ID A0A093H305_STRCA Unreviewed; 576 AA.
AC A0A093H305;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=N308_04958 {ECO:0000313|EMBL:KFV76953.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV76953.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV76953.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV76953.1};
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};
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DR EMBL; KL205920; KFV76953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H305; -.
DR STRING; 441894.ENSSCUP00000006157; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd21952; MIU2_RNF168; 1.
DR CDD; cd16550; RING-HC_RNF168; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_03066; RNF168; 1.
DR InterPro; IPR034725; RNF168.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23328:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF168; 1.
DR PANTHER; PTHR23328; UNCHARACTERIZED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 16..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 222..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 372..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 576
FT /evidence="ECO:0000313|EMBL:KFV76953.1"
SQ SEQUENCE 576 AA; 65471 MW; 0B40A728173128F7 CRC64;
MAKKSEAPLS LADCLCQICM EIFVEPVTLP CSHTLCNSCF QLTVEKASLC CPFCRRRVSS
WARYNTRRNT LINWELWEKI QKNYPKECER RINGQDLEDE ICVSQPQHQL SKPGELRQEY
EAEISKVEAE RRAHEQEENK ASEEYIQRLL AEEEEEHRLA DERRKEMEKQ LKQDEELAWQ
LSNSLLFLLL KNEDARGNRL NSPSPAGTLS SETSPVNLCK MKNRSSSSGD IQKYLSSKSH
PMLGSTSLSR TTERGRTDSC SVESNSNESS NSVWQDEQEE MPTLSPQLTS VIKDCSANDS
FLESCMNYLS ASASVEFTTV KQEKIPGPNC AGDEVPYAIC GIAKGEGSRT VLPRLKGEAD
GIELDSGSLT HAAGKPDEEK LENPKETPKR KLGEPLAEAV VDLGLLDKRR RTFPETSEDQ
GEQINDFNVQ MQKAFEQEFY ERRMQEEQDR LLALQLQRQI NKEERTLNRR KGSPDEYHLR
TKPPQTAKDS PTRKGSSKVV KDSKLPKKQA ETNHRKIRKG SCNENWQSPT RVRMKSPSIK
GGKILNCVVN TSDSNDICSL PKNKQKTILQ MFKRSV
//
