TIAS_CALMQ
ID TIAS_CALMQ Reviewed; 407 AA.
AC A8MA77;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS {ECO:0000255|HAMAP-Rule:MF_01892};
DE Short=tRNA(Ile2)-agm2C synthetase {ECO:0000255|HAMAP-Rule:MF_01892};
DE EC=6.3.4.22 {ECO:0000255|HAMAP-Rule:MF_01892};
DE AltName: Full=tRNA(Ile2) agmatidine synthetase {ECO:0000255|HAMAP-Rule:MF_01892};
GN Name=tiaS {ECO:0000255|HAMAP-Rule:MF_01892}; OrderedLocusNames=Cmaq_0160;
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent agmatine transferase that catalyzes the
CC formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34)
CC of tRNA(Ile2), converting the codon specificity from AUG to AUA.
CC {ECO:0000255|HAMAP-Rule:MF_01892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-
CC agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H(+) + 2 phosphate;
CC Xref=Rhea:RHEA:43608, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10626,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58145, ChEBI:CHEBI:82748,
CC ChEBI:CHEBI:83545, ChEBI:CHEBI:456215; EC=6.3.4.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01892};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01892}.
CC -!- SIMILARITY: Belongs to the TiaS family. {ECO:0000255|HAMAP-
CC Rule:MF_01892}.
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DR EMBL; CP000852; ABW01009.1; -; Genomic_DNA.
DR RefSeq; WP_012185229.1; NC_009954.1.
DR AlphaFoldDB; A8MA77; -.
DR SMR; A8MA77; -.
DR STRING; 397948.Cmaq_0160; -.
DR EnsemblBacteria; ABW01009; ABW01009; Cmaq_0160.
DR GeneID; 5709670; -.
DR KEGG; cma:Cmaq_0160; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OMA; GMCTTYL; -.
DR OrthoDB; 58019at2157; -.
DR Proteomes; UP000001137; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01892; tRNA_Ile2_agm2C_synt; 1.
DR InterPro; IPR013696; DUF1743.
DR InterPro; IPR024913; tRNA_Ile2__agm2C_synt.
DR Pfam; PF08489; DUF1743; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..407
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407289"
SQ SEQUENCE 407 AA; 45402 MW; 1A32C627903579AF CRC64;
MITWVGIDDT DTYDKGCTTY VMYNMLKEFL KTKGEWRIIT YPRLIRLNPN VPFKTRGNAA
VSVGLNVDDP REALELAEWA VDAYSHKIGK TSPGIVVSIS NNEHWIYWKA LSDVIPLNAA
VKWMSKLGVI YRGGRGVIGA LASVMADLSQ DSTLELLAYS ESTPKPSIPI DLVKKLNDST
TPLTFENVSG DYVLIQPHGN DPVIFGIRGD SPYHIIHFAS MLINEVDVEP RWLIYLTNQA
TGHHLNSIMN KPYTTGYVEG SVNEVRLVQG GNIEIRVNST HVFSYRHYGF KSIDKATYLI
AYGGFKPGVN SLDLYMEGGV ALMLNNIVKN PRCPRCGSNL ESTGRVGLLK CPKCGLITGL
PRLMNYTSEF TLEEPREAEV RHLHKPTARI GLEGLVNVFN RPSLWII