ID   TIAS_HYPBU              Reviewed;         429 AA.
AC   A2BIT1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=Hbut_0008;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM79887.1; -; Genomic_DNA.
DR   RefSeq; WP_011821204.1; NC_008818.1.
DR   AlphaFoldDB; A2BIT1; -.
DR   SMR; A2BIT1; -.
DR   STRING; 415426.Hbut_0008; -.
DR   PRIDE; A2BIT1; -.
DR   EnsemblBacteria; ABM79887; ABM79887; Hbut_0008.
DR   GeneID; 4781575; -.
DR   KEGG; hbu:Hbut_0008; -.
DR   eggNOG; arCOG01115; Archaea.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   OMA; GMCTTYL; -.
DR   OrthoDB; 58019at2157; -.
DR   Proteomes; UP000002593; 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..429
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407292"
FT   REGION          403..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  48075 MW;  B73885E524B82BEB CRC64;
     MSIQEDGLEP MLLAIGIDSF DTPLAGCTTH FTSILAYTLS IHGYRLADYP WLVRLNPAVP
     WKTRGNGATA LLVSVDREDE ARRVAEEVTS RLAKAYGSTG KESFVAILLY HADNLQDYIT
     ARPHCLVELY RRAVHELVPL KTAMNCLESI REDGKTKLIA LHGSTHRGLV GALAALGADL
     ITDHTFELIV YRKPRMWSEP RRIDEDSIIE FDLKTRPLTF LNYDYEQSKP LIAPHGFDPV
     LYGVRGEEPH ILLKALKIID VEEEPSHWTI FRTNQATNAH LQRKEIERVR PYDNAIVCGV
     IEDTKPIPGG HVIVRLCNNT CIDTAFYRET GRLRNHVLKL PRGTLVEVGG QVKPHTDKLT
     LNAEYLRILE PASLRAGGCT ATIPSGRNVI LYPPRAAFHH LMKPPERPLH PSKSLEPPST
     PIHSDTISL