TIAS_THEVO
ID TIAS_THEVO Reviewed; 437 AA.
AC Q97B59;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=TV0599;
GN ORFNames=TVG0590669;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB59741.1; -; Genomic_DNA.
DR RefSeq; WP_010916857.1; NC_002689.2.
DR AlphaFoldDB; Q97B59; -.
DR SMR; Q97B59; -.
DR STRING; 273116.14324814; -.
DR EnsemblBacteria; BAB59741; BAB59741; BAB59741.
DR GeneID; 1441705; -.
DR KEGG; tvo:TVG0590669; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OMA; GMCTTYL; -.
DR OrthoDB; 58019at2157; -.
DR PhylomeDB; Q97B59; -.
DR Proteomes; UP000001017; 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..437
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407306"
SQ SEQUENCE 437 AA; 49674 MW; FB358153AB562755 CRC64;
MFLAFDDTDS PSGMCTTYLM EEFLRKVNLD VIGYPRLVRL NPNIRYKTRG NGALSVHLGR
GIGKKHTIGE LHGKILYGYA EGEDEYDENV LYVMKDLVEK YSELDYFNTN PGIVVSKNPF
PENYYWSALE REIRIEEAEN FITENNGKFL KFKSGRGIIG SGAAISWPAT RTTYEILAYK
YPHPEEIETE KKMRLSILAD TFRGTFNNVD IANKYPAIFP NPKTPVIFGI RGLYPSVLAN
AAKKVIDDGS INYDSTVTYL TNQATDDHII DEPNVIEDLH SYKITAEIID KPFSVAGGHY
FVRSISRAGE FTAAAFEPTK EFRHTFSKLM PGDTVTFYGS FTNGNLNVEK MQIISVSRVF
SRVTPLCKFC NTRTKSKGKN DFRCPKCGRR YNTPDYHEVK REISPGKYDV PVVARRHLSM
PFEIESMFKT KINALEA