ID   TIAS_METKA              Reviewed;         433 AA.
AC   Q8TWM9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=MK1003;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02216.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TWM9; -.
DR   SMR; Q8TWM9; -.
DR   STRING; 190192.MK1003; -.
DR   EnsemblBacteria; AAM02216; AAM02216; MK1003.
DR   KEGG; mka:MK1003; -.
DR   PATRIC; fig|190192.8.peg.1052; -.
DR   HOGENOM; CLU_675459_0_0_2; -.
DR   OMA; GMCTTYL; -.
DR   Proteomes; UP000001826; 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..433
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407297"
SQ   SEQUENCE   433 AA;  47948 MW;  2DECF42DAB5664DC CRC64;
     MDWVALDDTD SPAGGCTTHA AVLLRAELAE AGAEPVGRPL LVRLNPNVPF KTRGNAAVAL
     PVEAPWSVDI EAVVLRALKK VVRKGYPETR PGLVVCEGEP PRVCESVYEE AVRRILNPGR
     VKESVDDDVN VVLEGRGIVG AVAALGFARV RKDHEVTFEG IAYRAEKYWG TERRVEESSI
     REFDRRTFPV TFDNLDSRDG DVLITPNTPC PVLYGVRSVE PDVLEVAPDM IKTREPVVEY
     EIFESNQATD AHLVRVDRLA DAEDYSNPVL DLTVVEEPRR IPGGHVVVRC EDEEGVRVDI
     AAFRPARPLT EVVAALHPGD EIRVAGALRP ETPKHPRTVN VEKLRVLRLE RVEEVRNPVC
     GRCRRSMKSA GRKKGFKCSC GERAPEDSKI GVEVPRELVE GVTYEAPPVA RRHLSKPEYL
     VELGLLEPSP LSR