位置:首页 > 蛋白库 > TIAS_PYRHO
TIAS_PYRHO
ID   TIAS_PYRHO              Reviewed;         424 AA.
AC   O59476;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=PH1812;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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; BA000001; BAA30931.1; -; Genomic_DNA.
DR   PIR; D71192; D71192.
DR   RefSeq; WP_010885872.1; NC_000961.1.
DR   AlphaFoldDB; O59476; -.
DR   SMR; O59476; -.
DR   STRING; 70601.3258248; -.
DR   EnsemblBacteria; BAA30931; BAA30931; BAA30931.
DR   GeneID; 1442654; -.
DR   KEGG; pho:PH1812; -.
DR   eggNOG; arCOG01115; Archaea.
DR   OMA; GMCTTYL; -.
DR   OrthoDB; 58019at2157; -.
DR   BRENDA; 6.3.4.22; 5244.
DR   Proteomes; UP000000752; 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; IPR012340; NA-bd_OB-fold.
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.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT   CHAIN           1..424
FT                   /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT                   /id="PRO_0000407300"
FT   DNA_BIND        268..342
FT                   /note="OB"
SQ   SEQUENCE   424 AA;  48450 MW;  7C40652197462817 CRC64;
     MLLHIGLDDT DSPNGMCTTY LGALLYRELS RFGEPVDLPK LIRLNPNIPY KTRGNGAVSL
     TFDILEDYLN EAKELVVKTV KKLAEVEHEN TNPGIAFLEG EVPEILRRFA IKALREHVTI
     DEAEKIAKKA GAEIVKLKLG RGIIGALASI GYPLNNYTYE LLAYRKLENR EKVRRVDRDS
     VFEMDRKFYP FTYDNVDPFK KTILITPHGK DPVLVGIRGI DKGKVLLAYE NVIINENVEM
     IQLFKTNQST DDHLVWKKIG DIKLYDNVIV KGKVASKYWE RGRHVFFEIE DETGKIRVAA
     FEPTKKFRNY VRKLLPGDEV IVAGGVKEHE GVLTINLEKF YPIKLVPKVE YRKPKCPKCG
     GTMKSKGDYL KCKRCGYKMP KVLIPVKLPR DLERKIYEVP PDARKHLSRP LVLPKSEDKF
     IGPL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024