ID A8XEC1_CAEBR Unreviewed; 2072 AA.
AC A8XEC1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=ubr-1 {ECO:0000313|WormBase:CBG12009};
GN Synonyms=Cbr-ubr-1 {ECO:0000313|EMBL:CAP31056.2};
GN ORFNames=CBG12009 {ECO:0000313|WormBase:CBG12009}, CBG_12009
GN {ECO:0000313|EMBL:CAP31056.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP31056.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP31056.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP31056.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601540; CAP31056.2; -; Genomic_DNA.
DR STRING; 6238.A8XEC1; -.
DR WormBase; CBG12009; CBP49404; WBGene00033024; Cbr-ubr-1.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_001801_2_0_1; -.
DR InParanoid; A8XEC1; -.
DR OMA; GEASYMC; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:EnsemblMetazoa.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:2000212; P:negative regulation of glutamate metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0043058; P:regulation of backward locomotion; IEA:EnsemblMetazoa.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
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; 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; 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; 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:UP000008549};
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 93..180
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 93..180
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1401..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2072 AA; 233881 MW; E4F4BB36D9C1E9D8 CRC64;
MIVDLVNCVR QEEWGQVHQL LLKHWLAQVP EVFEINADMP WDNSGINERL LGAPGELLFS
PLVSAFLLDV HNTKSSLETM NELAGVDPAK GAKICGHVFK NGELTYTCLD CATDGTCVMC
LQCFEVSIHK AHKYKVSVLY IWLILKQTTF KMHSSSGSGY CDCGDKDAWL EGYACANHEK
KEEEEAAVLA PELRNRCEQL VEIILHFALS LITHKDDLTL PEAFEEFKPE VPVDSQQFLT
VLYNDETHTY ESVIKVLELY IHCTKDQAML VATIVDREGR SAVKLGNKVD CTKAKEDVQK
KTSRDSLSIR RASTHHLPLS VKVMDTMLFS LQSFSISLLT WLNAQMEVFP PLREIVGEIL
LTSKFELKKD YVKKQSKSEE GLIAQIVQNV RDGMDADDEA ELIQLVNDGI DAGEIIAEVE
DEQMEVDADD DEEIVRALTA GIEQQGPSRE STTFTILENI LLQDTQMWKA GRCILHQLLM
RTVFMIYEQK VRFAKVFMQH YNEIYEDFVK DDHEMEVSVV GLSVQFMTVP SLARKLVAED
EALSVISNAI RLQTNKYISR GSTNMSEIGR FDFTSRSFPA DLRRALQITR DLAYILNAIP
SDADWTRELI EGFVKGFTDF LVFLQHLQGM DEVKRQAVEH QVWESEWETA FNILLRLKDA
IALVISWAES NVSDFVRFYL SFKVYHFQEE VHNRLLLMCL ELMNKMPPVY TKTSEDSSGL
TVTINGESST ITHFDVLKSA TSIHQPVVRI IAGLFTAKDH AMFLKTSKPG TELQEKIRSL
LQSNEDTNLY ELALRVLVLC AQTNASLWRR NGFSLVNQIH NYFSPLCRSE MFDRDVLMMQ
VGAALTPPLK FIIHLLHRFR LDKWATTEFE QDKAAAAQTK PESEDLSKTM VLIAEEFFQC
LILIFSERYT YGVGKTNPLD GLKREVVHIL CTGSHTFSHI QQKVSHDNNT KRVSLHEAVN
QVADFRKPLS TSAGQFHCKE SCLPMYSPFF MHYSKSDQSA AEQCQARVRA KMDRVTRSCF
PNPLPDYLPF FENLPLILKS NMLIHVFKLV IDRTTRRSRF SSDRVFHKVL YLIGIALNEE
EKDPDFGFTH KAEENVGLLG MLEGLLGKQE ASICPALLEV TVEKYRKLLK RNSGPPEPVI
VETHPMSTAE ELKAKRQAKA AEMRQKAMAK MSSMQSKFMK KIEVDESKDE THVKTEGAIK
PEDCDNKDED IVKQIGHDFP VCIGINKWQT EIEKPRILTC ILCQEDEVIA PQLGKPMVCA
AFIQQSQLFT HKNQKGELMT ASSGAISTRD LLTAPATLQY GVDASTCSHS MHYECYKSLP
ESHPSPDSSR ARQVAPHPHK MVDTESGEFQ CPLCKRLWNA AIPILPAYQL TNQIGFSTVS
GAANENFEVW VARVKRSLEM PLSSESVTKK GHSRKRSHSE RSLLDLEKLS QTSKESDGSP
KYSYNATHTD TPTESKIIMN SPPSADDADF YNELAALFVD PETNNTNSPT ATPTPAGESN
PRSSESTSSE AVKKPLSSQI QHAIHTLIRP FPSMSKSKIC STAFDGFEEP IKDLGKNMIK
YRRRGNESKV NFIEKHLKGY AISTVTWQSA AHVARAISSY LYYDKKPLFG ALNTRQRDCM
SAMSRLCASL SHNMQFLLHA VSDMLRVLLC DPPTAKVTQT LGSPLFGTSS SSANPSSTPH
SGTNFAFFVQ LFNPAGPRKN VNLNILQVDI LSLAISLMMT IGWTWNNGVQ SMSNTSTKAT
THQKSRLLTP DGSVDEAYVL RLALLAHYFQ IFATHDESDG EDANMDDGSE IHSNLDPAII
EIMVKLYSIC HPDDQPLRRV DVLWKKLEEG AHSLLRPVAL LYHYITLVDP PEALKDPSIH
SAEALFRYVG LPSKIEEHIQ GSLVESLFVM WSLAIPKDDH LLRELVVQPV KPNLLVDLPD
RYSQLINRVA SFKCPTIPIE ESTSNVPTLC LVCGTILCSQ AYCCQKIVNK QSYGACRYHM
SQCSGSVGMF LRVRDCSLVL MTTRKRGCFR PAPYVDEFGE VDQGFRRGNP LHLNPELYQK
LKSLWLQQGI TEEVVNYNEI DYRNVQYDWA HF
//
