ID A0A2P7YS26_9ASCO Unreviewed; 1255 AA.
AC A0A2P7YS26;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=C7M61_002704 {ECO:0000313|EMBL:PSK38765.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK38765.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK38765.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK38765.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
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:PSK38765.1}.
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DR EMBL; PYFQ01000005; PSK38765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YS26; -.
DR STRING; 418784.A0A2P7YS26; -.
DR EnsemblFungi; C7M61_002704_t1; PSK38765.1; C7M61_002704.
DR VEuPathDB; FungiDB:C7M61_002704; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000241107; 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; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
KW Transferase {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 88..161
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 88..161
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1255 AA; 143012 MW; 22E51E7C73BB90B4 CRC64;
MEDLKRFLVE LPPHFCYKDN RQVKVNVYKA FYWAITGEGE YFSELFTGSA EDHAEILGGF
KWNPTEHLSK KPFFVNTGTG EYSHPKQQIC GYTLKEGDAI YRCAECGYDD TCVICGHCFN
KEDHVHHNVS LYYAGSGNEG MCDCGDDTAF KGQLDCACQG TLDVETNFRG YIHDALHTAF
DYVLDVTNFS ISTLPFVHDN LENRGQRVFD TRQLSDFGAL PFHKYGSVDE NTYDSWYLVL
WNDENHNYDE AQTAIRAATG LPISAAEKIA RLINASGRAV LKEETEPRAL LSSQKLAEAD
GLVCTIMSRR DYVREMIVGA ILNWVCDIIT FSSNSAFREE CKKQLGILLL KPSYEFSKSL
SSEMFPSSIT QLADQCFRSG LVVDGVLDDL SPLSIVKPDF SLDRLIDRFV TPYKVKRRHD
SRLQYLLYFE IRFPLRTRKL CRKIFLALIG GEQASKAQFA DQYIEAYSQL LIISALSDRE
EALSCMDHIR VQLLTCPRTN ARVLENRSLG RLLGPVCWLI EHFASLKNST NGLLNIKEIV
YDVRSKREKS SIEKAIGSCI NDITYIFAKN DSTDILSCIS SDDSFYWLLT LMKFYQGSLP
ITRKVGEHVS QELLKDVLIF LQRSVPIYFI TKCATLADPS VGISDVLKKF FALYSKHMGS
TSRKPSSKVS VNPISLINPI NAFASRLIQA TPVSDLAETI GFHELALLHL TDTSLKSIVL
NSQVKIGLWI RNGSSVSRQA SYYSEYSLKE LSYFRDMQYI HAAGVYSLGE LAYSRDLHIL
QTALVFANPR VVLKMIIDLW ELEEWYSGEV GSELTVYEDR FSYACEQLIK VLYHIFTDRS
LFQTQHLEGP DMFVRRICYS LCDKPKSFSD LITEFDGDDI DVGDFEIHLQ KCALLQSPSG
ITDSGVYRLK PEYYEQLDPL SSCVDLSRFE SVAESLIKNL SKSRKIKENE VVLEPKFVSA
SCGQVNEKFL SFFTTREFAK LMYKLMRESI DSGQEIYIQQ LLHFLHAILV DVQSSETMKK
HLDTYIDIPI CDLLLTIAES SMSSAVTVKA DHLLTKLIDM DDRTSSQFRC TVISLLQHHA
IMASQHLDKI ADPHDIAESS IFTEVIMKYL NGYGPALDYI QKGYVKLIVA LSFELMNIIK
SNSFDFAKLQ TFSKSYDDHI EDDFRTYFGN LFESFKDGII TEHVEREKLE KFFLDSLTQI
AAVYLRQCTI FWDLLTAIQS ENGYETSEKI RKLNVELDKA EENSVFDVLF KLIKY
//
