ID C1CAT0_STRP7 Unreviewed; 282 AA.
AC C1CAT0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=23S rRNA m1G745 methyltransferase {ECO:0000313|EMBL:ACO17440.1};
GN OrderedLocusNames=SP70585_2209 {ECO:0000313|EMBL:ACO17440.1};
OS Streptococcus pneumoniae (strain 70585).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488221 {ECO:0000313|EMBL:ACO17440.1, ECO:0000313|Proteomes:UP000002211};
RN [1] {ECO:0000313|Proteomes:UP000002211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70585 {ECO:0000313|Proteomes:UP000002211};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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DR EMBL; CP000918; ACO17440.1; -; Genomic_DNA.
DR RefSeq; WP_001095521.1; NC_012468.1.
DR AlphaFoldDB; C1CAT0; -.
DR KEGG; snm:SP70585_2209; -.
DR HOGENOM; CLU_050931_2_0_9; -.
DR Proteomes; UP000002211; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR048647; RlmA_N.
DR InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43460:SF1; METHYLTRANSF_11 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43460; METHYLTRANSFERASE; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF21302; RlmA_N; 1.
DR PIRSF; PIRSF018249; MyrA_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR018249-1};
KW Methyltransferase {ECO:0000313|EMBL:ACO17440.1};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR018249-2};
KW Transferase {ECO:0000313|EMBL:ACO17440.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR018249-1}.
FT DOMAIN 18..58
FT /note="23S rRNA (guanine(745)-N(1))-methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21302"
FT DOMAIN 99..180
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT BINDING 106..107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
SQ SEQUENCE 282 AA; 31998 MW; DFB8C85CBFC2242B CRC64;
MNTNLKPKLQ RFASATAFAC PICQENLTLL KTNFKCCNRH SFDLAKFGYV NLAPQIKQSA
NYDKENFQNR QQILEAGFYQ AILDAVSDLL ASSKTTTTIL DIGCGEGFYS RKLQESHSEK
TFYAFDISKD SVQIAAKSEP NWAVNWFVGD LARLPIKDAS MDILLDIFSP ANYGEFRRVL
SKDGILIKVI PTENHLKEIR QRVQDQLTNK EYSNQDIKEH FQEHFTILSS QTASLTKTIT
AEQLQALLSM TPLLFHVDQS KIDWSQLTEI TIEAEILVGK AF
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