DTD1_HUMAN
ID DTD1_HUMAN Reviewed; 209 AA.
AC Q8TEA8; A8K5X5; D3DW37; Q496D1; Q5W184; Q8WXU8; Q9BW67; Q9H464; Q9H474;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
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 {ECO:0000303|PubMed:15653697};
DE Short=DUE-B {ECO:0000303|PubMed:15653697};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
DE AltName: Full=Histidyl-tRNA synthase-related;
GN Name=DTD1; Synonyms=C20orf88, DUEB, HARS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12392168; DOI=10.1023/a:1020256718720;
RA Meng X.X., Chen J.J., Yang Q.Q., Wang S., Chao Y., Ying K., Xie Y., Mao Y.;
RT "Cloning and identification of a novel cDNA which may be associated with
RT FKBP25.";
RL Biochem. Genet. 40:303-310(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, PHOSPHORYLATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15653697; DOI=10.1074/jbc.m404754200;
RA Casper J.M., Kemp M.G., Ghosh M., Randall G.M., Vaillant A., Leffak M.;
RT "The c-myc DNA-unwinding element-binding protein modulates the assembly of
RT DNA replication complexes in vitro.";
RL J. Biol. Chem. 280:13071-13083(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH CDC45
RP AND TOPBP1.
RX PubMed=20065034; DOI=10.1128/mcb.00710-09;
RA Chowdhury A., Liu G., Kemp M., Chen X., Katrangi N., Myers S., Ghosh M.,
RA Yao J., Gao Y., Bubulya P., Leffak M.;
RT "The DNA unwinding element binding protein DUE-B interacts with Cdc45 in
RT preinitiation complex formation.";
RL Mol. Cell. Biol. 30:1495-1507(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND MAGNESIUM-BINDING
RP SITES.
RX PubMed=17264083; DOI=10.1074/jbc.m609632200;
RA Kemp M., Bae B., Yu J.P., Ghosh M., Leffak M., Nair S.K.;
RT "Structure and function of the c-myc DNA-unwinding element-binding protein
RT DUE-B.";
RL J. Biol. Chem. 282:10441-10448(2007).
CC -!- FUNCTION: Possible ATPase (PubMed:15653697) involved in DNA
CC replication, may facilitate loading of CDC45 onto pre-replication
CC complexes (PubMed:20065034). {ECO:0000269|PubMed:15653697,
CC ECO:0000269|PubMed:20065034}.
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 -!- 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 (PubMed15653697). Interacts with CDC45 and TOPBP1
CC (PubMed:20065034). {ECO:0000269|PubMed:15653697,
CC ECO:0000269|PubMed:17264083, ECO:0000269|PubMed:20065034}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15653697,
CC ECO:0000269|PubMed:20065034}. Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}.
CC Note=Associated with chromatin at some replication origins containing
CC functional DNA-unwinding elements (PubMed:20065034).
CC -!- TISSUE SPECIFICITY: Expressed in many adult and fetal tissues. Highest
CC levels in testis, ovary, spleen and in adult and fetal brain.
CC {ECO:0000269|PubMed:12392168}.
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 (PubMed:15653697). Phosphorylation in the C-terminus weakens the
CC interaction with CDC45 (PubMed:20065034). {ECO:0000269|PubMed:15653697,
CC ECO:0000269|PubMed:20065034}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85044.1; Type=Miscellaneous discrepancy; Note=Presence of Alu-repeat DNA.; Evidence={ECO:0000305};
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DR EMBL; AF332356; AAL57046.1; -; mRNA.
DR EMBL; AK074304; BAB85044.1; ALT_SEQ; mRNA.
DR EMBL; AK291440; BAF84129.1; -; mRNA.
DR EMBL; AL121900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10227.1; -; Genomic_DNA.
DR EMBL; BC000599; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471133; EAX10228.1; -; Genomic_DNA.
DR EMBL; BC045167; AAH45167.1; -; mRNA.
DR EMBL; BC100923; AAI00924.1; -; mRNA.
DR EMBL; BC100924; AAI00925.1; -; mRNA.
DR EMBL; BC100925; AAI00926.1; -; mRNA.
DR CCDS; CCDS13138.1; -.
DR RefSeq; NP_001304972.1; NM_001318043.1.
