ID   TIAS_SULIL              Reviewed;         443 AA.
AC   C3MRH3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
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=LS215_1991;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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; CP001399; ACP35986.1; -; Genomic_DNA.
DR   RefSeq; WP_012714015.1; NC_012589.1.
DR   AlphaFoldDB; C3MRH3; -.
DR   SMR; C3MRH3; -.
DR   PRIDE; C3MRH3; -.
DR   EnsemblBacteria; ACP35986; ACP35986; LS215_1991.
DR   GeneID; 7799639; -.
DR   KEGG; sis:LS215_1991; -.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   OMA; GMCTTYL; -.
DR   OrthoDB; 58019at2157; -.
DR   Proteomes; UP000001747; 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; tRNA processing.
FT   CHAIN           1..443
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407302"
SQ   SEQUENCE   443 AA;  51372 MW;  8028EA39D4523393 CRC64;
     MKYLIGIDDH DSYKFGCTTH FSVILTSYLY KNHNTILLDL PYLVRLNPNI PWKTRGNASI
     KLIVDFNGTK KELADIIFSY SVKYVKNVSL ALEHGRRPGI AIIEYDKYKS LFEKLYDFYI
     KGILDIIPID YAKKFAEKND IEIRGDRGII GSIAALGMSG DYTYELITYR KKENWLKKRM
     INEDSVKRVD EETFPLTFAN YDYINDSPLI TPHGNDPILY GIRGTSIEHL IKAMELIESN
     EDINFFAVFK TNQNTDIHFQ KVGNRFYQEI KKVIQIKNIK ILEGGDVMIR TTDDDILFVY
     KETGELNSAA KLLKEGDEIV AYGAIKPSIT YGKIIELERF EILKLNDLQL INPKCPICGG
     PTKSLGKNKG YKCKKCKYII NTANKSMKNI IRNLSLGIYQ TRAYRHLTRP IFLTLENNNQ
     SFHEERKFLD MYRSELYKLD YHL