ID A0A3B3CHS1_ORYME Unreviewed; 1544 AA.
AC A0A3B3CHS1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=UBR2 {ECO:0000313|Ensembl:ENSOMEP00000017397.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000017397.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000017397.1}
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|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 Ensembl; ENSOMET00000026113.1; ENSOMEP00000017397.1; ENSOMEG00000020662.1.
DR GeneTree; ENSGT00950000183075; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261560; Unplaced.
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 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1544
FT /note="E3 ubiquitin-protein ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017183614"
FT DOMAIN 111..182
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 111..182
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT COILED 952..981
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1544 AA; 174011 MW; CD49601DB87608DA CRC64;
ITCSPPGGAM SLTRLFFFHI NVWLSPVSQT LLPPLPQCWW ASADLQQELY HHLAAYVPRI
FLGRGEGNSR EEQKEELACQ LLLLAPLEWL LLGEDPASGL ALLQENNCPS ALCGHVFKVG
EPTYSCRECA ADPTCVLCMQ CFLESAHRQH RYRMTTSGGG GFCDCGDTEA WKNAPWCQKH
ARVDGHTEEV RKVFFIILKY AVDLLTWEQE DQLPAGLEPP YRADTYFCVV FNDEVHTYEQ
VIYTLQKAVS CSHKEALSFA TAVDREGRKS VRFGDFQFCE QAKSVIVVNS ASLIQRNKSR
QSKPLRVQVM HSSVVAHQCF ALKTLKWLGQ IIKYSDGLRR ILCQVGLQQG PEGENSSLVD
RLMLNDSRMW KGARNIYHQL LMNSVLMDLK FKKIFAIQFA KNYRSLQTDF LEDDHERVVS
VTSLSVQLFT VPTVGRMLMV EENLMTTIIR TFVDHLRHRD VHGRFQFDRY TAQQAFKFGR
VQSLIGDLKY VLISAPSEWS DSLRVKFLEG FDAVLDLLTC MQGMDPVVRQ VGQHIEMEPE
WEAAFTLQMK LTHIISMIQD WCSTDERVLI QAYRKCLSAL TQCHGGLLDG EPPVSLSMAG
HCVETFRYQV SQDKVSIHLP VCRLLAGLHV LLSRTEVASR FPEQLPLVGV LPLRCLVLCA
QVHAGMWRRN GFSLINQIYY YHNVKCRMEM FDKDIIMLQA GASMMDPNHF LMMVLSRFEL
FHIFSSDFVQ QNTLIEEMLH LIIMVIGERY VAGVGQVEPL EEVRREIIHQ LSIRPMAHSE
LVKALPENGN KETGLERVID SVALFKSPGV TGRGLYELRP ESFKHFNLYF HHYSRADHSF
AVSDLSRDPA VALPPPLPPP LCPLFGSLVN LLQCDVLLAV ESAVLQWAME PGGGGWTESM
LQRVSQQGKA PTSSGSILAL LETLQNAPHL EVHKDMITWI LKVKRTSSAS KKEKAERKRK
AEMARLRREK IMAQMSEMQK NFINENKEMF QQSGEEMGVF PSLELTCASQ VCVGPRRVGG
SERRQQVICI LCQEEQEVTG VGQAMVLAAF VQRSTVLSRN RHWRDPPRDR LTPTLSVATS
CTPAAGRARS LCSSRYFEAV QLKEQRRQQR LRGHNSYDVE NGEFLCPLCE CLSNTVIPLL
PHTPLPDHSA DHLSLEAWLK KTSQQVESSP FSISICEMII TFSMSVYKVG LKTNPNEQDH
RVPVLSWSTC AYTIQSIGEN SPERASQDDC LSALTRFSSA CWASVPLRTV HAHLSRLLTV
LLPDPPVENA PCILHVDMFH LLVYAVLSYN SLHSTEPSGP SVDSSHVHLL HLITVAHMVQ
ILLTSVTALK CNNLMINLEC KSSSSHSTKS VVLPDVSSGW QLLHRLKVGL LPFLRAAALF
FHYLNSSVPP TDLMGECSSA GWEVLCSYLS LPSNLLLLYQ SETRCLCRYR WCHHPALKHT
LQGGGDFIRF PRESNRLIDL PEDYSVLINQ ASSFTCPRSG GDKSRAPTLC LVCGAMLCSQ
SYCCQVEFFP SMNCHLTVVE GFEGSSSPSP VWGIPWQTDP SRLY
//
