01272.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK01272.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK01272.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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 ---------------------------------------------------------------------------
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; KN838609; KIK01272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9XU82; -.
DR STRING; 1095629.A0A0C9XU82; -.
DR HOGENOM; CLU_001287_0_0_1; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000054477; 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; 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 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; 2.
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:UP000054477};
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 1007..1042
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 188..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 120396 MW; F92DB4BCC05C5DE9 CRC64;
MSQNLATLAA SASTGVASAS AAPAWRQFSF FDVVPVKDIH DLDSPPYIFK AATEISTVAS
SGFGVLVADI HGSIHLLNRD FESTNSWVAH VAGRVTHMVE RQGVLVTLGE EDNVKSPLLK
IWDMQNTDKK TGSPLLLRST KVQLSNRPHP VTTIALSASL THLAIGLGDG TVLLYRHLDQ
SLASSTSLTS LPKPRTVHES PTEPITGLGF REPTEDIVNA HLFVVTTNRV LSYQASGRGS
GGSATVVDEV GSGLGCATMD WKKRDIVVAR DEAIYICGID GRGACYAYEG HKSSVHTHRN
YLVIVSPPFF ATATAASATV RNFVARSANP GETDITKVNV FDLENKLVAY SGTFKQGVKE
VISQWGEIYV LATDGRLLCL EEKSTADKLD MLYRKSLYLL ALNMAKTQNL DVASVADIHK
QYGDHLYGKG DYDGAMQQFV QTIGHLQPSY VIRKFLDAQR IHNLVTYLQE LHSLGLANSD
HTTLLLNTYT KLKDVSRLDT FIKTESRRGD DSDELPFDLE TAIRVCRQAG YFEHAGYLAK
KYQRHEDYLR IQIEDAGNFK DALVYLRKLG SEAAESNLAR YGRAMLNSLP EETTQLLIDL
CTSTGPLIPE PEEITPKSPA AAVASGPSYL SYLALNRNSV VAPTNLETAT VTPPSPSVKT
VKADSTSRRG SVHGGVSISG TITPPTTDIP PSKSNALLPP PKSPSPTPHH RLSPKLYFPH
FVDNVDQFLV FLETVAIRRW NQSVDPTPPS PGMVGVLGGV EPPDPSDKLG VELDRRDQVA
VWNTLLELYL TLPSPGGARK AGGGEKGAKF DEKVMREKAM RVLRSENIPY DPMHALILCS
THSFTDGLVL LYEKMGMYED VLRFWMDKHN SQTSSSSFPG ASAKVVEHLM HYGNQHPHLY
SLVLRFLTST PELLGKHQED VRGILEYIDN EGMMSPLSVV QVLSRNGVAS VGLVKEWLVG
RIKEARGIIQ SDRELITSYR TETAAKLKQV EALSNPDNPH VFHVTRCSAC HAQLDLPSVH
FMCDHSYHQR CIAEHETECP NCAQEHGVIR EIRRNNERLA DQHDVFVLEV KESGIEAVAG
AFGRGLMNMG RVEEVA
//
