ID A0A1V2L8V9_CYBFA Unreviewed; 1866 AA.
AC A0A1V2L8V9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=BON22_2113 {ECO:0000313|EMBL:ONH68328.1};
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH68328.1, ECO:0000313|Proteomes:UP000189513};
RN [1] {ECO:0000313|Proteomes:UP000189513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(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}.
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:ONH68328.1}.
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DR EMBL; MPUK01000003; ONH68328.1; -; Genomic_DNA.
DR STRING; 36022.A0A1V2L8V9; -.
DR VEuPathDB; FungiDB:BON22_2113; -.
DR OMA; GEASYMC; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000189513; 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; cd19672; UBR-box_UBR1_like; 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:UP000189513};
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 107..180
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 107..180
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1866 AA; 213866 MW; E098A46DFED0C7C1 CRC64;
MNHRGGDCAL PCTFVDNGEL LKKALLQFPK RYQHDFSRPA KVDLRRLLSF AASYKGTYMK
ELFPEVDELT LPKAWQHVLV PERYQHLESQ DFYFQRGSFD DPAHPHRACG RKFKKGEPVY
RCMTCSDDET SGLCQNCFDA DQHDSHDVIT SICQRENGGV CDCGDEEAWR VQLNCKHYHT
AETPESEIPE KFKNSLLQTF EIVLDYIVDV MSSSPLSFSK DRKQNNESIL MDGHSSTLEQ
GMYFGTDWPS DKFHLMLYND QNRQYRDAVQ RITSTTDKVD DFAIMVADEV NVNGRAKVMT
SSHIDELLQA QSTLEATGLA SLIRNARDVF REEMCGEMVL WLTEMMNGPV HGNYNITRDI
LAEAFCQKWK IGVKPTHDAQ PFPGSLFNNE IPTIPSRTTA SWQFGEASVP QTPEHWKVSP
VKWDIDPVLA ARCDYDPDFI RNTQSTASFH GSRFQYILYF DIRLWKSIRS NMHTLLNSVL
TSNKRFRPLV CAQYTDIYPT ILELFFLFDR EPEFSCMTTL TSQIFTSSLN ATMIANHGDL
TRFLAAIYSY LTKLFLMRPE DIVISKDLLS TSFKNRRIGQ VFFEICCVLN KTKSFSPILC
PEFMNQVCDI LDLFQGKPTL KREAVEHVEY ESNDYGLYFN MYSVISSLAE MIAKTLLKTD
SAEGLNWVAL IFDRIGLAGE MPSDQVSQGE PTDVGPLNKI VIESLEGPQE IVSFKLENSP
VSFLHPLHAF ATWVVQYSNI GDTYELERFL RDSGDLKFHI LEYPLRTLVL LAQIRVGYWV
RNGFSIRTQQ HIYRTSGIRE SGFKRDFYMI QLMMCLLDRD LVVSSFLSRW ALLSWCKEEL
SPEPYDETIL PLMVEEFLLT TIQLLSDTSA LEDFENSTEN RIKKEIIHCL CFQPMSYSKI
CSDIPDYMAH EKRFDLILSS VANYIPPASP SAAGMYKLKE EFMDQVDPFY VHYSTNKRDE
AEKLVKERIA KKTGLAVKDV YIEPSPHSLA NTPFKNLFKI TSSKIFVQFI RSTLKVVNNE
GVVKTESLLN LSLHLIHLAS AGLELAYSAV FNELIFSEFR ADHNEPFYYE SVGALLYKFL
TDETCAAYHS KIRAIFKVLK SYHFDIEAYL HEQVQNFDAS LLGMAALTAS TKESEFEKKK
RMAKERREKI MAKFKRKQTE FVEKNNVEPE AADISPEDAE NGNSWHYPEE HCILCQMSVT
TGDSVFGVVC NVSRFSGSRT VPFHDKYWTL RSFEESGSLD DDDCVSQSEC LPRYFEKIQK
EAVVGPAFPS HTRNALRSDM MATSCGHGMH YSCYQNYLSS AKARQTQITR TVPEDFENSE
FICPLCKSLG NLFIPIMWNN NKNKLSAFTA PDQDWYSQFE KIKNISFVEP EICDQFSRQV
VEDCKLSLKN SFKDMAFDDE QHMMLHDIWV SLSSKLESIT QPQFREHLNK LVSSTIKGTE
ISVRGLASDT GLVTGLISNQ CLTTLRILTE LKKTWVALAA NPEANKAKPK GFSVKFAEEM
VGKLVYLSSD RLFDVFEDID FFELLVGCTP FYGISMNSLY RLTFTYHFIQ QLAIILAQLH
NELFEGEISI LDITVVKAPE TAYYNLVAMA RDLRDNHPLF DNVSDGIFES IEFQEVLYTL
LVRSLTPFLR RVAIWSIANC ADYSDVSLDP WLEDEDVDGL EVNRLCDYLN IPSVEEMLAL
FSGDGIENQK FQAFLKYVST TDNELSFKSL EYTGQVRLVD LPERMDDIFT QLLYKKYKFT
SLAHYDPAIC LFCGDIVNLQ KKAPGQVIGE CNHHAENECL NDMGLFLLPK HSATLLLDRG
NGSFHPAPYI DSHGEYDSDV RQNQVLLLSR QKYDTFIRQM WLQHDVKNFI TRKLEGTVDI
GGWETL
//
