ID   TIAS_STAMF              Reviewed;         459 AA.
AC   A3DP93;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=Smar_1362;
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
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; CP000575; ABN70453.1; -; Genomic_DNA.
DR   RefSeq; WP_011839647.1; NC_009033.1.
DR   AlphaFoldDB; A3DP93; -.
DR   SMR; A3DP93; -.
DR   STRING; 399550.Smar_1362; -.
DR   EnsemblBacteria; ABN70453; ABN70453; Smar_1362.
DR   GeneID; 4908093; -.
DR   KEGG; smr:Smar_1362; -.
DR   eggNOG; arCOG01115; Archaea.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   OMA; GMCTTYL; -.
DR   OrthoDB; 58019at2157; -.
DR   Proteomes; UP000000254; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR024913; tRNA_Ile2__agm2C_synt.
DR   Pfam; PF08489; DUF1743; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..459
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407301"
FT   DNA_BIND        282..360
FT                   /note="OB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01892"
SQ   SEQUENCE   459 AA;  53401 MW;  67E4EA753ACC72DE CRC64;
     MKETIVHMGF DDIDTPFGGC TTHFVASILV KWVKDRRIKL IDYPNLIRLN PGVPWKTRGN
     GAVVLRFKVK NYDEAIKLLE EAYDEALEYL GKYHHPQHHP VIGMYIGGLS ERIKWIGWKA
     VHDLIPLDLM HRVLEKEKNK IIYKLLRKDK KRGLIGVFSA IGYRMTNTDY TYELIAYRSE
     EYIDKPRQVN AESVKYMDKV FHNDTILNYD YETNRPLITP HGGDPVLLGI RGEYPDVLIK
     AYNMVKINEP VPIRLIYRTN QHTDAHLRRI NNLGEAFIYR GVRVRVWVAS IPKRIMGGHV
     IFKVTDGRRF IDVAAYEPTG KLRRIAEKLR PGDEVEVMGI VRPQSSKHGP TINLEKLHII
     MVKPLIKLEN PRCPRCGARM KSAGRGKGYK CPKCGYRDPN AKKIVRVIKR DLEPGWYEPS
     PRAFKHLMKP LKRFGKEKNH YPEEIEPSNF IWYNNMLLK