ID A0A384BDZ2_BALAS Unreviewed; 1754 AA.
AC A0A384BDZ2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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_007197921.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007197921.1};
RN [1] {ECO:0000313|RefSeq:XP_007197921.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007197921.1};
RG RefSeq;
RL Submitted (JAN-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_007197921.1; XM_007197859.2.
DR GeneID; 103004035; -.
DR CTD; 23304; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261681; 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 CDD; cd16686; RING-H2_UBR2; 1.
DR CDD; cd19679; UBR-box_UBR2; 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; 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; 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:UP000261681};
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 DOMAIN 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1005..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1754 AA; 200474 MW; 7A569B4EB9E29026 CRC64;
MASELEPEVQ GLDRSLLECS AEETAGKWLQ ATDLTREVNQ HLAYYVPKIY CRGPNPFPQK
EDMLAHQVLL GPMEWYLCGE DPELGFSKLE QTNKPSHLCG RVFKVGEPTY SCRDCAVDPT
CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHELNT SEIEEEEDPL
VHLSEDVIAR TYNIFAIMFR YAVEILTWEK ESELPPDLEM VEKSDTYYCM LFNDEVHTYE
QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC EQAKSVIVRN TSRQTKPLKV
QVMHSSIVAH QNFGLKLLSW LGSIIGYSDG LRRILCQVGL QEGPNGENSS LVDRLMLSDS
KLWKGARSVY HQLFMSSLLM DLKYKKLFAV RFAKNYERLQ SDYVTDDHDR EFSVADLSVQ
IFTVPSLARM LITEENLMTI IIKTFMDHLR HRDAQGRFQF ERYTALQAFK FRRVQSLILD
LKYVLISKPT EWSDDLRQKF LEGFDAFLEL LKCMQGMDPV TRQVGQHIEM EPEWEAAFTL
QMKLTHVISM MQDWCALDEK VLIEAYKKCL AVLTQCHGGF TDGEQPVTLS ICGHSVETIR
YCVSKEKVSI HLPVSRLLAG LHVLVSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA
QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDIVMLQT GVSMMDPNHF LMIMLSRFEL
HQIFSTPDYG KKISSETTHK DLVQQNNTLI EEMLYLIIML VGERFSPGVG QVNATDEIKR
EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIEAVAHF KKPGLTGRGM YELKPECAKE
FNLYFYHFSR AEQSKAEEAQ RKLKRQNKED TALPPPVLPP FCPLFASLVN ILQSDVMLLI
MRTVLQWTVE HNGHVWSESM LQRVLHLIGM ALQEEKQHLE NVMEEHVVTF TFTQKISKPG
EAPNNSPSIL AMLETLQNAP YLEVHKDMIR WILKTFNAIK KIRESSSTSP VAETEGTIME
ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DASISAVLDN
SPVVSDMTLT ALGPAQTRVP EQRQFVTCIL CQEEQEVKVE SRAMVLAAFV QRSTVLSKNR
SKFIQDPEKY DPLFMHPDLS CGTHTGSCGH IMHAHCWQRY FDSVQAKEQR RQQRLRLHTS
YDVENGEFLC PLCECLSNTV IPLLLPPRNI FNRLHFSDQP NLTQWIRTIS QQIKALQVLR
KEENTPNTAL SRNLENVDEL QLPEGFRPDF HPKNPYSESI KEMLTTFGTA TYKVGLKVHP
NEEDPRVPIM CWGSCAYTIQ SIERILSDED KPLFSPLPCR LDDCLRSLTR FAAAHWTVAS
LSVVQGHFCK LFASLVPGDN HGDLPCILDI DMFHLLVGLV LAFPALQCQD FSGISLGTGD
LHVFHLVTMA HIIQVLLTSC TEENGMDQEN ASGEEELAVL ALYKTLHQYT GSALKEMHSG
WHLLRNVRAG IMPFLRCSAL FFHYLNGVPS PPEIQASGTS HFEHLCNYLS LPNNFICLFQ
ENKEIIKLLI ESWCHNIEVK RYLEGERDAI SYPRESNKLI DLPEDYSSLI NQASNFSCPK
SGGDKSRAPT LCLVCGTLLC SQSYCCQTEL EGEDVGACTA HTYSCGSGVG IFLRVRECQV
LFLAGKTKGC FYSPPYLDDY GETDQGLRRG NPLHLCRERF KKIQKLWHQH SITEEIGHAQ
EANQTLVGID WQHL
//
