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Database: UniProt
Entry: A0A099JLE9_9MICO
LinkDB: A0A099JLE9_9MICO
Original site: A0A099JLE9_9MICO 
ID   A0A099JLE9_9MICO        Unreviewed;       455 AA.
AC   A0A099JLE9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:KGJ79164.1};
GN   ORFNames=GY21_05800 {ECO:0000313|EMBL:KGJ79164.1};
OS   Cryobacterium roopkundense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ79164.1, ECO:0000313|Proteomes:UP000029864};
RN   [1] {ECO:0000313|EMBL:KGJ79164.1, ECO:0000313|Proteomes:UP000029864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RuG17 {ECO:0000313|EMBL:KGJ79164.1,
RC   ECO:0000313|Proteomes:UP000029864};
RA   Sisinthy S.;
RL   Submitted (AUG-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|ARBA:ARBA00007494,
CC       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:KGJ79164.1}.
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DR   EMBL; JPXF01000017; KGJ79164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099JLE9; -.
DR   STRING; 1001240.GY21_05800; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   Proteomes; UP000029864; 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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 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:UP000029864};
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          161..453
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        385
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         263..269
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   455 AA;  48539 MW;  9D1F17E722FF5F66 CRC64;
     MQPARRVAYE VIAAVRESDA YANLLLPTRI QRAALNTADA GLATELTYGT LRMQGLYDRV
     IALAAGRAVT AIDPAILDVL RLGTHQLLAT RVATHAAVNE SVSLAKQVGS RSATGFTNGV
     LRTISRSSAE EWLERVLADA GNDDDRLAAE HSHPSWVVRA FRQSLRNEGR ENELVELLVA
     DNVPAKVNMV ALPGLTSKDD TDKLGEPDAF SPTGFVLAGG DPYHLMSAAG GRVRVQDEGS
     QLAALSLSRA RAVKPGERWL DLCAGPGGKA ALLAAEARSH GAELVANELV PARATLVRNA
     LAAIPEKIPV WELDGTRIAE KHPEEFDRIL LDAPCTGLGA LRRRPEARWR KQPKDVAELA
     GLQSGLIDAA LGALKPGGIL AYVTCSPHTA ETRSIVATAL KKWAGKVSAL DTAAVVQSLS
     SSELDLAGDP SSVQLWPHRH GTDAMFITLL ERHTE
//
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