UniProt: A0A0Q3Q479

Database: UniProt
Entry: A0A0Q3Q479_AMAAE

LinkDB:  A0A0Q3Q479_AMAAE 
Original site:  A0A0Q3Q479_AMAAE

All links

Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (2)   
   SMART (1)   
All databases (23)   

Download RDF

ID   A0A0Q3Q479_AMAAE        Unreviewed;       742 AA.
AC   A0A0Q3Q479;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN   ORFNames=AAES_64269 {ECO:0000313|EMBL:KQK83020.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK83020.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK83020.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK83020.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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         ECO:0000256|RuleBase:RU367105};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC   -!- SIMILARITY: Belongs to the Deltex family.
CC       {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK83020.1}.
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; LMAW01001658; KQK83020.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3Q479; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd09633; Deltex_C; 1.
DR   CDD; cd16506; RING-HC_DTX3-like; 1.
DR   Gene3D; 3.30.390.130; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039396; Deltex_C.
DR   InterPro; IPR039399; Deltex_C_sf.
DR   InterPro; IPR039398; Deltex_fam.
DR   InterPro; IPR048418; DTX3L_a/b_dom.
DR   InterPro; IPR048409; DTX3L_KH-like.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR   PANTHER; PTHR12622:SF41; E3 UBIQUITIN-PROTEIN LIGASE DTX3L; 1.
DR   Pfam; PF18102; DTC; 1.
DR   Pfam; PF21717; DTX3L_a-b; 1.
DR   Pfam; PF21718; DTX3L_KH-like; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367105};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          563..602
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          100..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  83780 MW;  82874F3D16521D58 CRC64;
     MAASPLLVRL CPAPDAGEKV LLKLYTYFQS VKRSGGGECE VRAGPVPNTY WVLFQQEQDR
     KSVESRTDHV VEIGARHLKI VIQPGEGDLS KSLFTKQAFD SCPTPSSSSP PPQLEQQAAK
     GRGDTTREVI TKKIFLTVSA TLNTSMFTEQ QRKRITIICP NLKREGHPDI DGSEKLTGDF
     ADIEKAYCYF KDILAGNYPN LVFSHSESKN GLKDENGLKT EEGNEFTVPS ALYEYFNHTC
     KEQIKELRER FGVCITSKDL YNGNTSVGFI SDRSSASIQQ ASDFFIRTFQ KNVENLRQEE
     LPVTNSHTLS EIIAKLNAKF SNLLAXEEGN QLLLCGPVRE ILAAKKFLTE EGENSQAEKN
     LKMSSELYKY RNGIEVDASL FMLLETILSK EIEDIKDKFD TTIEKRNVSC EQKMLIIFRP
     RIKTFDMSSH ATECFINAFQ SASAMLREKL ISLKLSEGQK ERLNMLLNGK QLEKLHVKLK
     KDKDKFMLIG LPNHLSNAEK YVMNFLPMED STQSKNRTPL TSDLSYQEDT GASEKKYDCR
     QKNNLFSEGQ AMETTEENDK DTCPICMEII DNKETLRKCK HAFCKNCIDQ AMTYKQACPI
     CNTFYGAMRG DQPEGRMSSR ILSSALPGYP SCGTIEITYK MRGGIQTGNH PNPGKHYSST
     FRKAYLPDNK EGQEILKLLR KAFNQKLIFT VGESRTTGAT DVITWNDIHH KTSMVGGPTN
     FGYPDPNYLH RVRLELKAKG IE
//

DBGET integrated database retrieval system