ID A0A2K6V6G6_SAIBB Unreviewed; 944 AA.
AC A0A2K6V6G6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MIB1 {ECO:0000313|Ensembl:ENSSBOP00000039742.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000039742.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000039742.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A2K6V6G6; -.
DR STRING; 39432.ENSSBOP00000039742; -.
DR Ensembl; ENSSBOT00000056704.1; ENSSBOP00000039742.1; ENSSBOG00000035880.1.
DR GeneTree; ENSGT00940000156781; -.
DR OMA; CCGGIGR; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
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:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd16724; RING-HC_MIB1_rpt1; 1.
DR CDD; cd16725; RING-HC_MIB1_rpt2; 1.
DR CDD; cd16727; RING-HC_MIB1_rpt3; 1.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042056; MIB1/2_ZZ.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202:SF53; E3 UBIQUITIN-PROTEIN LIGASE MIB1-RELATED; 1.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 1.
DR Pfam; PF13920; zf-C3HC4_3; 3.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 3.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 6..74
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 80..132
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 143..221
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 401..433
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 434..466
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 467..499
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 500..532
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 569..593
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 603..635
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 757..792
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 804..839
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 901..934
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 944 AA; 103353 MW; 0DAFA1C7FEB40985 CRC64;
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL
RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE
IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN
RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
GNTLGKVGRV QQIYSDSDLK VEVCGTSWTY NPAAVSKVAS AGSAISNASG ERLSQLLKKL
FETQESGDLN EELVKAAANG DVAKVEDLLK RPDVDVNGQC AGHTAMQAAS QNGHVDILKL
LLKQNVDVEA EDKDGDRAVH HAAFGDEGAV IEVLHRGSAD LNARNKRRQT PLHIAVNKGH
LQVVKTLLDF GCHPSLQDSE GDTPLHDAIS KKRDDILAVL LEAGADVTIT NNNGFNALHH
AALRGNPSAM RVLLSKLPRP WIVDEKKDDG YTALHLAALN NHVEVAELLV HQGNANLDIQ
NVNQQTALHL AVERQHTQIV RLLVRAGAKL DIQDKDGDTP LHEALRHHTL SQLRQLQDMQ
DVGKVDAAWE PSKNTLIMGL GTQGAEKKSA ASIACFLAAN GADLSIRNKK GQSPLDLCPD
PNLCKALAKC HKEKVSGQVG SRSPSMISND SETLEECMVC SDMKRDTLFG PCGHIATCSL
CSPRVKKCLI CKEQVQSRTK IEECVVCSDK KAAVLFQPCG HMCACENCAN LMKKCVQCRA
VVERRVPFIM CCGGKSSEDA TDDISSGNIP VLQKDKDNTN VNADVQKLQQ QLQDIKEQTM
CPVCLDRLKN MIFLCGHGTC QLCGDRMSEC PICRKAIERR ILLY
//
