TIAS_ARCFU
ID TIAS_ARCFU Reviewed; 420 AA.
AC O28025;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS;
DE Short=tRNA(Ile2)-agm2C synthetase;
DE EC=6.3.4.22;
DE AltName: Full=tRNA(Ile2) agmatidine synthetase;
GN Name=tiaS; OrderedLocusNames=AF_2259;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-140; GLY-141; TYR-163;
RP ARG-164; ARG-217; GLY-218; THR-248; ASP-249; CYS-352 AND CYS-355.
RX PubMed=20139989; DOI=10.1038/nchembio.323;
RA Ikeuchi Y., Kimura S., Numata T., Nakamura D., Yokogawa T., Ogata T.,
RA Wada T., Suzuki T., Suzuki T.;
RT "Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA
RT decoding in archaea.";
RL Nat. Chem. Biol. 6:277-282(2010).
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:0000269|PubMed:20139989}.
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:0000269|PubMed:20139989};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TiaS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB88990.1; -; Genomic_DNA.
DR PIR; C69532; C69532.
DR RefSeq; WP_010879748.1; NC_000917.1.
DR PDB; 3AMT; X-ray; 2.90 A; A=1-420.
DR PDB; 3AMU; X-ray; 3.10 A; A=1-420.
DR PDB; 3AU7; X-ray; 2.60 A; A=1-343, A=386-420.
DR PDB; 4RVZ; X-ray; 2.90 A; Z=1-420.
DR PDB; 5XOB; X-ray; 2.48 A; Z=1-420.
DR PDB; 6AGG; X-ray; 2.71 A; Z=1-420.
DR PDBsum; 3AMT; -.
DR PDBsum; 3AMU; -.
DR PDBsum; 3AU7; -.
DR PDBsum; 4RVZ; -.
DR PDBsum; 5XOB; -.
DR PDBsum; 6AGG; -.
DR AlphaFoldDB; O28025; -.
DR SMR; O28025; -.
DR STRING; 224325.AF_2259; -.
DR EnsemblBacteria; AAB88990; AAB88990; AF_2259.
DR GeneID; 24796023; -.
DR KEGG; afu:AF_2259; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OMA; GMCTTYL; -.
DR OrthoDB; 58019at2157; -.
DR PhylomeDB; O28025; -.
DR BRENDA; 6.3.4.22; 414.
DR EvolutionaryTrace; O28025; -.
DR Proteomes; UP000002199; 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; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome; tRNA processing.
FT CHAIN 1..420
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407288"
FT DNA_BIND 268..329
FT /note="OB"
FT MUTAGEN 140
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 141
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 163
FT /note="Y->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 164
FT /note="R->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 217
FT /note="R->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 218
FT /note="G->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 248
FT /note="T->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 249
FT /note="D->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 352
FT /note="C->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT MUTAGEN 355
FT /note="C->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:20139989"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5XOB"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3AMT"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6AGG"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3AMT"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:5XOB"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4RVZ"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5XOB"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4RVZ"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5XOB"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5XOB"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3AMT"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5XOB"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:5XOB"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:3AMU"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:5XOB"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:5XOB"
SQ SEQUENCE 420 AA; 48222 MW; 846D3F445EEC4885 CRC64;
MRVWVGIDDT DSSRGMCTTY LAVLAMERVE RELGKVIGFP RLIRLNPTIP YKTRGNGAVS
FLVEVDDVGE LVDVVNEVII EHAMLDDEKT NPGAVFVDEE LAVKLKPFAD KAIKDVLQID
EALFVIGKYF IPHLRHKKGR GLIGALAAVG AELEDFTLEL IAYRYPERFG TEREYDEESF
FDMDYELYPQ TFDNVDWCND VVVCIPNTPC PVLYGIRGES VEALYKAMES VKTEPVDRRM
IFVTNHATDM HLIGEEEVHR LENYRSYRLR GRVTLEPYDI EGGHVFFEID TKFGSVKCAA
FEPTKQFRNV IRLLRKGDVV EVYGSMKKDT INLEKIQIVE LAEIWVEKNP ICPSCGRRME
SAGRGQGFRC KKCRTKADEK LREKVERELQ PGFYEVPPSA RRHLSKPLIR MNVEGRHIFR