位置:首页 > 蛋白库 > TYW3_AERPE
TYW3_AERPE
ID   TYW3_AERPE              Reviewed;         188 AA.
AC   Q9YDV3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00266};
DE            EC=2.1.1.282 {ECO:0000255|HAMAP-Rule:MF_00266};
DE   AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw3 {ECO:0000255|HAMAP-Rule:MF_00266};
GN   Name=taw3 {ECO:0000255|HAMAP-Rule:MF_00266}; OrderedLocusNames=APE_0816;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of hypothetical protein from Aeropyrum pernix.";
RL   Submitted (JAN-2007) to the PDB data bank.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that acts
CC       as a component of the wyosine derivatives biosynthesis pathway.
CC       Probably methylates N-4 position of wybutosine-86 to produce
CC       wybutosine-72. {ECO:0000255|HAMAP-Rule:MF_00266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC         tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC         carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC         COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00266};
CC   -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00266}.
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; BA000002; BAA79794.1; -; Genomic_DNA.
DR   PIR; B72674; B72674.
DR   PDB; 2DVK; X-ray; 1.80 A; A=1-188.
DR   PDBsum; 2DVK; -.
DR   AlphaFoldDB; Q9YDV3; -.
DR   SMR; Q9YDV3; -.
DR   STRING; 272557.APE_0816; -.
DR   EnsemblBacteria; BAA79794; BAA79794; APE_0816.
DR   KEGG; ape:APE_0816; -.
DR   eggNOG; arCOG04156; Archaea.
DR   OMA; GFKYTTF; -.
DR   EvolutionaryTrace; Q9YDV3; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031591; P:wybutosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1960.10; -; 1.
DR   HAMAP; MF_00266; TYW3_archaea; 1.
DR   InterPro; IPR022908; Taw3.
DR   InterPro; IPR003827; tRNA_yW-synthesising.
DR   InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR   Pfam; PF02676; TYW3; 1.
DR   SUPFAM; SSF111278; SSF111278; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..188
FT                   /note="tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-
FT                   demethylwyosine(37)-N(4))-methyltransferase"
FT                   /id="PRO_0000157091"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   HELIX           22..29
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          34..40
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   HELIX           70..77
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   HELIX           100..112
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:2DVK"
FT   HELIX           153..183
FT                   /evidence="ECO:0007829|PDB:2DVK"
SQ   SEQUENCE   188 AA;  20994 MW;  2574AC83FEE9FC1C CRC64;
     MGSIEEVLLE ERLIGYLDPG AEKVLARINR PSKIVSTSSC TGRITLIEGE AHWLRNGARV
     AYKTHHPISR SEVERVLRRG FTNLWLKVTG PILHLRVEGW QCAKSLLEAA RRNGFKHSGV
     ISIAEDSRLV IEIMSSQSMS VPLVMEGARI VGDDALDMLI EKANTILVES RIGLDTFSRE
     VEELVECF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024