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Database: UniProt
Entry: A0A073AZT0_9PSEU
LinkDB: A0A073AZT0_9PSEU
Original site: A0A073AZT0_9PSEU 
ID   A0A073AZT0_9PSEU        Unreviewed;       473 AA.
AC   A0A073AZT0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:KEI44826.1};
GN   ORFNames=GU90_06225 {ECO:0000313|EMBL:KEI44826.1};
OS   Saccharopolyspora rectivirgula.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=28042 {ECO:0000313|EMBL:KEI44826.1, ECO:0000313|Proteomes:UP000031419};
RN   [1] {ECO:0000313|EMBL:KEI44826.1, ECO:0000313|Proteomes:UP000031419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43113 {ECO:0000313|EMBL:KEI44826.1,
RC   ECO:0000313|Proteomes:UP000031419};
RA   Barrera C., Millon L., Rognon B., Zaugg C., Monod M.;
RT   "Saccharopolyspora rectivirgula DSM-43113 Genome sequencing.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KEI44826.1}.
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DR   EMBL; JNVU01000017; KEI44826.1; -; Genomic_DNA.
DR   RefSeq; WP_029721027.1; NZ_JNVU01000017.1.
DR   AlphaFoldDB; A0A073AZT0; -.
DR   STRING; 28042.GU90_06225; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000031419; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000031419};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          189..472
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         293..299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         342
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         358
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   473 AA;  50420 MW;  496E2D16A6C51073 CRC64;
     MNHRRRPARP ARNRPPKRKP NPARPVDVDP ARLAAVDTLR AVRERDAYAN LALPALLQQR
     QITGRDAALA TELTYGTCRA QGLLDAVLAE CSSRPLSEVD GKLLDALRLG AYQLLRTRIP
     AHAAVAATVD IVRMHSGTKL AGFVNAVLRR VAEHDEETWV AKIAPDPDTD PVGHLALRHA
     HPRWIAQAFA DSLEDSDAEL AAALAADDAR PAVHLTARPG EISADELAAI TGGDPAPYSP
     YGVHLEAGSG DPGELEPVKE GFATVQDEGS QLVALALTRA ELSGSDSRWL DLCAGPGGKA
     ALLGALITLD GGELDAVEQA PHRADLVRKA TEGLSVSVHV ADGREPGLEP GYDRVLVDAP
     CTGLGSLRRR PESRWRRQPS DVGELTKLQR ELLLSAVRLT RPGGVVGYVV CSPHLAETEG
     VVADVVRRAP VEQIDARECF PGVPDLGGGP AVQLWPHRHG TDAMFCALLR VTG
//
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