ID A0A0L8H3M3_OCTBM Unreviewed; 587 AA.
AC A0A0L8H3M3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN ORFNames=OCBIM_22023096mg {ECO:0000313|EMBL:KOF83883.1};
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:KOF83883.1};
RN [1] {ECO:0000313|EMBL:KOF83883.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF83883.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF83883.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KQ419348; KOF83883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8H3M3; -.
DR STRING; 37653.A0A0L8H3M3; -.
DR EnsemblMetazoa; Ocbimv22023096m; Ocbimv22023096m.p; Ocbimv22023096m.g.
DR EnsemblMetazoa; XM_014920183.1; XP_014775669.1; LOC106872992.
DR OMA; NVAWASS; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51416; MIB_HERC2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 4..56
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 67..145
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 384..416
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 417..449
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 450..482
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOF83883.1"
SQ SEQUENCE 587 AA; 65909 MW; 8B112EE2C7A048FC CRC64;
GVKHTSIICD SCNKSAIQGM RWRCLTCHDF DLCTVCYHGD KHDIKHSFLR FDTPASKGVK
MPKRASSTKM EAWGIFKGAK VLRGNDWDWG NQDGGEGKPG KVRDIRGWDL ESGRSVANVV
WSNSQMNVYR VGHKGKVDLK ATQCASGGMF YVDHLPVLGE FTETSASGEP TCHFKVGDRV
RVDLDMEILK VMQEGHGGWN PRMAEYIGQV GSVHRITDRG DVRVQYEGCS NRWTFHPGAL
TKVQLFAIGD SVQIIEDIRK VKEYQKGHGE WTDSMASALG KIGKVKQVYP DGDLLVAVSG
KKWTYNPLCC AVAPNSPLEV NNIHSMSDRE EDPASLTELL EQLLNMSHKD TRLDQFVREA
AQGQIENIRE VITKHPDKID QRSSGKTALQ VASHQGHKDI VLMLLEAGAN LELQDEDGDT
ALHYSAFGNQ PEVMELLLLK GANINAFNKG GCSTLHVAVN KQFVKCVRVL LKHSTPVNIQ
HYICSGAKLW PPLRKYNLRM RKGLAFPEAL RVHMRSFCLL ALRRLRRRGF QLIRSTEQPA
REINVLVAEH STDTCTLNVV LGDIQRDTEC NKADPLNYKH NRDRKYE
//
