DTD1_BOVIN
ID DTD1_BOVIN Reviewed; 209 AA.
AC Q2T9V8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=D-aminoacyl-tRNA deacylase 1 {ECO:0000250|UniProtKB:Q8IIS0};
DE Short=DTD;
DE EC=3.1.1.96 {ECO:0000250|UniProtKB:Q8IIS0};
DE AltName: Full=DNA-unwinding element-binding protein B;
DE Short=DUE-B;
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
GN Name=DTD1; Synonyms=HARS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala),
CC protecting cells against glycine mischarging by AlaRS. Acts via tRNA-
CC based rather than protein-based catalysis; rejects L-amino acids rather
CC than detecting D-amino acids in the active site. By recycling D-
CC aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC counteracts the toxicity associated with the formation of D-aminoacyl-
CC tRNA entities in vivo and helps enforce protein L-homochirality.
CC {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- FUNCTION: ATPase involved in DNA replication, may facilitate loading of
CC CDC45 onto pre-replication complexes. {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- SUBUNIT: Homodimer. Interacts with CDC45 and TOPBP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TEA8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IIS0}. Note=Associated with chromatin at some
CC replication origins containing functional DNA-unwinding elements (By
CC similarity). {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of L-amino
CC acids. {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- PTM: Preferentially phosphorylated in cells arrested early in S phase.
CC Phosphorylation in the C-terminus weakens the interaction with CDC45
CC (By similarity). {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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DR EMBL; BC111244; AAI11245.1; -; mRNA.
DR RefSeq; NP_001033193.1; NM_001038104.2.
DR RefSeq; XP_010809535.1; XM_010811233.2.
DR AlphaFoldDB; Q2T9V8; -.
DR SMR; Q2T9V8; -.
DR STRING; 9913.ENSBTAP00000011800; -.
DR PaxDb; Q2T9V8; -.
DR PRIDE; Q2T9V8; -.
DR Ensembl; ENSBTAT00000011800; ENSBTAP00000011800; ENSBTAG00000008964.
DR GeneID; 514493; -.
DR KEGG; bta:514493; -.
DR CTD; 92675; -.
DR VEuPathDB; HostDB:ENSBTAG00000008964; -.
DR VGNC; VGNC:28228; DTD1.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076901_0_0_1; -.
DR InParanoid; Q2T9V8; -.
DR OMA; GVFQAHM; -.
DR OrthoDB; 1411453at2759; -.
DR TreeFam; TF314886; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000008964; Expressed in myometrium and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
DR CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; -; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA replication; DNA-binding; Hydrolase; Magnesium;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..209
FT /note="D-aminoacyl-tRNA deacylase 1"
FT /id="PRO_0000245032"
FT REGION 142..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 139..140
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q8IIS0"
FT COMPBIAS 162..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8TEA8"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8TEA8"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEA8"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DD18"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEA8"
SQ SEQUENCE 209 AA; 23232 MW; 1552D655B30E8218 CRC64;
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL NLRVFEDESG
KHWSKSVMDK QYEVLCVSQF TLQCVLKGNK PDFHLAMPAE QAESFYKGFL EQLRKAYRPE
LVKDGKFGAY MQVHIQNDGP VTIELESPAP GAAASDPKQL SKLEKQQQRK EKTRAKGPSE
SSKERSAPRK EDRSASSGAE GDVSSEREP
