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Database: UniProt
Entry: A0A0Q7UP53_9MICO
LinkDB: A0A0Q7UP53_9MICO
Original site: A0A0Q7UP53_9MICO 
ID   A0A0Q7UP53_9MICO        Unreviewed;       442 AA.
AC   A0A0Q7UP53;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:KQZ10050.1};
GN   ORFNames=ASD19_10475 {ECO:0000313|EMBL:KQZ10050.1};
OS   Microbacterium sp. Root53.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQZ10050.1, ECO:0000313|Proteomes:UP000051407};
RN   [1] {ECO:0000313|Proteomes:UP000051407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ10050.1, ECO:0000313|Proteomes:UP000051407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root53 {ECO:0000313|EMBL:KQZ10050.1,
RC   ECO:0000313|Proteomes:UP000051407};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQZ10050.1}.
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DR   EMBL; LMFR01000002; KQZ10050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7UP53; -.
DR   STRING; 1736553.ASD19_10475; -.
DR   Proteomes; UP000051407; 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:UP000051407};
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          139..441
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        370
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         248..254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   442 AA;  47085 MW;  748C0DDE5B4B7B81 CRC64;
     MLRAVNESDA YANLLLPREL ERAGLSGGDA ALATELTYGT LRRLGTYDAV ITAAADRDAA
     SIDPPVLDAL RLGVHQLMAT RVASHAAVNE SVSLAREASG AGAGGFANAV LRRVARDRPG
     EWMARVADTA RSDDERIGLE AAHPVWIVRA LRRALAAEGR ADELDDLLDA DNVSPRVTMA
     ALPGLAEPDG LRTAYSPVGF RLRSGDPEPL VRESGGTVRV QDEGSQLVAL ALSRHAPVEP
     GERWLDLCAG PGGKTALLAA EALAHGARLE ANELVPARAG LVRRALEAVP LEVVVHERDG
     RELAAENRGV YDRILVDAPC TGLGALRRRP EARWRKQPSD VAELAEIQTG LLREAIGALK
     PGGVVAYVTC SPHLAETAAI VAQVRDELGD AVEELDARAV LRRVSRGALD LPVPESGAGH
     AQLWPHRHGT DAMFLALLRR RR
//
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