ID A0A7E6DQ46_9CHIR Unreviewed; 1631 AA.
AC A0A7E6DQ46;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, 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|RefSeq:XP_035880925.1};
GN ORFNames=HJG60_019905 {ECO:0000313|EMBL:KAF6116824.1};
OS Phyllostomus discolor (pale spear-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Phyllostomidae;
OC Phyllostominae; Phyllostomus.
OX NCBI_TaxID=89673 {ECO:0000313|Proteomes:UP000504628, ECO:0000313|RefSeq:XP_035880925.1};
RN [1] {ECO:0000313|EMBL:KAF6116824.1, ECO:0000313|Proteomes:UP000664940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bat1K_MPI-CBG_1 {ECO:0000313|EMBL:KAF6116824.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
RN [2] {ECO:0000313|RefSeq:XP_035880925.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_035880925.1};
RG RefSeq;
RL Submitted (APR-2025) 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 E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, ECO:0000256|RuleBase:RU366018}.
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DR EMBL; JABVXQ010000004; KAF6116824.1; -; Genomic_DNA.
DR RefSeq; XP_035880925.1; XM_036025032.1.
DR GeneID; 114493913; -.
DR CTD; 23304; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000504628; Chromosome 4.
DR Proteomes; UP000664940; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 FunFam; 1.10.10.2670:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform X1; 1.
DR FunFam; 3.30.1390.10:FF:000003; E3 ubiquitin-protein ligase UBR2 isoform X1; 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; IPR039164; UBR1-like.
DR InterPro; IPR055194; UBR1-like_WH.
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; PF22960; WHD_UBR1; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KAF6116824.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000504628};
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|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 1..43
FT /note="UBR-type"
FT /evidence="ECO:0000259|SMART:SM00396"
FT REGION 879..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1631 AA; 185855 MW; E0211BB97A14A5AA CRC64;
MECFLGSIHR DHRYRMTTSG GGGFCDCGDT EAWKEGPYCE KHELNTSETE EEEDPLIHLP
EDVIARTYSI FAIMFHYAVE ILTWEKESEL PADLETVEKS DTYYCMLFND EVHTYEQVIY
TLQKAVNCTQ KEAIGFATTV DRDGRRSVRY GDFQYCEQAK SVIVRNTSRQ TKPLKVQVMH
SSIVAHQNFG LKLLSWLGSI IGYSDGLRRI LCQVGLQEGP DGENSSLVDR LMLNDSKLWK
GARSVYHQLF MSSLLMDLKY KKLFAVRFAK NYERLQSDYV TDDHDREFSV ADLSVQIFTV
PSLARMLITE ENLLTIIIKT FMDHLRHRDA QGRFQFERYT ALQAFKFRRV QSLILDLKYV
LISKPTEWSD GLRQKFLEGF DAFLELLKCM QGMDPITRQV GQHIEMEPEW EAAFTLQMKL
THVISMMQDW CALDEKVLIE AYKKCLAVLT QCHGGFTDGE QPITLSICGH SVETIRYCVS
QEKVSIHLPV SRLLAGLHVL LSKSEVAYKF PELLPLSELS PPMLIEHPLR CLVLCAQVHA
GMWRRNGFSL VNQIYYYHNV KCRREMFDKD IIMLQTGVSM MDPNHFLMIM LSRFELYQIF
SAPDCGKRLS SEITHKDVVQ QNNTLIEEML YLIIMLVGER FTPGVGQVNA TDEIKREIIH
QLSIKPMAHS ELVKSLPEDE NKETGMESVI EAVAHFKKPG LTGKGMYELK PECAKEFNLY
FYHFSRAEQS KAEEAQRKLK RQNREDTALP PPILPPFCPL FASLVNILQS DVMLCVMRTV
LQWAVEHTGC AWSESMLQRV LHLIGMALQE EKQHLENVME EHVVTFTFTQ KISKPGEAPN
NSPSILAMLE TLQNAPYLEV HKDMIRWILK TFNAIKKMRE SSSTSPVAET EETITEESSR
DKDKAERKRK AEIARLRREK VMAQMSEMQR HFIDENKELF QQTLGLEASN SAVLDNSPMV
SDVTLTALGP AQTQVPKQRQ FVTCILCQEE QEVKVESKAM VLAAFVQRST VLSKNRSKGI
QDPEKHDPLF MHPDLSCGTH TGSCGHIMHA HCWQRYFDSV QAKEQRRQQR LRLHTSYDVE
NGEFLCPLCE CLSNTVIPLL LPPRNIFNNR LNFSDQPNLT QWIRTISQQI NALQILRKEE
SIPNIASSKN SKNMDKLQLP EGFRPDFHPK NPYSDSIKEM LTTFGTAVYK VGLKVHPNEE
DPRVPLMCWG SCAYTIQSIE RILSDEDKPL FGPLPCRLDD CLRSLTRFAA AHWTVALLSV
VQGHFCKLFA SLVPDDSYGD LPCILDIDMF HLLVGLVLAF PALHCQDFSG ISLGTGDLHI
FHLVTMAHIV QILLTSCTEA NGMDQETPAG EEELAVLALY KTLRQCTGSV LKEIPSGWHL
WRSVRAGIMP FLKCSALFFH YLSGVPAPPE IQVAGTRHFE HLCNYLSLPS NLISLFQENS
EITKVLIESW CQNSEVKRYL NGERDAISYP RESNKLIGLP EDYSSLINQA SNFSCPKSGG
DKSRAPTLCL VCGTLLCSQS YCCQTELEGE DVGACTAHTY SCGSGVGIFL RVRECQVLFL
AGKTKGCFYS PPYLDDYGET DQGLRRGNPL HLCKERFKKI QRLWQQHSVT EEIGHAQEAN
QTLVGVDWQH L
//
