ID   TIAS_CENSY              Reviewed;         446 AA.
AC   A0RZ60;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   25-MAY-2022, entry version 49.
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=CENSYa_2023;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK78627.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DP000238; ABK78627.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0RZ60; -.
DR   SMR; A0RZ60; -.
DR   STRING; 414004.CENSYa_2023; -.
DR   EnsemblBacteria; ABK78627; ABK78627; CENSYa_2023.
DR   KEGG; csy:CENSYa_2023; -.
DR   PATRIC; fig|414004.10.peg.1855; -.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   Proteomes; UP000000758; 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..446
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407290"
SQ   SEQUENCE   446 AA;  48442 MW;  CBD3E3FCF8891467 CRC64;
     MGPLLQLAGT RLHIGIDDTD SIKGMCTTYL GFRLARLLQK EGAEFEDYPR LVRLNPNVPW
     KTRGNGAVGM TVNVSDPEAA RKIAIDAVSL YSDLENGANP AAVFCEGGIP QPVRDLSREA
     LHVMVEQERA RGIIERHCSG LFYTGSGQGM VGAAAAIGYE FGDSTLELLS YRREENRGTP
     RPIWPEDVRG IQGAYPDTFN SYDEARGTSI IAPRGPDPVF YGIRGELASS LLGASEMVRT
     PERLEGYMIY RSNQGTADHL EYVIDAADPR PYSSGTISGV ISTEPVVREG GHVFFEINAG
     GSMVPCAVYK ESGMTDAAAL LRGGDKVVVG GGIRRESGSH PKVLNVEFAR VERLARIYRM
     ANPYCTKCSK SMKSKGIGQG FKCTRCGAAS IHRVEREIPR GISVGLYLPV ASSQRHLARP
     YGRQGRTSRI QFDGASPWLG VFDSGE