ID A0A1Y2E3J6_9PEZI Unreviewed; 2172 AA.
AC A0A1Y2E3J6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=BCR38DRAFT_340296 {ECO:0000313|EMBL:ORY65876.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY65876.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY65876.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY65876.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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:ORY65876.1}.
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DR EMBL; MCFJ01000005; ORY65876.1; -; Genomic_DNA.
DR STRING; 1141098.A0A1Y2E3J6; -.
DR InParanoid; A0A1Y2E3J6; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000193689; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16482; RING-H2_UBR1-like; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 87..159
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 87..159
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 421..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..457
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2172 AA; 245321 MW; 88818D9FD6BDC022 CRC64;
MDTSMSTQEQ QLCQHLIELP MRHGYRYNDA ANRDLLYNLF WSIAGGKPEY MRLIFPDGKL
SRQGTLKLRE AQGAVEGAEY TEAARGKACG HIFRAGEASY ACRTCSTDDT CCLCSKCFDA
TDHTGHMVRI SISPGNSGCC DCGDPEAWKH PMFCTIHSER EQDQSKGKGK EVAGLPEDLT
RNIRMTIARV IDFICDVVSC APEQLRQPKT KESIQQDEEM SRLNSTYCGG DTESPGEWAV
LLWNDEKHTV VEVQTQVARA CRTSLADGYQ RALETDSIGR SILMYGDDIE SLLSVAKILE
QIKVTVTIRS SRDTFREEMC GTMIAWLNDI AGCSVGSDST ILRLIVCEEL LIPWRKGSAA
VHAIVGKDGI EDEEKLEQLH AQNLETRNFL RQTRLLARAR AQVNAADGQV TIQAALADIL
DNDTSDDEDM ARNQTPSSGE EDDDDDDDDD DDVDGDVMMV DAGTGASADV NMADWRQGSI
GEALEEEEAT IAGYPPPPPP PPVLRRGTRD RDLTPSDSDT AEPLIAPTVY AKVNLDIPKT
PGLAKSGETP PPKPGKYWVE TPTPYMERAK DKPYEDVFSR VRLDWLILFD LRMWKKVRND
LRSLYISTVV TIPEFKRILG LRFAALYTTL AQLYLIADRE PDHSIINISL QMLTTPSITA
EVVERGNFLT TLMAILYTFL TSRQVGHPWE VSSSAVLGFD TGSVTNRRMY HFYVDMRFLF
GSPHVQERMR TEERYLLQFL DLVKLHQGIC PNTRAVGEHV EYETDSWIGA SLMTREINKL
CRLIAESFRK APEQDSQYIS RAIRLTAKNA IINSIGADRT RFTQAEIRDE VRFKTLTDFE
FAGETNKFDV VKFVVEEQPI SFHHALHYTL SWLIECGKSM TAQQLGSVLS FTAQELKMKP
RSMGRKTMPR RDYTPEDYLT ALFDYPLRVC AWLAQIKATM WVRNGISLRH QAVTYKNILH
RDVTHHRDIF LLQTAMVVCN PSRVLASIVD RFGMDKWIKG FFEQTSTGQD EGQHLDVIED
MLHLLIVLLS DRTSLMPTED EHEMQLMTMR RDISHVLCFR PLSFNEVCNK LPDKFHEQEE
FHQVLDEIAT FKPPEGVSDV GTFELKPQFI EEIDPYIAHY NKNQREESEA AYRKWLAKKT
GRSAEEIVYE PKLRVIPSGP FVGLSDFTGT GMFAQIIYYS LLYPLVATKL TPTVPFTRVE
ALLHVVLHLT LIAVTEDKAD ERSLASENSF IYIALTKHAR SNFMQEAPAA KTIVSLLEMM
SAREELKSCH PKVALILKRM RQRMPQHFDT AYARLGVPID RVDTASPADI QNAEEEREKK
KKAALDRQAK VMAQFQQQQK SFLENQGDID WGDEDLEELD EAKPIEERKN FWKYPRGTCI
LCQEDTDDGR LYGTFGLFTE SQILRQTDLQ DADFVREAAN TPVNLDRSAD EIRPFGLAHE
NRKTVEKVNA AGETFLAERQ GIGRGFPSKL CRPGPVAVSC GHIMHFSCFE MYIEATSRRH
VHQIARHHPE TLERREFVCP LCKALGNAFL PITWDGKEES YPGVLSSPAD LDSFVQTHAR
PDTYVPSLSR MFSPPTHQQA FAAYVRSKMP HSLIEGSTQL VMDTWDGSGT RSVSTGTPFS
DSFSAMATPD SSVRSRSPSD AQQSDKGLLS VYRRLRDTLL KNKLYTRIDG EEKDDELCGS
GALARAVGYS VSATEIQQRG IEAEYGMTLI EKIPEQTLIQ LRILSETTSS YIAIGGLRFG
GENNIDMEFR KDSERQHCQL FISEYFGRET NNSRRPADAY PPLLSQDPFI FMCESIFGMA
MSQNMNITSL VRLCYLAEIV KVVYHISRNV PISKWLEHMV SRDTEDAAMN NFATFCHSIT
LAGINYSEEL NELPDSDLPN VGFDQPCMDS LAKFHAFVQK YALVFLRKTA ILLHVHYGVD
FNSHVFTSPE ADELSRLTAA LRVPAFDEMC TALTPFGPTF GWPSRIEAIA HGWVRHQIMW
PGSNTPAVIA DVSRDSRLLP SSAMISHPGI FELVGLPKNY DMLIEECARR RCPKTDKDLA
DPIVCLMCGD IFCGQTMCCL MDYELPGSTS TMKIGGAQQH MLFKCQGNIG LFINIRKCAI
FYLHRVSGSF SNAPYIDKYG EVDVGLRHGR QLFLNQRRYD SMVRSMWLSH GVPSFISRKL
EADINNGGWE TI
//
