GenomeNet

Database: UniProt
Entry: A0A099ZE14_TINGU
LinkDB: A0A099ZE14_TINGU
Original site: A0A099ZE14_TINGU 
ID   A0A099ZE14_TINGU        Unreviewed;       273 AA.
AC   A0A099ZE14;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=N309_12324 {ECO:0000313|EMBL:KGL80011.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL80011.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL80011.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL80011.1};
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL892746; KGL80011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099ZE14; -.
DR   STRING; 94827.A0A099ZE14; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16740; RING-HC_RING2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR043540; RING1/RING2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076:SF2; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR   PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          25..65
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL80011.1"
FT   NON_TER         273
FT                   /evidence="ECO:0000313|EMBL:KGL80011.1"
SQ   SEQUENCE   273 AA;  29748 MW;  B5D981C51CF6DEAC CRC64;
     SPQEAIMDGT EIAVSPRSLH SELMCPICLD MLKNTMTTKE CLHRFCSDCI VTALRSGNKE
     CPTCRKKLVS KRSLRPDPNF DALISKIYPS RDEYEAHQDR VLAKLSRLHN QQALSSSIEE
     GLKMQAMHRP GEGLGVSPCP QRGTGVLGMN GRWHLGMVGS HCGGRVLHPC RHGGWVGLPP
     CRHGGQVLLQ PCCHGGRVLL PPLPSWWTGS STLSSWYVKT TANATVDHLS KYLALRIALE
     EAPAPGPDAA GLEDVSEKQY TIYITTAAGA FTV
//
DBGET integrated database retrieval system