ID A0A8C5C9V5_GADMO Unreviewed; 1654 AA.
AC A0A8C5C9V5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 3.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049 {ECO:0000313|Ensembl:ENSGMOP00000057471.1, ECO:0000313|Proteomes:UP000694546};
RN [1] {ECO:0000313|Ensembl:ENSGMOP00000057471.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSGMOP00000057471.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSGMOT00000026110.1; ENSGMOP00000057471.1; ENSGMOG00000010333.2.
DR GeneTree; ENSGT00950000183075; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694546; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
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 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; IPR047507; UBR-box_UBR1.
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: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; 2.
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.
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:UP000694546};
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 80..152
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 80..152
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 816..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1654 AA; 186540 MW; 30220F82D3C0EA62 CRC64;
MACHLSAVMQ KWLDAADSYA ELRSYLRDMV PRTYHLDTVL DPQEEERVQK CLLHPLECFL
FGEDPEEGLA KLKQGSESSG ICGRVFKEGE TVYSCRDCAI DPTCVLCMDC FQENFHGNNA
YFPMHASSGG GFCDCGDLEA WKIGPCCAIH DQGTAVAMET DASVLDPVLH ERAEQLFRCL
LRYVTEMLVW EKYYELPEDL EPRVDEEVYL CVLYNDDHHS FDHVIYSLQR SIKCTQAVAQ
AHTALIDKEG RWIVKKGTVL ACQEVNDLIE SNSKHISQEA LRVEVLLYAV VAHQTFALRL
GNWFQKIVGY SGKSNHPVPF PVSCLISRTL FFWSLPLGAR RIVYELIFCS LLMDTESKRL
FAIEFTKNYD MLQQCFIFDY HDRSIFISSL SVQIFTVPTL ARHLIEEAKV IKVIVGTIME
VLKGHLCDSN RFQFQGYNSD KFFRIHVIFH DLRYILISKP TEWTDALRTA FLEGFKAFLD
LLGCMQGMEE VKRQFGQHIE VEPEWEAGFS LQIQLRHILS MFQDWCASDE TVLLQAFREC
HGALIHCNHR ANQSEPTDFY MCKQILHIRP YKVSQEPVSI HLPISRLFAG LYLHLCRTGA
IERLHQHVDP ASYDYTYLAE HSLRCLVLVA QVSAEMWRRN GLSLVSQVYY YQDVKCRDEM
YDKDVLMLQI AASKMDPNHF LMLLLLRFEL FDVFNGSTSG KDQELLKQWN RLTEEMLFLL
IVIIGERYVP GVSEVTKEDV TMREVIHLLC IEPMAHSGLV KGLPENESHE TGLESVISKV
SNFKKPGVSG HGLYEVKKEC LPEFNPFFYH YSKSQHSKAE DSQKKRRAQE GTDQALRPPV
PPAFCPAFSS VVRLLSCDIF VHILRRVLQR AAKDRSTQWT EAMVQRALHL IGQALLEEKS
QLEAAADEEV AFDFSVKARL GSEHSKSVFQ LLTKVKSLPA LEGHSDMVKW ILQVTMNRPK
ALPSSLLSPQ VAQDKDKAER KRKADAAKLH RQKIMAQMSA MQRNFIESNK MLYDNMPDSS
SSHPGPAATS SESSSVPEQR ERCVALGPQR GSTPAQREVL TCILCQEEQE VAALSQAMVL
TACVQRSTVL TQCRGKALGH LSEAFLRTPS NSLFMSPELV VGTHTGSCGH IMHSSCWQKY
FEAIQNTTRN RLHAELIIDL ENGQYLCPLC KSLCNTVVPL VPLEPLTIDY ENAEIVGQHL
TLPRWILILL ARINGLKSIN HKGASPEEAS GLCGEGRPDF RSILSFGVQE PRKFSDSIAE
MLVVCATTVH RVGLETPPNE LCPHVPTMAW NTCAFTIQAI GEPSRTHDAP PLSPVLLPTI
SRENTPSILE VDFFHLLVGM VLSVPALYHE EAVELQPSAV SSAYNHLYIL HLVTMAHLVQ
VLLTSGTTTT AVGFIFYVQG FCAVAEGVKR AITPFLRCTA LFFNGLTGVP PPVEISSTAG
HSGALCSYLA LPSNLFQLFW EHRESVRPLL QRWCQDPAVT KAQKGEIQTV RYPRRRNHLI
DLPADYSSLL NQASHFKCPK SNDGERKHPT LCLVCGTMLC SQSTCCQSQL EGEDVGACTA
HAATCGAGVG VFLSIRECEI VLKASKTRGS TYPAPYLDDY GETDPQLVRG NPLHLCPERY
KKLHQLWQQH CVLEEIARSL EVDNVMFALE WQML
//