DR RefSeq; NP_543010.3; NM_080820.5.
DR PDB; 2OKV; X-ray; 2.00 A; A/B/C/D=1-209.
DR PDBsum; 2OKV; -.
DR AlphaFoldDB; Q8TEA8; -.
DR SMR; Q8TEA8; -.
DR BioGRID; 124965; 24.
DR IntAct; Q8TEA8; 5.
DR MINT; Q8TEA8; -.
DR STRING; 9606.ENSP00000366672; -.
DR iPTMnet; Q8TEA8; -.
DR PhosphoSitePlus; Q8TEA8; -.
DR BioMuta; DTD1; -.
DR DMDM; 29427856; -.
DR EPD; Q8TEA8; -.
DR jPOST; Q8TEA8; -.
DR MassIVE; Q8TEA8; -.
DR MaxQB; Q8TEA8; -.
DR PaxDb; Q8TEA8; -.
DR PeptideAtlas; Q8TEA8; -.
DR PRIDE; Q8TEA8; -.
DR ProteomicsDB; 74433; -.
DR Antibodypedia; 42815; 121 antibodies from 20 providers.
DR DNASU; 92675; -.
DR Ensembl; ENST00000377452.4; ENSP00000366672.4; ENSG00000125821.13.
DR GeneID; 92675; -.
DR KEGG; hsa:92675; -.
DR MANE-Select; ENST00000377452.4; ENSP00000366672.4; NM_080820.6; NP_543010.3.
DR UCSC; uc002wrf.5; human.
DR CTD; 92675; -.
DR DisGeNET; 92675; -.
DR GeneCards; DTD1; -.
DR HGNC; HGNC:16219; DTD1.
DR HPA; ENSG00000125821; Low tissue specificity.
DR MIM; 610996; gene.
DR neXtProt; NX_Q8TEA8; -.
DR OpenTargets; ENSG00000125821; -.
DR PharmGKB; PA162384107; -.
DR VEuPathDB; HostDB:ENSG00000125821; -.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076901_0_0_1; -.
DR InParanoid; Q8TEA8; -.
DR OMA; HASIRPR; -.
DR OrthoDB; 1411453at2759; -.
DR PhylomeDB; Q8TEA8; -.
DR TreeFam; TF314886; -.
DR PathwayCommons; Q8TEA8; -.
DR SignaLink; Q8TEA8; -.
DR BioGRID-ORCS; 92675; 20 hits in 1084 CRISPR screens.
DR ChiTaRS; DTD1; human.
DR EvolutionaryTrace; Q8TEA8; -.
DR GenomeRNAi; 92675; -.
DR Pharos; Q8TEA8; Tbio.
DR PRO; PR:Q8TEA8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TEA8; protein.
DR Bgee; ENSG00000125821; Expressed in gingival epithelium and 193 other tissues.
DR ExpressionAtlas; Q8TEA8; baseline and differential.
DR Genevisible; Q8TEA8; HS.
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 DisProt; DP02452; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA replication; DNA-binding; Hydrolase;
KW Magnesium; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..209
FT /note="D-aminoacyl-tRNA deacylase 1"
FT /id="PRO_0000164626"
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:0000269|PubMed:17264083"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17264083"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17264083"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DD18"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT CONFLICT 94
FT /note="H -> N (in Ref. 5; AAH45167)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="H -> R (in Ref. 1; AAL57046)"
FT /evidence="ECO:0000305"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:2OKV"
FT STRAND 18..32
FT /evidence="ECO:0007829|PDB:2OKV"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2OKV"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2OKV"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2OKV"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2OKV"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2OKV"
FT HELIX 99..116
FT /evidence="ECO:0007829|PDB:2OKV"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2OKV"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2OKV"
FT STRAND 131..146
FT /evidence="ECO:0007829|PDB:2OKV"
SQ SEQUENCE 209 AA; 23424 MW; F006ED14974ACC92 CRC64;
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL NLRVFEDESG
KHWSKSVMDK QYEILCVSQF TLQCVLKGNK PDFHLAMPTE QAEGFYNSFL EQLRKTYRPE
LIKDGKFGAY MQVHIQNDGP VTIELESPAP GTATSDPKQL SKLEKQQQRK EKTRAKGPSE
SSKERNTPRK EDRSASSGAE GDVSSEREP
