ID A0A2A2EJJ4_9BIFI Unreviewed; 299 AA.
AC A0A2A2EJJ4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=S-adenosyl-methyltransferase MraW {ECO:0000313|EMBL:PAU69211.1};
DE Flags: Fragment;
GN ORFNames=B1400_1097 {ECO:0000313|EMBL:PAU69211.1};
OS Bifidobacterium italicum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1960968 {ECO:0000313|EMBL:PAU69211.1, ECO:0000313|Proteomes:UP000217986};
RN [1] {ECO:0000313|EMBL:PAU69211.1, ECO:0000313|Proteomes:UP000217986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70 {ECO:0000313|EMBL:PAU69211.1,
RC ECO:0000313|Proteomes:UP000217986};
RX PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT tree of life.";
RL ISME J. 11:2834-2847(2017).
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000256|ARBA:ARBA00010396}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAU69211.1}.
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DR EMBL; MVOG01000020; PAU69211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2EJJ4; -.
DR Proteomes; UP000217986; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.170; Putative methyltransferase TM0872, insert domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00006; 16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH; 1.
DR PANTHER; PTHR11265:SF0; 12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11265; S-ADENOSYL-METHYLTRANSFERASE MRAW; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF81799; Putative methyltransferase TM0872, insert domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:PAU69211.1};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PAU69211.1}.
FT NON_TER 299
FT /evidence="ECO:0000313|EMBL:PAU69211.1"
SQ SEQUENCE 299 AA; 32254 MW; 53C513AC61F7A2A6 CRC64;
MTDLTDYAHI HQPVLLRDCV ELVSPALAAP GSVVVDCTLG LAGHAVAFLK ANPQARLIGI
DRDSEALGMA GARIASEGLS DRFTPVHAAF DAFDDVLGGL DVAQVDAVFM DLGLSSLQID
ERGRGFSYSH DAPLDMRMDV TQPLTARDVL ATYDERALAH IFKEYGEERF ARQIARRIVA
ERAHGPLETS AQLNALVDGV IPQAHRASGN PAKRVFQALR IEVNGELDKL ARTLPQIANR
LAVGGRLVVE SYHSLEDRSV KTFMNQGLHA DVPAGMPVIP DDMQPFFAPV TKGAVMADA
//
