TIAS_METV3
ID TIAS_METV3 Reviewed; 508 AA.
AC D7DRZ8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, 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=Mvol_0248;
OS Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=456320;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1334 / A3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanococcus voltae A3.";
RL Submitted (MAY-2010) 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; CP002057; ADI35908.1; -; Genomic_DNA.
DR RefSeq; WP_013179636.1; NC_014222.1.
DR AlphaFoldDB; D7DRZ8; -.
DR SMR; D7DRZ8; -.
DR STRING; 456320.Mvol_0248; -.
DR EnsemblBacteria; ADI35908; ADI35908; Mvol_0248.
DR GeneID; 9275468; -.
DR KEGG; mvo:Mvol_0248; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OrthoDB; 58019at2157; -.
DR Proteomes; UP000007722; 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..508
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407295"
FT DNA_BIND 367..427
FT /note="OB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01892"
SQ SEQUENCE 508 AA; 57821 MW; 92DEDC60858C1C4C CRC64;
MYIGIDDTDS REKYCTTYVG TLIVEELLKL GYILEEPRLI RMNPMVKYKT RGNGGVCLKI
VGKIGAEDTK KNNSNKNNSN NGTPKNIEYD YKQALEDFNR GNIDYEALSK ESNCKSSLKS
HIKSLKSLKS YRTTLNPEIT EESYKLSKSE YLEVKTIVSS IVEKYTDFDC STTNPGIVLI
NSRLTRQKKA ILKNYYNSVL TEIVSLDEAE AIIKKVGAEY IKYKKGLGII GSLGAISSYF
SENQTYTYEL LAYRENDKWG TERYVIDSSV VEMDKMTYPY TFNNVDNNKN IIAPNTKCPV
LYGIRGVSKE ILFNAKEIVE SENIDKYMIY RTNQGTDHHL RIMNIADARE NTGAILSGYI
SEEFTEITGG HVLIELTDST GSINCIAYEP TKKFRHIIRE LAIGDLITVY GTIREEPYQL
NIEKINVVKL NNLYEKVKKC ECGGTLKSKG VSSGYKCNKC GKRLKYDEIP KIQIVRNLRE
GFYEVPPSAR RHLSMPLSLI NYLPNNLR