TIAS_THEGJ
ID TIAS_THEGJ Reviewed; 428 AA.
AC C5A5L9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 64.
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=TGAM_1029;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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=ACS33531.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001398; ACS33531.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048811413.1; NC_012804.1.
DR AlphaFoldDB; C5A5L9; -.
DR SMR; C5A5L9; -.
DR STRING; 593117.TGAM_1029; -.
DR PaxDb; C5A5L9; -.
DR EnsemblBacteria; ACS33531; ACS33531; TGAM_1029.
DR GeneID; 7988086; -.
DR KEGG; tga:TGAM_1029; -.
DR PATRIC; fig|593117.10.peg.1025; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OrthoDB; 58019at2157; -.
DR Proteomes; UP000001488; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR024913; tRNA_Ile2__agm2C_synt.
DR Pfam; PF08489; DUF1743; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT CHAIN 1..428
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407303"
SQ SEQUENCE 428 AA; 48909 MW; 167FB40EEADE1CC7 CRC64;
MLLHIGIDDT DSPNGMCTTY LGALLYREIS RLAEPTDLPR LIRLNPNIPY KTRGNGAVAM
TFEVDEEAVP EVKDLVLFYV NQLADFTHEN TNPGVVFFEG EIPEELQEFS LKALREHVTI
EEAERVAREV GAEFFKFKLG RGIIGALASI GYPLERFTYE LLAYREPENW GTPRKVDAES
VFLADRWSYP FTYDNVDPYK RTILIAPHGK DPVLVGLRGI DRGRVLQTFE MVRFGEPVAF
YQLYKTNQNT DDHLTPKKIG ELKLYDSAVV RGRVSKPYWE RGRHVFFELE DETGKIRVAA
FEPTKKFRNY VRKLLPGDEI IAAGGVKEHE GVLTLNLEKF YPVKLVPKIE YRKPKCPRCG
GTMKSKGDYL KCKRCGYRMP KKLIPVEVPR ELERKIYEVP PDARKHLSRP LVLPGGEERV
LEALGNSG