ID A0A093QCD8_9PASS Unreviewed; 579 AA.
AC A0A093QCD8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=N305_13034 {ECO:0000313|EMBL:KFW86226.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW86226.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW86226.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW86226.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL672547; KFW86226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QCD8; -.
DR STRING; 328815.ENSMVIP00005021122; -.
DR Proteomes; UP000053258; 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; 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; PF14447; Prok-RING_4; 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:UP000053258};
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 187..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..178
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 187..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 579
FT /evidence="ECO:0000313|EMBL:KFW86226.1"
SQ SEQUENCE 579 AA; 64855 MW; 0B9E1F7A02EF07D0 CRC64;
MSTKSKAPLS LSDCLCQICM EIFVEPVTLP CSHTLCNSCF QLTVEKASLS CPFCRRRVSS
WARYNARRNT LVNWELWEKI QKNYPEECER RINGQDLDEE ICAPKPQHQL SKPGELRQEY
EAEISKVEAE RRVHEQEENK ASEEFIQRLL AEEEEEENRL AEQRRREMEK QLKQDEELAW
QLSNSLNEDS EGHVLSSPSP AHSLSPQTSP AHLCRAKNRP SNAGDIQKYL SPKHHGTLGP
ALFCSTTGRS RSSSGPVETK SNEGNCSALQ DEQEKMPTLS PQLTSVNKDS DAKDLFLESC
MNYFSASASG ETTTVNQEKT PGPNCLGDGV PGALHEATEG EGSGTALCRS KGKDDEIETN
SGSLTRCGLG KVAAHSDEKE AEGLQNTKET PKRKLLEAPA DAVTDSGVLD KRRRTCSEGV
EDEGVQMNDF SLQTQRAFEQ EFYERRRQEE QDRLLALQLQ KELDKEERTL NRQKGSPDEY
LLRTKPPQSL KDSAAKKGSS KVAKDSKGSK KQAETNHYKT RKGSCNENWQ SPTKVRVKSP
GIKEGKVLNC VVNTSDKNEI CSLPKNKQKT ILQMFKSPV
//
