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Database: UniProt
Entry: T1ZGG6_STRIT
LinkDB: T1ZGG6_STRIT
Original site: T1ZGG6_STRIT 
ID   T1ZGG6_STRIT            Unreviewed;       278 AA.
AC   T1ZGG6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Ribosomal RNA large subunit methyltransferase A {ECO:0000313|EMBL:AGU77028.1};
DE            EC=2.1.1.187 {ECO:0000313|EMBL:AGU77028.1};
GN   Name=rrmA {ECO:0000313|EMBL:AGU77028.1};
GN   ORFNames=SIR_1681 {ECO:0000313|EMBL:AGU77028.1};
OS   Streptococcus intermedius B196.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU77028.1, ECO:0000313|Proteomes:UP000016233};
RN   [1] {ECO:0000313|EMBL:AGU77028.1, ECO:0000313|Proteomes:UP000016233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B196 {ECO:0000313|EMBL:AGU77028.1,
RC   ECO:0000313|Proteomes:UP000016233};
RX   PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA   Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA   Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA   Corbett C.R.;
RT   "Phylogenetic relationship and virulence inference of Streptococcus
RT   Anginosus Group: curated annotation and whole-genome comparative analysis
RT   support distinct species designation.";
RL   BMC Genomics 14:895-895(2013).
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DR   EMBL; CP003857; AGU77028.1; -; Genomic_DNA.
DR   RefSeq; WP_021003267.1; NZ_UZBH01000002.1.
DR   AlphaFoldDB; T1ZGG6; -.
DR   KEGG; sib:SIR_1681; -.
DR   PATRIC; fig|862967.3.peg.1703; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_050931_2_0_9; -.
DR   OrthoDB; 5522265at2; -.
DR   Proteomes; UP000016233; Chromosome.
DR   GO; GO:0052911; F:23S rRNA (guanine(745)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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:AGU77028.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016233};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR018249-2};
KW   Transferase {ECO:0000313|EMBL:AGU77028.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR018249-1}.
FT   DOMAIN          14..56
FT                   /note="23S rRNA (guanine(745)-N(1))-methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21302"
FT   DOMAIN          95..180
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT   BINDING         32
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         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT   BINDING         102..103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
SQ   SEQUENCE   278 AA;  31544 MW;  8D7A6D760CFDBA73 CRC64;
     MKVKLKRFET ANLFACPICQ QALFLSANSL KCQNSHSFDL AKFGYVNLAP QIKQSKAYDK
     SNFQNRQLIL EAGFYQPILN QLIKIATSFS HHSNILDIGC GEGYYARHLQ QLLPDSRIYA
     FDLSKDSIQL AAKSDHSLAV NWFVGDLARL PIQKTSMDVI LDIFSPANYQ EFQRVLRKNG
     LLIKVIPNSQ HLQEIRGIVA DKLTNTNYSN QNILDHFKES FTIIDSYDVA GTFSLKENEK
     NALLKMTPLL FNINIKNIDW SSLDNITIAA KILIGQQK
//
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