ID   TIAS_IGNH4              Reviewed;         397 AA.
AC   A8A990;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS;
DE            Short=tRNA(Ile2)-agm2C synthetase;
DE            EC=6.3.4.22;
DE   AltName: Full=tRNA(Ile2) agmatidine synthetase;
GN   Name=tiaS; OrderedLocusNames=Igni_0309;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TiaS family. {ECO:0000305}.
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DR   EMBL; CP000816; ABU81492.1; -; Genomic_DNA.
DR   RefSeq; WP_011998344.1; NC_009776.1.
DR   AlphaFoldDB; A8A990; -.
DR   SMR; A8A990; -.
DR   STRING; 453591.Igni_0309; -.
DR   PRIDE; A8A990; -.
DR   EnsemblBacteria; ABU81492; ABU81492; Igni_0309.
DR   GeneID; 5562757; -.
DR   KEGG; iho:Igni_0309; -.
DR   eggNOG; arCOG01115; Archaea.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   OrthoDB; 58019at2157; -.
DR   PhylomeDB; A8A990; -.
DR   Proteomes; UP000000262; 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   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..397
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407293"
SQ   SEQUENCE   397 AA;  44412 MW;  32BFC930653EBAB3 CRC64;
     MIVALDSFDE PRSGCTTLTA SLLALHLASK GFRMLDYPRL VRLNPAVPWK TRGNAAVALE
     FEGSAEELFE EAKAFLERAP GRGALAVGEE FPEVYPDAVE KVLDPDEVAK KFEGLWWGRK
     EALVGALAAG AAEGLNNFEL LAYRLPQNLG RPRRCSFHPA YEALLELAYP SIHESSPEVV
     CPKGPDPVLL GIRGSHPPLM WAALQLFDGE PFWLATMFRT NQHSYEPSRR AEEYPYEFVQ
     KEFEGSYEVR GEDVLFGDYV LFNETGITKI FKEMIGYENK VSVKLDVVVK PGSKGVAALR
     DLRALFWKRK APKCPKCGGP MVSMGKKTLM RKCKKCGYKA EVLPKLEIKV FEGTVFPVQG
     RKLHLEGDYR SPPWPPEGRI CEKPGCAIWV AHGFDHH