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RSMD_HAEIN
ID   RSMD_HAEIN              Reviewed;         193 AA.
AC   P44869;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase D;
DE            EC=2.1.1.171;
DE   AltName: Full=16S rRNA m2G966 methyltransferase;
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase;
GN   Name=rsmD; OrderedLocusNames=HI_0767;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RG   Northeast structural genomics consortium (NESG);
RT   "Crystal structure of the putative methylase HI0767 from Haemophilus
RT   influenzae.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: Specifically methylates the guanine in position 966 of 16S
CC       rRNA in the assembled 30S particle. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:23548, Rhea:RHEA-COMP:10211, Rhea:RHEA-COMP:10212,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.171;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmD family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22425.1; -; Genomic_DNA.
DR   PIR; F64158; F64158.
DR   RefSeq; NP_438926.1; NC_000907.1.
DR   RefSeq; WP_005693161.1; NC_000907.1.
DR   PDB; 2IFT; X-ray; 2.30 A; A/B=1-193.
DR   PDBsum; 2IFT; -.
DR   AlphaFoldDB; P44869; -.
DR   SMR; P44869; -.
DR   STRING; 71421.HI_0767; -.
DR   DNASU; 949786; -.
DR   EnsemblBacteria; AAC22425; AAC22425; HI_0767.
DR   KEGG; hin:HI_0767; -.
DR   PATRIC; fig|71421.8.peg.806; -.
DR   eggNOG; COG0742; Bacteria.
DR   HOGENOM; CLU_075826_2_2_6; -.
DR   OMA; FNWLMPY; -.
DR   PhylomeDB; P44869; -.
DR   BioCyc; HINF71421:G1GJ1-807-MON; -.
DR   EvolutionaryTrace; P44869; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0052913; F:16S rRNA (guanine(966)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004398; RNA_MeTrfase_RsmD.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF004553; CHP00095; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00095; TIGR00095; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..193
FT                   /note="Ribosomal RNA small subunit methyltransferase D"
FT                   /id="PRO_0000169550"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   TURN            19..22
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   HELIX           39..52
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   HELIX           66..73
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   HELIX           86..98
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          153..167
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          175..183
FT                   /evidence="ECO:0007829|PDB:2IFT"
FT   STRAND          186..193
FT                   /evidence="ECO:0007829|PDB:2IFT"
SQ   SEQUENCE   193 AA;  22001 MW;  C0D6FC3CF0A831B7 CRC64;
     MKKIQTPNAK GEVRIIAGLW RGRKLPVLNS EGLRPTGDRV KETLFNWLMP YIHQSECLDG
     FAGSGSLGFE ALSRQAKKVT FLELDKTVAN QLKKNLQTLK CSSEQAEVIN QSSLDFLKQP
     QNQPHFDVVF LDPPFHFNLA EQAISLLCEN NWLKPNALIY VETEKDKPLI TPENWTLLKE
     KTTGIVSYRL YQN
 
 
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