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Database: UniProt
Entry: A0A1Y2V3R4_9PEZI
LinkDB: A0A1Y2V3R4_9PEZI
Original site: A0A1Y2V3R4_9PEZI 
ID   A0A1Y2V3R4_9PEZI        Unreviewed;      2158 AA.
AC   A0A1Y2V3R4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   ORFNames=M434DRAFT_396731 {ECO:0000313|EMBL:OTA92053.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA92053.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA92053.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA92053.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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}.
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DR   EMBL; KZ112490; OTA92053.1; -; Genomic_DNA.
DR   STRING; 1001938.A0A1Y2V3R4; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000194361; 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; 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; 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; 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:UP000194361};
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          83..155
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         83..155
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          401..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..420
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2158 AA;  244791 MW;  EF8F277A3B5C09D8 CRC64;
     MSTQEQQLCQ YLIELPKRYA FRYEEAACRD LLYNLFWSMA GGRPENLRLF FPEGRLTPKS
     TLKLREAQGA VEGAEYTEAA RGKACGHIFR AGEASYSCKT CSTDETCCLC SKCFNATDHT
     GHMVRISISP GNSGCCDCGD PEAWKIPMFC TIHSEREEDK SKGKGKEAAA LPEDVVSNIR
     MTISRVLDFI CDVISCAPEQ LRQPKTKESI EQDEKMSRLA STYCGGDVEP PEEYALLLWN
     DEKHTVKEVQ DQVARACSTT LDEGYNRAVE TDSIGRSILK YDKSIEKLLR CATVLEHIKI
     TVTIRSSRDT FREQMCGTMI DWLNDIAGCV VGNDQNILRT VVCEELLKPW RKGSPGTHAM
     PGKDGLEDEE KLEYDPLEAH SAALFIQRAR FLAETGNVAR LAELEDSDED DNDDEDEDMD
     GGNRTPSSGE EDNDEDEDED EDVMMVDMRP EASADVSVSD WIAPGVASLE EEEATMAGYP
     PPPPPPPVPR RTTRDRDLTP SDSDTAEPLI APTVYAKANL EIPKTPGLSK ADKAGPPKPG
     RYWVETPAAY MERDSVHPFE DVFQRVRLDW LILFDLRMWK KVRNDLRSLY ISTVVTIPEF
     KRVLGLRFAA LYTTLAQLYL IGDREPDHSI INISLQMLTT PSITAEVVER GNFLTTLMAI
     LYTFLTTRQV GHPWEVSSSA VLGFDTGSVT NRRMYHFYVD LKFLLGSPHV QERMRTEERY
     LMQFLDLVKL HQGICPNVRA VGEHVEYETD SWIGASLMTR EINRLCRLLS GSFRNLPEQD
     SIYLSRAIRT TAKSVIINSI GAERARFTQA EIKDEVRFKS LSDFEFAGEA TRFEVVKFIV
     EEQSISFHHA LHYTLSWLIE CGKNMSPQEL RSILSFTSQE LKMKPRSMGR KTMPRRDYSP
     EDYLMAAFDY PLRVCTWLAQ IKAGMWVRNG ISLRHQAGTY KNILHRDVTH ARDIFLLQTA
     MVVCNPSRVL ASIVDRFGME HWIKGLFEQT STGQDEIQHL DVVEDMVHFL IVLLSDRTSL
     IPVKDEQQTH LMAMRRDITH VLCFRPLSFN EIASKLPEKF HEQEDFQRVL DEVSTFKPPE
     GVSDVGTFEL KPEFIEDIDP YIAHYNKNQR EESEAAYRKW MAKKTGKPAE EIVYEPKLRP
     IESGVFVGLA QFTSTGMFAQ IIYYCLLYPL VAAKLTPKVP FTRIETFLQV VLHLILIAIA
     EDKADETELA AGASSFVYIA LTTHARSNFM QDAPNAKTIV SLLDMMSTKE EFKACHPKIA
     LILKRMKQKY PQHFDTAYSR LGIPVDRIDT ASPASTHNAE EERERKKKAA LDRQAKVMAQ
     FQQQQKSFLE MQGDIDWGEE EWDDMDEAKP VEEQKNFWKY PRGTCILCQE DTDDGRLYGT
     FALFTESKIL RQTDLQDPDF VREAANTPIN LDRSAEAIRP FGLAHENREI VTKVNAEGQT
     FLAERQGLGK GFPAKLCRTG PVSVGCGHIM HFSCFDMYME ATVRRHGHQI ARHHPESLER
     LEFVCPLCKA LGNAFLPITW DGKEEAYPGI LQTDSDLSSF ISTYMTGRHF TAVVSRDQSQ
     NAFANYLRTR MPECLLEKAS ASQSPYSIWD TGNFRPVSSV ASSSDTFSLA ATPGSSVRSH
     SPPESQQGDK ELMLTYRRLR DTLRKNKLVA ATLDNDSRDD DLYASDTLAQ SVGFSISAAE
     IQQRGVEAQY GMTLIERMPE QLLVQLRILS ETVSSYIAVG GLRHGGDNQI EREFCKASER
     QYCQLFISQY FDTSIGDQRR PFDEYAPLLS QDVFIFLCET MFGLSVAHNM DPMHLVRLCY
     LAEIVKVVHN VSRNLALSRW LEYMSNRNVE DPAMNNFANF FHYITVARMN ISQKLSHEAL
     EPSSDLPNLG FEQPGFDTLE SLHSFVRKYA LVFLRKVTIL LHVHLGVDFN SHISPIPEAD
     ELTRLTTALK LPSFDEMCTA LTPLSTQFGW PPRIEAIVKG WLRHQIRGHT ARHFAIEKGI
     EQIPPPSAQI SHPGIFELVG LPKNYDTLIE ECAKRRCPKT GKDLADPIVC LMCGDIFCGQ
     TMCCLMEYQE PGPDKPLLRI GGAQQHMLFK CQGNIGLFIN IRKCAIFYLH RRSGSFSNAP
     YIDKYGEVDI GLRHGRQLFL NQKRYDSMLR NMWLSHGIPS FISRKLEADI NSGGWETI
//
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