ID A0A367Y3D8_9ASCO Unreviewed; 1795 AA.
AC A0A367Y3D8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:RCK59561.1};
GN ORFNames=Cantr_07383 {ECO:0000313|EMBL:RCK59561.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK59561.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK59561.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK59561.1,
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|ARBA:ARBA00004906, 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:RCK59561.1}.
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DR EMBL; QLNQ01000027; RCK59561.1; -; Genomic_DNA.
DR STRING; 5486.A0A367Y3D8; -.
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; cd19672; UBR-box_UBR1_like; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF26; 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 PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 89..162
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 89..162
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT COILED 1077..1115
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1795 AA; 204615 MW; DB09488A8B52D65E CRC64;
MNPDNLKRFL VEVPLKLHFR DSTGIQHYIF KVLYYSATNG GEYLQTLFPN ISTDDAYDIT
TIYDVPIETE QTRPFYKQVK AEYTHARDKA CARPFAAGER VYHCLDCGFD DTCVLCSYCF
NEKDHLSHNV TSYQSRGTSG GICDCGDTEA FVNTLHCKCQ VDDEEGEELN DTLESLQKTM
TIALDYVLDV TNYSLLTLPF IHTELCKGYP AVNLEQLSDY SSLPKESYGG TEDINSTDKW
YLVLWNDEFH NVTQATNAIK DGTGVNEARA QQIAKKIDHD GYCVLKESTT PRALARSKKL
VESNGLVATI VSARDFLREK VCVAILNWFN DVLNSHSLKI SKFAQTCFAE LLLDSSFEFS
NVLPAKLLLA TFRISSDDEK RTYFENGIPY EGKLVNLNYH ELKQPVESLN LYESISDLMN
SKIQLDDLKG SRLQLLLAFQ IRFPKRIRKS LGSLLVPYLV KTPELKQEFA YQVVELYPTL
LNMYALTDRE EDLNLLNDIA SQLFTCPQTV RTILENGKVD SILGPLAKLV EEHSSKYDPS
KGYGVYSESY PKSQQRRRLR KAISHSFKSL THFFYPAVSG DSMVNFLKPN TIRLLILLLR
NFQGFAPLVR KYGDHVEMDI VDLSIYWDFT LPILSSMKNL AVAMWDQPEV DNATIKLLDF
LIKQPKTEKQ PGVLQFQVSK EPVGFVNPLN TLLSFFLEFR DIQTFQPLLE AYKSDLVAIT
DVSLRSIVLG SQVLTGFWIR NGAVASRQAT LYFGAFLPEF TFIRDFHLNQ VAVLFEDPEK
VLINFLERWE LYPWFKNEVK FDRTIYEERF FPIVERFISF AYNLFVDRSL LIKESPREAT
LKKLKRSIAY ALCEEAMAYT PLRDKLDSDV KKLDEFDDIL FEVADYQPPS ALVDTGLYRL
KGSLYKNLDP LSILLDPGDF QVISEVLLKN TKKKRDEPKV LTPVIIESGV ESIDKRIGDF
AKTLQFVKLI YKFLQVAIDT SNETYLPHLL HLIHAIILDD EKIHGKQYLN ENFVDIPVTD
LLLTIVESKM SKQVCEKADF LVDQLVSKDK RIVDSLVDCF GEEYIQTYKK RKTNLFESEA
NRKKRQAEER NNKVLKKFLR QQEKFLNQNK DLTSETAGNE KVSAGDDTKN LRTCVACGEL
ESFEKPLGIM VSSTKAPIFW KLPPLAGEAL AAAYKEWNND LLLHSNVDDY GIGYDTGDAP
PTYGNDFEAR VLSTCGHSIH YECVARRTLG ISQYPCPLCH NLHESFIPSF MGNLDVEVPR
DILFGSTELA KYNQIVQGVN SNSKRTRLLE VFVKLEHFSE ASRVLHGVVE TAGTALLRRK
YLFPGNGPND SKFNRLMDLG NLLADTIRMN EIATRLNGAE GYTDFLSQIP GSTKTLLLSI
IQLRLIHEGK TFSRTLEGNA VDFSREVCQF WDANTLLDSV FNEVVVLFFQ TDESLSTLAK
WGMAKIVSIS VYSMLNRYEH DEEYFKSIQS GLGETDSADD ETVEAFYQFL SNVLFANDRH
VRKFDKEMSV LLYHAIERIL GVFLRQMIIF QDALTIKQQA ENTYESIPEL AQLGEKIELQ
TRLSDTKALT DVLQIPSYNE LILNLLHSAD SLETNVFDIL WNAKIPKHMN QKILSLDYPG
MVHLTSLPLD YSASILKAPL SVSRENFKCL VCGAWIKERG TMSHMMMCAS QTGIFFSPST
NGFKVYVYIG HSPIGIRLPA PYLTKHGEVK TRSYKGKATL NEFRFAYLNK LWVTQGLYAF
VTRNLFGSGI ELGGINVNFE TDDVEAEDEE EEEEDDVFVQ FGPDDDIDDD NFMIM
//
