ID A0A091FKL9_9AVES Unreviewed; 1739 AA.
AC A0A091FKL9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
DE Flags: Fragment;
GN ORFNames=N303_05393 {ECO:0000313|EMBL:KFO70148.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO70148.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO70148.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO70148.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL447129; KFO70148.1; -; Genomic_DNA.
DR STRING; 55661.A0A091FKL9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053760; 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; cd16685; RING-H2_UBR1; 1.
DR CDD; cd19678; UBR-box_UBR1; 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; IPR047507; UBR-box_UBR1.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF27; 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:UP000053760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 70..141
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 70..141
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 818..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO70148.1"
FT NON_TER 1739
FT /evidence="ECO:0000313|EMBL:KFO70148.1"
SQ SEQUENCE 1739 AA; 198914 MW; A6DC88331CE1FC39 CRC64;
WCDERFNFQA MFLKCLAKHV PNIYSAEMDP LLEKQEEMVQ AAILYPLECY LFGEDPDMFL
EKLQQSGTSQ LCGKVFKGGE TTYSCRDCAV DPTCVLCIDC FQNSIHKNHR YKMHSSTGGG
FCDCGDTEAW KAGPLCTKHE PGASGSAKEN SEWQLNEEIL EHSRRVFPSV IKYIVDMLVW
EEEKELPPEL TISREKIDSY YCVLFNDEHH SYDHVIYSLQ RALGCELGEA QLHTTAIDKE
GRRAVKAGHY ASCQEAKEEI KRHSENVSQR PLHVEVLHAD VMAHQKFALR LGSWLNKLMS
YSSDFRQIFC QICLTEEAGS EKPCFISKLM LWDAKLHKGA RKVLHELIFS SFFMEMEYKK
LFAVEFVKYY KTLQKEYISD DHDRVLSVTA LSVQMFTVPT LARHLIEEQN VITTITETLL
EVLPEYLDKN DKFNFQGYSQ DKLNRVYAVI YDLRYVLVSK PTLWTDRLRE QFLEGFVSFL
RILTCMQGME EIKRQIGQHI EVDPDWEAAI AIQMQLKNIL LMFQEWCASD EELLLRAYRE
CHKAVMRCST NGRSREKTVF HLCGHTLESR PYRVSADPVS IHLPLSRTLA GLHVRLSKTG
AISRLHEFVS PEEFQVELLV EYPLRCLVLV AQVAAEMWRR NGLSLISQVF YYQDVKCREE
MYDKDIIMLQ IGASLMDPNQ FLLLILQRYE LADAFRKIKP TKDQDLIKQY NVLIEEMLQI
LIYVVGERYV PGVSNVTKED VIMREIIHLL CIEPMAHSAI TKSLPENENN ETGLENVIDK
VATFKKPGVS GHGVYELKDE CLKEFNMFFY HYTKTQHSKA EHTQKKRRKQ ENRDEALPPP
PPPDFSPAFN NVVRILNCDV MMHILRTILQ RAVELETHLW TEAMIQMVLH LLSLGLLEEK
QQLQKSPEEE VTFDFYHKAT RMGSSALNAV SVLMLLEKLK RVPQLEAQKD TVSWILQMFD
TVKRLREKSS LTTVAATSGS EAIKGDETQS TQDKEKAERK RKAEAARLHR QKIMAQMSAL
QKNFIETHKL LYENTLEAQG KEDTVMEDES MPSAIDYSRI ALGPKRGPSV SEKEVLTCIL
CQEEQEVKLE SAAMVLSACV QKSTALTQNR SRILELSGDT LDPLFMHPDL PCGTHTGSCG
HVMHAACWQK YFEAMQLNFR QRLHVEQIFD LENGEYLCPL CKSLCNTVIP IVPLQTQKIN
SEDAEAVAQI LSLSRWLETI IVRISGYSAK NAKGEKQNLP AFANKGVGSS ALEFHSILSF
GVQSSAKYSS SIKEMLILFA TTIYRVGLKV APNETDYRIP MMTWSTCAFT IQCIENLLET
EGKPLFGSLQ NRQHSGLKAL VQFASAQRTT SPQVLIQKHL IRLLGVLLPN FKVEDTPSLL
EVDMFHVLVG IVLSFPSLYW EDAVDLQPSS ISSAYNHLYL FHLTTLAHIT QIVVSSATVG
FIFLCVESPD AQPPDNSEEA RSAQSFCREV YQYTSGCFSQ DIPGWHMWDR VKKGIMPYLR
CAALFFHYLL GVSPPEELLQ VSEEGQFKAL CSYLSLPTNL FLLFQEYWDT VNPLLQRWCA
DPVVLSCLKG KSIAIRYPRK RNSLIELPED YSCLLNQASQ FRCPRSSDDE QKHPVLCLFC
GAMLCSQNTC CQELVNGEEL GACTSHALQC GAGVCMFLKI RECKVVLIEG KTRGCLYPAP
YLDEYGETDP GLKRGNPLQL CRERYRKLHL LWQQHCIIEE IARSQETNQI FFGFNWQLL
//
