ID A0A316URA0_9BASI Unreviewed; 2125 AA.
AC A0A316URA0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=BDZ90DRAFT_232210 {ECO:0000313|EMBL:PWN27822.1};
OS Jaminaea rosea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Jaminaea.
OX NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN27822.1, ECO:0000313|Proteomes:UP000245884};
RN [1] {ECO:0000313|EMBL:PWN27822.1, ECO:0000313|Proteomes:UP000245884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN27822.1,
RC ECO:0000313|Proteomes:UP000245884};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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|ARBA:ARBA00004906, 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; KZ819667; PWN27822.1; -; Genomic_DNA.
DR STRING; 1569628.A0A316URA0; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000245884; 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; IPR003769; ClpS_core.
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; PF02617; ClpS; 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:UP000245884};
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 209..283
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 209..283
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 135..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2125 AA; 234831 MW; 1940291427D3E567 CRC64;
MESQSHLLAS SQASSSRFPY ASTASLDAAS ADWHPIESVL KDLGYQGSRH FAHYGPTAPA
RLNANDALDH RLPLTKASRD ALKAKMYHRL LSADVGLVLD PAEAEPRLAR DPTAYVDTIQ
KYGWSLAKVQ QSISQLREQH KESTRSTHNP FASASSAFKG KAPQHRSHSS SSNSTMTSAA
GTPQSSRPST PAPIDPTSAP EYGEERRGMP CGHVFEKGEA IWRCRDCALD DTCVQCAPCF
NASIHVREGH DVVFSVSSSS GGCCDCGDEE AWKQDVCCGY HSVQRGDTDM AADEEANSTS
DSSRPPDVAR EVHDALHAEH FNPTSHPRIS QLLATWIDFI LIVLNHAPNE QKLFPRSFAR
ASAQEATKKV DDLPDLRQWG RPEAASSAPA GAKKERDSLM SPEVRTPLPP GAFDAFDLYV
DADGPTNSAG AETPGMKWGT LPPSSPAVLQ QGGHEREYAL ILWNDEKHSF REVIDTVKEA
LDVSDEEARA VAERVDVHGR DILAVSTDSR AMVGFARRMA GIDLEVTIRP GFDVYCEEVA
HALISVIKDL AEGVAYLPRS NSDPYGLVNA NASIPRLLLC SELLKTWDAS KRQADSFLSN
HMSTEFFDPR ELTRLDGLLL MDQKLWKEAR AWVRGWYMTI IARKEGRRSV AFHFAAMYPK
IIETFILRER EPEHSVVLMT VQLFSVPSIG SDLVRHYNFL QRLLLILQSI YTGQLIPPTG
TLMLPAKMDP MASANPQCTL LRQIYCRHVF YDARYLLQAE GVQQQIVADE RHLEYFLDFL
SLFHSFLPEA RQTQHHVEYE SEVWVAVFGV CQLLARKAKL FGEAYEKAPP AAIARAFVKT
VERINLRTHA IANRLAGVSV GGELCRVIDF AVEREETSFH HPMHWLLAEL SRRMASLTQR
DIQTIGHSSL QSLACGDIDQ SRIMIALDFP LRVIVKLAQV RAGIWVRNGA STRGQAAHYR
DVAMRSSMYD QDVFLMQAGL AFLKNPEELL VTIIDRYRLL EYFDIRRFNH TPEADPFDHE
QQHFFAEEFL FFLITMLSET SMVHSWPIEK VIRREMVHFL ALNQGTYSAL TRHIPEHISS
HPSFEKILAQ VSNFKAPDGT TDLGIFELKA ECYKEIDPFF FHFSRNQRER ADEQLRAREK
KAGRNPDSMV TVPLGGFAQE TSPMSLGVSR LFTSRIYQRI LICALIKGYI PPGASSANFA
LPEAVVDAGL QLVMIGIVEA GDTFIETVLA APLGKMTAIH LLCSLEESVK IPALKARITW
CLDKVAKVEA ATAPQAAAAL STHRKVTAPS QAKSGANSLE ARRAAAKARQ QAIMKDFNAR
QKTLMDKFGG DDEEADKSGA TAVDDDMEVD DEQQGEDEDL SHLGSCIMCQ EQLRRDSPFG
SLALVTPSMT IRTTPRNSLA ALNEVVNDVP LTLDRLCIDH EEKVQKRYEQ MSDSKSGVPF
DPQAAPASGG FPRGDHKSGF VASTCGHLMH VRCFDSYYRS IEQRHASQIA RNQAEDLSRS
EFVCPLCKSL GNILLPVPIP PRRSAATSPA TPGSGLGDQR LDRAPIGDWL RKINIDILKT
SGAHTASSVQ EMTTGTGCFS AWYADSSLSS LWDPASIAEN PDGIDESTLI MLDRIFQVLK
PLASSTRHQR VAWQSRTILA PISRKMYIPE ELVAYTISML EVSQRGIESK GNNVADGLSD
TSVGLLRSLV FALRSVASLQ TKGRGQASLR QGLLKRLLPH WSSDEAVRFP LLLRDPLAIL
VEAAAIVPEY FTQVTTLMYY ATLVQTVFGL AQPSVWPQAG AQATAGSPQP RGLAHISGPS
RLSAEEKAAL LECFPDVRWT VGNIVGFVGY ARGNITLGVD SLDDVSLAKM LCTYTLPFLR
RAAILKRTLC GTSTGDGAGS GRDGGVEYLR LLRDLEIVPP SQALPVRAER QAPISSIVEG
WIKHCYAPLA SLFRPLPIAP SPLSSLNEDG LATSQHASPS HPTLQLEHPA IYELVHLPLD
LTTLFQYTQR TVCRRCRTIP PDPALCLLCG ELVCYQNFCC MDQSSERGEC NRHVAVCGGN
VGLFFKIKAN VIFALYYSNG MFSFSPYLDS HGEVDVGLQK GRPQRLHRKR YLDLTKLWLT
GGSGIGSLVS RKLESIIDVG GWITT
//
