ID   TIAS_METLZ              Reviewed;         415 AA.
AC   A2SPT0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=Mlab_0159;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(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; CP000559; ABN06336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2SPT0; -.
DR   SMR; A2SPT0; -.
DR   STRING; 410358.Mlab_0159; -.
DR   EnsemblBacteria; ABN06336; ABN06336; Mlab_0159.
DR   KEGG; mla:Mlab_0159; -.
DR   eggNOG; arCOG01115; Archaea.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   OMA; GMCTTYL; -.
DR   Proteomes; UP000000365; 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..415
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407296"
SQ   SEQUENCE   415 AA;  46508 MW;  3BA277FDF053D73D CRC64;
     MRFYKIISFM LLGLDDTDSP DGMCTTYLGA LIANELKRRG FTVTNHRLVR LNPNVIWKTR
     GNAGISLEIS GGDSTVVFEI ACEFVERFAR FECEKTNPGV VVVESPPDPA FYYQALQRFC
     TIEETVKRLE RIGALYKGYK NGRGLIGALA AVSSVLPDKT YECLAYRKNE VLGTPRIYAE
     EGFFTSEEQT APHTWDTVDF IRREIVCVPH GKDPVLYGIR GDTPKWAIKA TGFLETEEPA
     FSQIWETNQG TDAHLLPLPD GGPIEGESYR FSGVVESLPI TNRGGHVQFT ILSNGMEIPV
     FAFEPTKYFR NAVRELVVGD EITICGSFQK GVLHLEKFRP NLLATQKSRS SPRCPICGGR
     MTSAGKDKGY KCRECSGKVR DVPDQERTLQ TKWYEVPPGS RRHLAKPAVR MKDDI