ID A0A091FUC9_CORBR Unreviewed; 959 AA.
AC A0A091FUC9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=N302_14283 {ECO:0000313|EMBL:KFO64830.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO64830.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO64830.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO64830.1};
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; KK719670; KFO64830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FUC9; -.
DR STRING; 85066.A0A091FUC9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000052976; 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; cd16726; RING-HC_MIB2_rpt1; 1.
DR CDD; cd16728; RING-HC_MIB2_rpt2; 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; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00184; RING; 2.
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; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
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:UP000052976};
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..80
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 149..227
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 480..512
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 513..545
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 636..660
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 670..702
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 915..948
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 959 AA; 106780 MW; 24DD2C4D56CC17AD CRC64;
MDLDPHASMQ VGMRVVRGVD WKWGSQDSGE GNVGTVVEIG RTGSPTTPDK TVVVQWDQGN
RTNYRTGFQG AYDLLLYDNA QIGVRHPNII CDCCKKHGIR GMRWKCKMCF DYDLCTQCYM
NNKHDLSHSF ERYETAHSQP VLVSPRQNLT RITLKGTFQG AKVVRGPDWE WGNQDGGEGK
TGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LKCTVEASGG FYYKEHLPKL
GKPAELQRKE STDRHPFQHG DKVKCLLDID ILREMQEGHG GWNPKMAEFI GQTGTVHRIT
DRGDVRVQFN SETRWTFHPG ALTKLNTFWV GDVVRVIDDM ETVKRFQPGH GEWTDEMAPT
LGHIGKVIKV YGDGDLRVSV GGQSWTFNPA CLTAYQREEE ANLMTTESAK ESKSTLVTVL
EKLLSQRTES EHAGCLVICA ALNNAAKVRE LLQKYPDKAR QGHPLFSVSL PFPKVDAKNQ
GRTALQIASY QGHLEVVKTL LQAHANVNLR DDEGDTALHY AAFGNQAEVA RVLLAKGATL
YVAVSQGFTE VVRALCELNC DVNLPDSQGD TPLHYAITLD YKVVIEILTE VPNIDFTVQN
CQGFNLLHYS ALKGNKLAIK KILARARQLV DSKKEDGFTA LHLAALNNHM EVAEILIKEG
RCDVNLKNNR NQSPLHLAVI QGHVGMVQLL VSQGSDVNAE DEDGDTAMHI ALERQQLMAL
AMEKREGDMG ASLLSKLQAS GFLGNVELNV GTAIACYLAQ EGADINYANH RGKSPLDLIT
DGRIIQIVKD FSQKFRERQV SSESSTITCS LRRVHTTPNT MTNLSVSSVA VPTECLVCSE
LALLIHFFPC QHSIVCEECS RRMKKCIKCQ VTITKKLKQD STEVECSPSS ESTEQRKLME
ELQSRYRQME ERITCPICID DQIKLVFQCG HGSCPDCSSA LTVCPICRQA IRERIQIFV
//
