ID A0A1L8FAF2_XENLA Unreviewed; 1750 AA.
AC A0A1L8FAF2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=ubr1.L {ECO:0000313|RefSeq:XP_018086546.1,
GN ECO:0000313|Xenbase:XB-GENE-6489184};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018086546.1};
RN [1] {ECO:0000313|RefSeq:XP_018086546.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018086546.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018086546.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_018086546.1; XM_018231057.2.
DR STRING; 8355.A0A1L8FAF2; -.
DR PaxDb; 8355-A0A1L8FAF2; -.
DR GeneID; 108699182; -.
DR AGR; Xenbase:XB-GENE-6489184; -.
DR CTD; 108699182; -.
DR Xenbase; XB-GENE-6489184; ubr1.L.
DR OMA; TWMKLLA; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 108699182; Expressed in spleen and 19 other cell types or tissues.
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:UP000186698};
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}.
SQ SEQUENCE 1750 AA; 199565 MW; CF7284C5C5CA6639 CRC64;
MEAGGGRVEH GREPGEREMH AMCLVNALDF ASAFHQHVAK HVPQIYRDEL QPQVEKQEEL
VQERILTPLE WCLFRDDPNV FMEKLRHSAA PPLCGRVFRG GETTYSCRDC AIDPTCVLCM
DCFQNSIHKS HRYKMHSSMG GGFCDCGDTE AWKTGPYCNI HEPGASDQNS DFRLTDELLA
QTKKVFPVII QYIVDMLIWE EQKSLPAYLD KCTEEWNQYY CVLYNDEHHT YDHFIYSLQR
SLGCDQKEAQ TLTTAAEREG RRAVKKGTSQ QCQEVAESLK TNSENVSLKP FRVEVLHGHV
MAHQSFALSL ANWLNKLLAY SSDFRQIFCQ VCLEREPKPS SFTHTCYVSL LILKDSKLHK
GVRKVLHDLI FSSFFMEMEY KKQFAIEFVK HYKQIQKEYM SDDQDRNISV TAISVQVFTV
PTLARLLIEE QNVIKVITET LLEIITEYLD SDNKFNFQGY SQERFFMVYA IILDLKYILI
SKPTSWSKKL KAKFLEGFKS FLYVLSCMQG MEGISRMVGQ HVEMDSDWEA AIAMQMQLKN
VLTLIQEWCA TDDDILLKSY KECHQSLLQC RTPAPSQEKK LIRMCGHSYQ SYPYQVSKDP
ISIHLPLSRM LAGLHAQMCR SGVITRLCEI FSPENLQVEL MIEHPLRCLV LVGQVAAEMW
RRNGLTIVSQ VFYYHDVKCR EEMYDKDIVM LQIGASYLDP NSFLLLLLQR YELEEAFSNV
AVPTKDMDLA RQHNILIEEM LHVLICIIGE RYVPGISNVT KEECTMREII HLLCMEPMAH
SAIAKALPET DNTDICLDKL ITKVATFKKP GVSGHGVYEL KAEYLDQFNV FFYHYTKTQR
SKAEHTQKKR RKQENSSEAL VPPAPPDFSS AFRNVINLLS CDVMMHILQT VLQRATEEDP
IMWTEGIIQM ALHIIALGLL EEKQQLQRAA ENEVTFHFYH KATRVGTADL NAESLVTLLE
KLKSITQLEA QKDMIIWVRQ LFETVKGLRE ASSHTVPTGA PSDVVKAEEG QSPLEKEKRK
RKAEAARLHR QKIMAQMSAL QKNFIETNKL LYDTTVEVHD STSPVEESPL LAEEGSKVVL
GPKRGPTVPS KDVLTCILCQ EEQEVRLDKP TMVLTACVQK STALSQTRGK VVAHTGETFD
PLFTNPEMLY GTHTGSCGHV MHVVCWQKFF EAMQKNTQQR LHVELIFDLG NGEYLCPLCK
CHCNTVIPII PHVAQQIKSV DAEAINCVFS LPHWLDIVAA RISGYNFNTI KGTKPITPEF
CQIHQDQNYE FRSILSFGVQ APPRYPTSTE GMLVHFATTV YRVGLNVPPN ESDLRMPVMA
WNTCAFTIQC IESWLRDEEK PLFGSLQNRQ HAGLQALVKF TEAQRVTCPQ PLIQRHLIQL
LAVFLPNINI EDTPSFLSVD VFHLLVGSVL AFPALYCEDN VDLHPSTLVS TYNNLYLFHL
LTMTHILQII ISLATDNVPS TEPDDCEEAR TAATLCQDIA QLTNNCVTVD LPGWYVWKCV
REGIMPYLRC AALFFHYLLG VMPPEELQSS GTTDNQLPAL CSFLCLPTNI LLLFQENKDT
VKLLIQSRMS SDQFLQSVLA GKTTALRYPR KRNTLIELPE DYSSLLNQAS QFKCPKSQDA
ERKHPVMCLL CGAILCSQNT CCQEVVNGEE LGACTVHAMH CGAGVCIFLR IRECKVVLME
GKTRGCIYPA PYLDEYGETD PGLKRGNPLH LCHERYRKLH QLWQQHCIIE EIGHNLEINQ
MFFGFNWSLL
//
