ID A0A367Y139_9ASCO Unreviewed; 1908 AA.
AC A0A367Y139;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=ubr1_0 {ECO:0000313|EMBL:RCK59564.1};
GN ORFNames=Cantr_07384 {ECO:0000313|EMBL:RCK59564.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK59564.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK59564.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK59564.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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:RCK59564.1}.
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DR EMBL; QLNQ01000027; RCK59564.1; -; Genomic_DNA.
DR STRING; 5486.A0A367Y139; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000253472; 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 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; SSF57850; RING/U-box; 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:UP000253472};
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 112..185
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 112..185
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1908 AA; 221494 MW; DF65A527CEE908F6 CRC64;
MDEHHHDDNG NTREFSLKRF LLQLPTNANF DFTKDVRKQI RKALFLSISN NGTYLNWLFL
NSFTDRAYTR DDMLEKIERE YDWTFNNYYK SLVSKTNLQH NTHNHRAFHK NLPCGRIFRK
GEPIHRCLTC GFDDTCALCS HCYQPEYHEG HKVHIGICQR ENGGVCDCGD PEAWTRDLFC
PYANVVEDDD EVPIYDRELP EDLAASILAT IAAILDYMVD VIVQCDLQFE DPEETTAATI
ELNTINSTLD PRKYECFDPG FVDANNDQYY LMLYNDQIRY YRDAVQRVHL ASKKVKDFAI
MVTDKVQKFG KAKVISSRNI KLLLERQKIL SSTGLATCIR SHRDVFREDM LDEIVVWLND
FTESELFKTN TMAKNLFCRA FCEKWQNGLL VAGKSDESYT YRIGTLDPTL KIPKIPSRER
NEDSHWLFNT SKWKLDEDLC RECDYNLDMS EYQRNVSHHG SRLQYLIYLD VRLWKATRAL
LHDMYSTSLI INLHYKNIIC YQYVDIYPTI VDMYLIMDRE PELSIMPTLS TQLFTCPTNS
AEILKHGDLT RILSSIYSFL TTGSIRSPED IDVTHQVSIK SLKNRRWGQI FFDISYILTR
SKNSKFIPNS NVVPMTCDML LLFQGRPVMK REKTNHVEYE SPDYTAFFQA VLVLYQFGEV
IASALKTTRE TDSLGILRNY QLAIQYVLTF LCRLENKELP GLVDNEVDIN MHTERMFLKE
PYTGELIQVS RVDEDKVSFL HPAHSFLGWL IEFAKFSEIS QLVEVFDNVK KVYPPSQFGS
LEVSLFDYPI KTIVLMSQIK AGFWVRNGFS VKSQLQLYKN TSLRDYGYAR DLFLIQVFAN
FSHPDVVTFL ILNRWILLDN WLENPESNTY DEKTLPYMLE ECLNFFIHLL TEDIHLKGDD
EETLLKIKVQ REIMHNLCFG PMGYTKLCAQ MPDHIVADRR FEIILKEMTT FKAPKGSNDF
GVYYLKNEYL DEVNPYYCHY TANIKDDAIK FVKERISKRI CKPVGDIIIE PKQLNPEELG
IYRYIGNFST SLHFNHFIIK TLIYICDNQT EVESLLETVL HLIHVCSLEQ TVDVGKYGQF
SDKFFNVSET FHMSIASLLY QILLKEEHKS THTKIRSIFK ILIQRDPEVL SIMQTQRQDF
DLKVVELDAD KINHEDEAGK KKRIAKERQA KLMAKFKKQQ SLFIKKNLYE NLECDSDIEM
ENYSDDHAAW KFPESHCMLC QNAAQDAGPF GIITYISKSS EFRNIPFDDE YWFLKAFSDN
VDLNSHENDV EGGPLLHNNP PTEKWNSFMR QTSNQSVIGP GFNLNDYVES HVVSLSCGHG
MHYQCYLNYL NNSRNRQNQI TRNTPENVDR REFLCPLCKA LNNIFIPLLW SGNDRSLLEF
LKPHSGKNTF ADLEISHAKN KDWVDTLATV SEQELDSTSI LTNIGKEMIS SMDPAREFSA
EQRHFRVLLN NMFQVLSLFT FPQIVKADSS FILVDTIKSI EISLRGVSTD RKLIIHQLSN
NALINLRTLN EFKNSSILMK VKNWSDLPNP RTDAYAKIFA HIFALSKSSI NNSILEADFF
HCLASVLPLP TLGFSFNCIL EATFVGHLIQ SLNIIVKEIS ENCLKKNWAY TILDVPTIAD
IPQNVADDVI ACFKKLWVFN DIANVSVIED KRFGEVIYSM LVRVATPFLR RAAVYAYVQC
ANIDNIDFTL YPETEIEADR LCTFLNIKPV CDYLRAFNDH ESCESRIFHD FINFSNNVSK
TKNTLHMRKE LEYPGIVRLV ELPERLDFFF TKYYYLDKHN NPSMAIEDPA ICLFCGDVVD
VQKQDIGCRE GQCTTHYLKE CANDVGIFLL PKDRSLLLLH KNGGSFYNAP FLDEHGEIAD
ESKKSKALHL MKPRYDDFMR NVWLQHNVQN CIVRNLENVL DPGGWETL
//
