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Database: UniProt
Entry: A0A091VUI2_OPIHO
LinkDB: A0A091VUI2_OPIHO
Original site: A0A091VUI2_OPIHO 
ID   A0A091VUI2_OPIHO        Unreviewed;       932 AA.
AC   A0A091VUI2;
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=N306_04826 {ECO:0000313|EMBL:KFR06405.1};
OS   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR06405.1, ECO:0000313|Proteomes:UP000053605};
RN   [1] {ECO:0000313|EMBL:KFR06405.1, ECO:0000313|Proteomes:UP000053605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR06405.1};
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; KK734337; KFR06405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091VUI2; -.
DR   STRING; 30419.A0A091VUI2; -.
DR   PhylomeDB; A0A091VUI2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053605; 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; 3.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
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; 1.
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; 1.
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; 1.
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:UP000053605};
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..58
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          69..147
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   REPEAT          389..421
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          422..454
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          455..487
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          488..520
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          557..581
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          591..623
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          745..780
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          792..827
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          889..922
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFR06405.1"
FT   NON_TER         932
FT                   /evidence="ECO:0000313|EMBL:KFR06405.1"
SQ   SEQUENCE   932 AA;  102060 MW;  4D307BF2766D23ED CRC64;
     PTGIKHDGTM CDTCRQQPII GIRWKCAECT NYDLCTVCYH GDKHHLRHRF YRITTPGSER
     VLLESRRKSK KITARGIFAG ARVVRGVDWQ WEDQDGGNGR RGKVTEIQDW SASSPHSAAY
     VLWDNGAKNL YRVGFEGMSD LKCVQDAKGG SFYRDHCPVL GEQNGNRNPG GLQIGDLVNI
     DLDLEIVQSL QHGHGGWTDG MFETLTTTGT VCGIDEDHDI VVQYPSGNRW TFNPAVLTKA
     NVVRSGDAAQ GAEGGTSQFQ VGDLVQVCYD LERIKLLQRG HGEWAEAMLP TLGKVGRVQQ
     IYSDSDLKVE VCGTSWTYNP AAVSKVASAG SAISNASGER LSQLLKKLFE TQESGDLNEE
     LVKAAANGDV AKVEDLLKRP DVDVNGQCAG HTAMQAASQN GHVDILKLLL KQNVDVEAED
     KDGDRAVHHA AFGDEGAVIE VLHRGSADLN ARNKRRQTPL HIAVNKGHLQ VVKTLLDFGC
     HPSLQDSEGD TPLHDAISKK RDDILAVLLE AGADVTITNN NGFNALHHAA LRGNPSAMRV
     LLSKLPRPWI VDEKKDDGYT ALHLAALNNH VEVAELLVHQ GNANLDIQNV NQQTALHLAV
     ERQHTQIVRL LVRAGAKLDI QDKDGDTPLH EALRHHTLSQ LRQLQDMQDV GKVDTAWEPS
     KNTLIMGLGT QGAEKKSAAS IACFLAANGA DLSIRNKKGQ SPLDLCPDPS LCKALAKCHK
     EKVSGQVGSR SPSMINNDSE TLEECMVCSD MKRDTLFGPC GHIATCSLCS PRVKKCLICK
     EQVQSRTKIE ECVVCSDKKA AVLFQPCGHM CACENCASLM KKCVQCRAVV ERRVPFIMCC
     GGKGTEDTTD DISSGNIPVL QKDKDNTNVN ADVQKLQQQL QDIKEQTMCP VCLDRLKNMI
     FLCGHGTCQL CGDRMSECPI CRKAIERRIL LY
//
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