ID Q1YDX4_MOBAS Unreviewed; 367 AA. AC Q1YDX4; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 40. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase; DE EC=2.3.1.-; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD; GN Name=tsaD; ORFNames=SI859A1_03651; OS Manganese-oxidizing bacterium (strain SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1; RX PubMed=18344346; DOI=10.1128/AEM.01656-07; RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., RA Bernier-Latmani R., McCarthy J.K., Torpey J.W., Clement B.G., RA Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine RT alphaproteobacterium Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37, together with TsaE and TsaB. TsaD likely plays a CC direct catalytic role in this reaction (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; AAPJ01000010; EAS48484.1; -; Genomic_DNA. DR ProteinModelPortal; Q1YDX4; -. DR MEROPS; M22.001; -. DR EnsemblBacteria; EAS48484; EAS48484; SI859A1_03651. DR PATRIC; 24565153; VBIAurMan112117_0733. DR BioCyc; AURANTIMONAS:SI859A1_03651-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-HAMAP. DR GO; GO:0070526; P:threonylcarbamoyladenosine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/YgjD. DR InterPro; IPR022450; TsaD. DR Pfam; PF00814; Peptidase_M22; 1. DR PRINTS; PR00789; OSIALOPTASE. DR TIGRFAMs; TIGR00329; gcp_kae1; 1. DR TIGRFAMs; TIGR03723; T6A_YgjD; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Iron; Metal-binding; Transferase; KW tRNA processing. FT REGION 145 149 Substrate binding (By similarity). FT METAL 123 123 Iron (By similarity). FT METAL 127 127 Iron (By similarity). FT METAL 319 319 Iron (By similarity). FT BINDING 178 178 Substrate (By similarity). FT BINDING 191 191 Substrate; via amide nitrogen (By FT similarity). FT BINDING 195 195 Substrate (By similarity). FT BINDING 291 291 Substrate (By similarity). SQ SEQUENCE 367 AA; 37990 MW; 110BFAFE5862144F CRC64; MTPANPPRPL ILGIETSCDE TAASVVGRDD AGAPVIHSNV VLSQVEEHAA FGGVVPEIAA RAHVEALDGI VKAAMDEAGI GFDELSAVAA TTGPGLVGGL IVGAMTGKAI AAARRLPFLA INHLEGHALT PRLTDRLAYP YLLLLVSGGH SQIVLVRGLG AYERWGTTID DALGEAFDKT AKLLGLPNPG GPHVERRAAA GDPKRFALPR PMKGNPRLDF SFSGLKTALR MAAQAAAPLS PTDVDDLCAG FQAAAADSLA DRVGRALTQF RDRFPDLADP VLAVAGGVAA NRAIRTALEA QTARTGVRLV APPLALCTDN AAMIAYAGLE RFEAGMVDGL DAPVRSRWPL DGDSAPMIGF GRRGAKA //