ID G3H0W2_CRIGR Unreviewed; 1247 AA.
AC G3H0W2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=I79_003782 {ECO:0000313|EMBL:EGV97222.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV97222.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH000098; EGV97222.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H0W2; -.
DR STRING; 10029.G3H0W2; -.
DR eggNOG; KOG1140; Eukaryota.
DR InParanoid; G3H0W2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001075; 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; cd19678; UBR-box_UBR1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
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; 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 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:UP000001075};
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 81..152
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 81..152
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 526..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 142618 MW; C72B1A26AD611446 CRC64;
MSDCHLFFPF QWWDQQADFY TAFLHHLAQS VPEIYFAEMD PDLEKQEENV QMSIFTPLEW
YLFGEDPDIC LEKLKHSGAF QLCGKVFKSG ETTYSCRDCA IDPTCVLCMD CFQSSVHKNH
RYKMHTSTGG GFCDCGDTEA WKTGPFCMDH EPGRAGTTKE TLHCPLNEEV IAQARKIFPS
VIKYIVEMTV WEEEKELPPE LQIREKNERY YCVLFNDEHH SYDHVIYSLQ RALDCELAEA
QLHTTAIDKE GRRAVKAGVY ATCQEAKEDI KARHLIEEQN VISVITETLL EVLPEYLDRN
NKFNFQGYSQ DKLGRVYAVI CDLNPAMHCT YLIVPKYKTN PLVQRNNNNN KKGHGLTNLS
FQGMEEIRRQ VGQHIEVDPD WEAAIAIQMQ LKNILLMFQE WCACEVFYYQ DVKCREEMYD
KDIIMLQIGA SMMDPNKFLL LVLQRYELTD AFNKTISTKD QDLIKQYNTL IEEMLQVLIY
IVGERYVPGV GNVTKEEVIM REITHLLCIE PMPHSAIARN LPENAEHMQK KRRKQENKDE
ALPPPPPPEF CPAFSKVINL LDCDIMMYIL RTIFERAVDT DSNLWTEGML QMMFDTVKRL
REKSCLVVAT TSGLESIKNV ETTHDKEKAE RKRKAEAARL HRQKIMAQMS ALQKNFIETH
KLMYDSTSEM PGREDSTMEE ESATAFSDCS RIALGPKRGP ALTEKEVLTC ILCQEEQEVK
LENNAMVLSA CVQKSTALTQ HRGKPIDLSG ETLDPLFMDP DLAYGTYTGS CGHVMHAVCW
QKYFEAVQLS SQQRIHVDLF DLESGEYLCP LCKSLCNTVI PIIPVQPQKI NRVKYSNSIK
EMVILFATTI FRIGLKVPPD ELDPRVPMMT WSTCAFTIQA IVVLPNLQSE DTPCLLSVDL
FHVLVGAVLA FPSLYWDDTV DLQPSSVSSS YNHLYLFHLI TMAHMLQILL TVDTGLPLAP
SEEDSEEARC ASAFFAEVSQ HTGGFVGCSI PGWYLWVSLK NGITPYLRCA ALFFHYLLGV
TPPEELFANS AEGEYSALCS YLSLPTNLFM LFQEYWDTIR PLLQRWCADP ALLDVLKQKS
AVVRYPRKRN SLIELPDDYS CLLNQASHFR CPRSSDDERK HPVLCLFCGA ILCSQNICCQ
EIVNGEEVGA CIFHALHCGA GVCIFLKIRE CRVVLVEGKA RGCAYPAPYL DEYGETDPGL
KRGNPLHLSR ERYRKLHLVW QQHCIIEEIA RSHETNQMIF GFNWQSL
//
