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Database: UniProt
Entry: A0A091G9S4_9AVES
LinkDB: A0A091G9S4_9AVES
Original site: A0A091G9S4_9AVES 
ID   A0A091G9S4_9AVES        Unreviewed;       994 AA.
AC   A0A091G9S4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=N303_04712 {ECO:0000313|EMBL:KFO77904.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO77904.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO77904.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO77904.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL447842; KFO77904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091G9S4; -.
DR   STRING; 55661.A0A091G9S4; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
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   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; 2.
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; 2.
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:UP000053760};
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          1..62
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   DOMAIN          68..120
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          131..209
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   REPEAT          451..483
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          484..516
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          517..549
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          550..582
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          619..643
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          653..685
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          807..842
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          854..889
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          951..984
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO77904.1"
FT   NON_TER         994
FT                   /evidence="ECO:0000313|EMBL:KFO77904.1"
SQ   SEQUENCE   994 AA;  108754 MW;  B18FAFBCB4B8B6BC CRC64;
     GVGGRVVRGP DWKWGKQDGG EGHVGTVRTQ LRPEEVVVVW DNGTAANYRC SGAYDLRILD
     SAPTGIKHDG TMCDTCRQQP IIGIRWKCAE CTNYDLCTVC YHGDKHHLRH RFYRITTPGS
     ERVLLESRRK SKKITARGIF AGARVVRGVD WQWEDQDGGN GRRGKVTEIQ DWSASSPHSA
     AYVLWDNGAK NLYRVGFEGM SDLKCVQDAK GGSFYRDHCP VLGEQNGNRN PGGLQIGDLV
     NIDLDLEIVQ SLQHGHGGWT DGMFETLTTT GTVCGIDEDH DIVVQYPSGN RWTFNPAVLT
     KANVVRSGDA AQGAEGGTSQ FQVGDLVQVC YDLERIKLLQ RGHGEWAEAM LPTLGKVGRV
     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 DVGKVDTAWE
     PSKNTLIMGL GTQGAEKKSA ASIACFLAAN GADLSIRNKK GQSPLDLCPD PSLCKALAKC
     HKEKVSGQVG SRSPSMINND SETLEECMVC SDMKRDTLFG PCGHIATCSL CSPRVKKCLI
     CKEQVQSRTK IEECVVCSDK KAAVLFQPCG HMCACENCAS LMKKCVQCRA VVERRVPFIM
     CCGGKGTEDT TDDISSGNIP VLQKDKDNTN VNADVQKLQQ QLQDIKEQTM CPVCLDRLKN
     MIFLCGHGTC QLCGDRMSEC PICRKAIERR ILLY
//
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