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Database: UniProt
Entry: A0A0Q5CMA7_9MICO
LinkDB: A0A0Q5CMA7_9MICO
Original site: A0A0Q5CMA7_9MICO 
ID   A0A0Q5CMA7_9MICO        Unreviewed;       468 AA.
AC   A0A0Q5CMA7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:KQQ27485.1};
GN   ORFNames=ASF54_01400 {ECO:0000313|EMBL:KQQ27485.1};
OS   Frondihabitans sp. Leaf304.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ27485.1, ECO:0000313|Proteomes:UP000051456};
RN   [1] {ECO:0000313|EMBL:KQQ27485.1, ECO:0000313|Proteomes:UP000051456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27485.1,
RC   ECO:0000313|Proteomes:UP000051456};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ27485.1, ECO:0000313|Proteomes:UP000051456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27485.1,
RC   ECO:0000313|Proteomes:UP000051456};
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:KQQ27485.1}.
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DR   EMBL; LMNV01000002; KQQ27485.1; -; Genomic_DNA.
DR   RefSeq; WP_055957883.1; NZ_LMNV01000002.1.
DR   AlphaFoldDB; A0A0Q5CMA7; -.
DR   STRING; 1736329.ASF54_01400; -.
DR   Proteomes; UP000051456; 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   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:UP000051456};
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          155..467
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        396
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         256..262
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         281
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   468 AA;  48977 MW;  3E364B0A1F99540E CRC64;
     MALDVIRAVE HDDAYANLLL PQRIVRAGLS PQDAGLATEL TYGTLRMSGY YDRVLSIAAR
     RPTDQIDPAL LDVLRLGAHQ LLATRVAPHA AVDESVSLAR QVGSRSGTGF VNGVLRTVSR
     STPDEWLARV LAETTSPDDA LAARYSHPEW VVRALRGALA AEGRADELET LLEADNEPAR
     VSLVALPGLA DPAAVEGVEG GRFSPVALTA PHGDPASLAD VRSGTLRVQD EGSQLAALAL
     SRLKPIEPGE RWLDMCAGPG GKAALLAAEA AVGGARLTAN ELVPGRVGLV KQALAAVTAA
     ARAAGSSSPA ATASVPELVE VRQGDATEIG ASEPETYARI LLDAPCTGLG ALRRRPEARW
     RKQPRDVAEL TGLQSELFSS ALAALAPGGT LAYVTCSPHT AETRGVVESG LKRWARDGGT
     PIDTIDATEV LQSVAVAELD LGAGPFAQLW PHRHGTDAMF VALLRKRA
//
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