TIAS_PYRNV
ID TIAS_PYRNV Reviewed; 415 AA.
AC B1YAA9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=Tneu_0126;
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001014; ACB39083.1; -; Genomic_DNA.
DR AlphaFoldDB; B1YAA9; -.
DR SMR; B1YAA9; -.
DR STRING; 444157.Tneu_0126; -.
DR EnsemblBacteria; ACB39083; ACB39083; Tneu_0126.
DR KEGG; tne:Tneu_0126; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OMA; GMCTTYL; -.
DR Proteomes; UP000001694; 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; IPR046349; C1-like_sf.
DR InterPro; IPR013696; DUF1743.
DR InterPro; IPR024913; tRNA_Ile2__agm2C_synt.
DR Pfam; PF08489; DUF1743; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT CHAIN 1..415
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407307"
SQ SEQUENCE 415 AA; 46507 MW; B9312D294EBD264B CRC64;
MRVVVGIDDT DSHRGGCTTY VGYLLAKEVL RRWGAGAFRD FPRLVRLNPN VPFKTRGNAA
VALDLEIPEG DVEELWRLAV ETVAAHSRRE GKTDPGVAMA AGGVPERAKT LYRMALTQVV
SISAAERAGV LTWGGRGKIG AVAAVGAYFP KSTFELIAYR RGDREAIPPD LVRLLEALTY
PYTFHNVDRR RVLIEPRGPD PVYYGIRGLT PQHLRYALSL LEAWGYRPAG WVIYRTNQAT
DAHIELGVFY GDPLPYSFYR ARGLVVEARR VAGRHLVGRL DSGLRFVAYR HLGRLASELE
RCLRCDVVLY GGLKPRRGGL YLYVERAYVL GRYIPARSRC TYCGGSLESL GRGRGWRCRR
CGAVFHSAPI RWLYDTAPRR ALLPRPGEWR HLLKPPDVDP TIPNFFSPSS AEWIG