ID A0A452RZD3_URSAM Unreviewed; 1328 AA.
AC A0A452RZD3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000024963.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000024963.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
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DR Ensembl; ENSUAMT00000027866.1; ENSUAMP00000024963.1; ENSUAMG00000019280.1.
DR GeneTree; ENSGT00950000183075; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000291022; 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; cd16686; RING-H2_UBR2; 1.
DR CDD; cd19679; UBR-box_UBR2; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR047508; UBR-box_UBR2.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF28; E3 UBIQUITIN-PROTEIN LIGASE UBR2; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 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:UP000291022};
KW Transferase {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 114..185
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 114..185
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 954..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1328 AA; 152447 MW; 241F2223D8E1AE9E CRC64;
MISSTASPSP FPEVGGGGCY FQPSYHMLCS PGNQVCIPGG FPKKWLQATD LTREVYQHLA
HYVPKIYCRG PNPFPQKEDM LAQHVLLGPM EWYLCGEDPA FGFPKLEQAN KPSHLCGRVF
KVGEPTYSCR DCAVDPTCVL CMECFLGSIH RDHRYRMTTS GGGGFCDCGD TEAWKEGPYC
QKHELNTSEI EEEEDPLVHL SEDVIARTYN IFAIMFRYAV EILTWEKESE LPADLEIINT
SRQTKPLKVQ VMHSSIVAHQ NFGLKLLSWL GSIIGYSDGL RRILCQVGLQ EGPDGENSSL
VDRLMLNDSK LWKGARSVYH QLFMSSLLMD LKYKKLFAVR FAKNYERLQS DYVTDDHDRE
FSIADLSVQI FTVPSLARML ITEENLMTTI IKTFMDHLRH RDAQGRFQFE RYTALQAFKF
RRVQSLILDL KYVLISKPTE WSDDLRQKFL EGFDAFLELL KCMQGMDPIT RQVGQHIEME
PEWEAAFTLQ MKLTHVISMM QDWCALDEKV LIEAYKKCLA VLMQCHGGFT DGEQPITLSI
CGHSVETIRY CVSQEKVSIH LPVSRLLAGL HVLLSKSEVA YKFPELLPLS ELSPPMLIEH
PLRCLVLCAQ VHAGMWRRNG FSLVNQIYYY HNVKCRREMF DKDIVMLQTG VSMMDPNHFL
MIMLSRFELY QIFSTPDYGK RFSSEITHKD VVQQNNTLIE EMLYLIIMLV GERFSPGVGQ
VNATDEIKRE IIHQLSIKPM AHSELVKSLP EDENKETGME SVIEAVAHFR KPGLTGRGMY
ELKPECAREF NLYFYHFSRA EQSKAEEAQR KLKRQNREDT ALPPPVLPPF CPLFASLVNI
LQSDVMLCIM RTVLQWAVEH NGYAWSESML QRVLHLIGMA LQEEKQHLDN VTEEHVVTFS
FTQKISKPGE APNNSPSILA MLETLQNAPY LDVHKDMIRW ILKTFNAIKK IRESSSASPV
AETEGTIMEE SSRDKDKAER KRKAEIARLR REKIMAQMSE MQRHFIDENK ELFQQTLELD
ASTSAVLDNS PMVSDTTLTA LGPAQTQVPE QRQFVTCILC QEEQEVKVES KAMVLAAFVQ
RSTVLSKNRS KFIQDPEKYD PLFMHPDLSC GTHTGSCGHI MHAHCWQRYF DSVQAKEQRR
QQRLRLHTSY DVENGEFLCP LCECLSNTVI PLLLPPRNIF NRLNISDQPK LTQWIRTISQ
QIKALQVLRK EENTASSKNS ESMDELQLPE GFRPDFHPKN PYSESIKEML TTFGTATYKV
GLKVHPNEED PRVPIMCWGS CAYTIQSVER ILSDEDKPLF GPLPCRLVSY QFTQFTEWWD
GNSVVLFF
//
