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Database: UniProt
Entry: A0A127A118_9MICC
LinkDB: A0A127A118_9MICC
Original site: A0A127A118_9MICC 
ID   A0A127A118_9MICC        Unreviewed;       542 AA.
AC   A0A127A118;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:AMM32581.1};
GN   ORFNames=SA2016_1908 {ECO:0000313|EMBL:AMM32581.1};
OS   Sinomonas atrocyanea.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM32581.1, ECO:0000313|Proteomes:UP000070134};
RN   [1] {ECO:0000313|EMBL:AMM32581.1, ECO:0000313|Proteomes:UP000070134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM32581.1,
RC   ECO:0000313|Proteomes:UP000070134};
RA   Kim K.M.;
RT   "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CP014518; AMM32581.1; -; Genomic_DNA.
DR   RefSeq; WP_066497570.1; NZ_CP014518.1.
DR   AlphaFoldDB; A0A127A118; -.
DR   STRING; 37927.SA2016_1908; -.
DR   KEGG; satk:SA2016_1908; -.
DR   PATRIC; fig|37927.3.peg.1959; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000070134; Chromosome.
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:UP000070134};
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          230..533
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        467
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         344..350
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         369
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         396
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         414
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   542 AA;  57084 MW;  A3D49817296A5843 CRC64;
     MSDGRGPGGS GRRGEPGRPE REPGGRGRPE GGGPGPRRDT HGRERNRGGR GPRQFSGQAP
     SQRSRAADPA RLVAFEVLRA VSRDDAYANL VMPQSIRRHR LDRRDAAFAT ELAYGALRGQ
     GTYDAILALN VDRPLSQLDP AVLDVLRLGA HQLLAMRVPP HAALNQTVAL TRAVVGAGPS
     SLVNAVLRRV SARTADEWLA ELTAAQPDAT ERDALAYAHP SWIVRALRQS LAAHGRPVEE
     ITELLDADNA APVVNLVALP GLGRLEEALD AGAQPGDLVE DSALSGGGDL GRLPAVREGT
     LRAQDVGSQL VARAVAAAPL HRAGDVPADA AGADRRPERW LDVCAGPGGK AALLGALAAE
     QGATLLANEV APHRAELVRK ALAPVPDSVW EVRTGDGRDL GREYPGRFDR VVVDAPCTGL
     GALRRRPESR WRRSPSDLAE LGPLQRALLD AAIDAAAPGG VVGYITCSPH PAETTVVVAD
     ALKRRHDIEL LDAGAALDAV ALRPLGAGHD GTAQLWPHVH STDAMFLALF RKLPAATPSK
     ET
//
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