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Y882_METJA
ID   Y882_METJA              Reviewed;         197 AA.
AC   Q58292;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable S-adenosylmethionine-dependent methyltransferase MJ0882;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MJ0882;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-197, AND S-ADENOSYLMETHIONINE
RP   BINDING.
RX   PubMed=12836702; DOI=10.1023/a:1021279113558;
RA   Huang L., Hung L., Odell M., Yokota H., Kim R., Kim S.H.;
RT   "Structure-based experimental confirmation of biochemical function to a
RT   methyltransferase, MJ0882, from hyperthermophile Methanococcus
RT   jannaschii.";
RL   J. Struct. Funct. Genomics 2:121-127(2002).
CC   -!- FUNCTION: Probable methyltransferase that uses S-adenosylmethionine as
CC       the methyl donor. Binds neither NAD nor NADP in vitro.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; L77117; AAB98886.1; -; Genomic_DNA.
DR   PIR; B64410; B64410.
DR   RefSeq; WP_010870396.1; NC_000909.1.
DR   PDB; 1DUS; X-ray; 1.80 A; A=4-197.
DR   PDBsum; 1DUS; -.
DR   AlphaFoldDB; Q58292; -.
DR   SMR; Q58292; -.
DR   STRING; 243232.MJ_0882; -.
DR   EnsemblBacteria; AAB98886; AAB98886; MJ_0882.
DR   GeneID; 1451771; -.
DR   KEGG; mja:MJ_0882; -.
DR   eggNOG; arCOG00110; Archaea.
DR   HOGENOM; CLU_018398_7_2_2; -.
DR   InParanoid; Q58292; -.
DR   OMA; HMIDVNE; -.
DR   OrthoDB; 72076at2157; -.
DR   PhylomeDB; Q58292; -.
DR   EvolutionaryTrace; Q58292; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..197
FT                   /note="Probable S-adenosylmethionine-dependent
FT                   methyltransferase MJ0882"
FT                   /id="PRO_0000157176"
FT   BINDING         63..67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305"
FT   BINDING         129..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..21
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          24..31
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   TURN            35..38
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   HELIX           42..50
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   HELIX           68..73
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          77..85
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   HELIX           87..99
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   HELIX           136..149
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          150..162
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   HELIX           164..177
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:1DUS"
FT   STRAND          189..195
FT                   /evidence="ECO:0007829|PDB:1DUS"
SQ   SEQUENCE   197 AA;  22244 MW;  F4E108E500ABEB28 CRC64;
     MHYFSEKPTT KSDVKIVEDI LRGKKLKFKT DSGVFSYGKV DKGTKILVEN VVVDKDDDIL
     DLGCGYGVIG IALADEVKST TMADINRRAI KLAKENIKLN NLDNYDIRVV HSDLYENVKD
     RKYNKIITNP PIRAGKEVLH RIIEEGKELL KDNGEIWVVI QTKQGAKSLA KYMKDVFGNV
     ETVTIKGGYR VLKSKKL
 
 
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