ID A0A0L8IE30_OCTBM Unreviewed; 1798 AA.
AC A0A0L8IE30;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=OCBIM_22012133mg {ECO:0000313|EMBL:KOF99748.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF99748.1};
RN [1] {ECO:0000313|EMBL:KOF99748.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF99748.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF99748.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; KQ415902; KOF99748.1; -; Genomic_DNA.
DR RefSeq; XP_014773171.1; XM_014917685.1.
DR STRING; 37653.A0A0L8IE30; -.
DR EnsemblMetazoa; Ocbimv22012133m; Ocbimv22012133m.p; Ocbimv22012133m.g.
DR EnsemblMetazoa; XM_014917685.1; XP_014773171.1; LOC106871298.
DR OMA; ICNCTTA; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
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; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 80..151
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 80..151
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1007..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1798 AA; 205236 MW; B4C01CFB2B7BA3EB CRC64;
MAGVSPELAS LMKKGKSAIA AHFKTAFAED KLLNELLNTV FNPEKAIDDY ENLEWYRFLI
AGGKKFDDYA NLVRIYDNAT TCGLVWTANF VAYRCRTCGI TPCMSLCSKC FQAGNHEGHD
YNMFRSKAGG ACDCGDASVM NPAGFCSRHL PGPNRYQLVP PREVMALPEL VMPRLFIRLI
YHLREFAKVE AADISQIAMQ DADSYLTFLH SLCEMGAVMM KQMGKTLTDS VIYEKFTQSE
GCYHSESQKN YLQAVKEMTY PPSFDIFSNK IYLDQKLVHT TILDELVFWM VKLELPQKIV
TLLLSLLPDD HYKQAFTKAF VQHYSRVSLV VVKSKDHYAV AHRVVHISVQ LFSNETLART
MCKDYNLLYI LVFSLRHMVE SVFMQSTLQN NFNNYHNVVD CDSKAMKDHC YWPIVSDLIN
LLSHHTIALQ FMENVNLVNT WLCLLVYFQG CNLNERELTQ HVEFEPDTYY AAFSAELEIS
ASPMSYLISH CKDSKTAHCT KAIVAACLET LEDWFESINF DANKGDKTSY LQLAFHLPLH
RYLAVFLAYA VQHQAVPITQ MLPFYSKLKN LLMFPLRIQA GIAEINANLW LRNGLQIKGQ
AMTYVQCHFC YSMLDADLYL IQVCAAHLPP NEFVRIVIES FHLTNWLLLC PKPIKIGCVL
ESEQELALVE SALSFLAMLQ SVRTYLGLSE KELVRVEMVA LLCVNDRTHS QLMDSMPEKS
GLAVHEKYYF ESTLKTVADY KAPVLESGGG LQQGTYVPKG FLWDQEFDPI QVSTRAVYKR
DIQSAMDRYH AYLKQTGKYT GKSPPWPPIK IPGKILPAYD GLRRMLHCRT LHGFIFSVLY
KAMKETHISE TILYFCVFLL ELGTRFPATE IQEYRCKKQV KDGDYENWFP TDCLQTNAAH
RIQEILISDS PNPEKDHSPS MSFVANIFSK DFGAASKLFT TTNPNCSNSS NNLEDEASGQ
MHVNCDSKDE VEEKDDNCRR VIVKESLISL LMKLHCKLSA KKQPSYMPTS MRKCSERPSA
EPSNPSVNCG DGPYYIGLLL DRLASQDYSC LQETERIYHE TKPKVREKQQ PQERGTATSE
DLEKEERRKK ARERRQKLMA EFASKQKAFM EQAMDMDDIG EDVQDNGEQS VLEDGFHCAI
CSQTMPSTSE RPFGIVVLLL STSVLGHCPS QEQRRHLPVG KLKFKSVPLS CADIRKQHLN
LLMKYYSETP VSKSANIGWE GGVLVQSCGH YLHLDCHKQY LESLKGPYLQ QTLAVNDGEY
WCPVCRQLAN AVIPIIPNDR KPTPIPAPTD SNNLQKMAQD IEQLLQQQPQ VNLFLAQKCS
LIDELTSATH PMYRKYCEDS SANIWLFTCS IVRTNLELEL LGYGGQLFTR ESPSSKPKVF
MPLFRMLSYT CKTLPPVPQT DLWKLITGVA VIGDSSSSFS NVPGQVPILL RDPVALLLNF
LLQLPEVSKQ HFSYVVNSLY NMAYIQALVV TSLKLTSNER VAWCKKRMSD SLQEVSGMMS
HVITRLQLSQ LYDEKDQQLG CISQWIWSPD SVESVLQSYL LPYLRIAALL QRHLFDEEFP
QKKCPSEFTY LCRYLMLGGK SCDSQPSASV DTQSGLSIPR KVEETQRTEH FVRFCVPEIL
PITRFWLQEL ATAIDGPPSL KSQYLLPSSF FFHPPRLVEL PDQYYKIFQE YRNKTCMICN
KIPRDPTICL ICAEFLCFRE ACCEHESVRE CVQHSITCGA GTGVFLLVNS SIVVVIRGQR
AALWGSVYLD KHGEEDEELR RGKPLYLSEE RYQLLEQQWR THNFDHACKQ WIWHKNNL
//
