ID A0A093I487_STRCA Unreviewed; 595 AA.
AC A0A093I487;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-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};
GN ORFNames=N308_04726 {ECO:0000313|EMBL:KFV86660.1};
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:KFV86660.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV86660.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV86660.1};
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNF12 family.
CC {ECO:0000256|ARBA:ARBA00038418}.
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DR EMBL; KL206889; KFV86660.1; -; Genomic_DNA.
DR RefSeq; XP_009683730.1; XM_009685435.1.
DR AlphaFoldDB; A0A093I487; -.
DR STRING; 441894.ENSSCUP00000025211; -.
DR Ensembl; ENSSCUT00000033431; ENSSCUP00000025211; ENSSCUG00000018484.
DR GeneID; 104150919; -.
DR KEGG; scam:104150919; -.
DR CTD; 51132; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd16674; RING-H2_RNF12; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45931:SF4; E3 UBIQUITIN-PROTEIN LIGASE RLIM; 1.
DR PANTHER; PTHR45931; SI:CH211-59O9.10; 1.
DR Pfam; PF13639; zf-RING_2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
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:PRU00175}.
FT DOMAIN 541..582
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65976 MW; 1897D1BE7FAC08A2 CRC64;
MESSDSSDKG NIDQSEAQRQ SQLDRLDREE AFYQFVNNLS EEDYRLMRDN NLLGTPGEIT
EEELLRRLHQ VKEGPPQQNS DENRGAESAE DVSNGDSIID WLNSVRQTGN TTRSGQRGNQ
SWRAVSRTNP NSGDFRFSLE INVNRNNGNT NPETENEPSV EPSSGEDLEN SQSDSEIPRS
ESPSVRQPGS ERSASEELTT EEASPPRGQR RARSRSPEQR RTRARTDRSR SPINPVSETP
RRAHHNTSSQ TLDHSSVNEA EGSSRTRQHV TLRQHTVGTE MPSENAVLFS TPETRPVPQA
TGSSETNGSS ESATPGQRPP TIVLDLQVRR VRPGEYRQRD SIANRTRSRS QTPNNTVTYE
SERGGFRRTF SRSERAGVRT YVSTIRIPIR RILNTGLSET TSVAIQTMLR QIMTGFGELS
YFMYSDSDAD PSGPAPNQNV DASEPQNGGG GSSSNESTDA SSGEVYEGGN EGGSTSGARR
EGRNTRGSVT FEESGSLPFL SLAQFFLLNE DDDDQPRGLT KEQIDNLAMR NFGESDALKT
CSVCITEYTE GNKLRKLPCS HEYHVHCIDR WLSENSTCPI CRRAVLASGN RESVV
//
