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Database: UniProt
Entry: A0A0Q8V6R1_9MICO
LinkDB: A0A0Q8V6R1_9MICO
Original site: A0A0Q8V6R1_9MICO 
ID   A0A0Q8V6R1_9MICO        Unreviewed;       460 AA.
AC   A0A0Q8V6R1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:KRC51187.1};
GN   ORFNames=ASE16_09710 {ECO:0000313|EMBL:KRC51187.1};
OS   Leifsonia sp. Root227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC51187.1, ECO:0000313|Proteomes:UP000051819};
RN   [1] {ECO:0000313|EMBL:KRC51187.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC51187.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC51187.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC51187.1,
RC   ECO:0000313|Proteomes:UP000051819};
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|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:KRC51187.1}.
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DR   EMBL; LMIO01000002; KRC51187.1; -; Genomic_DNA.
DR   RefSeq; WP_055894120.1; NZ_LMIO01000002.1.
DR   AlphaFoldDB; A0A0Q8V6R1; -.
DR   STRING; 1736496.ASE16_09710; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000051819; 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:UP000051819};
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          172..460
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        393
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         271..277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         340
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   460 AA;  49056 MW;  E7F42CF001999F67 CRC64;
     MNDRNRNQGG HVQPARRVAY DVIAAVRDSD AYANLLLPTR IARAGLNQGD AGLATELTYG
     TLRMQGYYDL VIARAAGRPV DRIDPPILDV LRLGAHQLLS TRVAPHAAVN ESVALARSVG
     SRSATGFTNG VLREIGRHSP EEWRQRILAD AKGADQELSA LTSHPVWIVR AFRRALEAEG
     REAELTDLLN ADNAAPRVNL VALPGLAELP DDATADRFSP VGFTAGGGDP QARVEGADGR
     LRVQDEGSQL AALALSRARP IVQGERWLDL CAGPGGKAAL LAAEARLGGA TLTANEVVPA
     RAELVRRALA AVPEPVEVWE LDGTTIGETH PERFDRILLD APCTGLGALR RRPEARWRKT
     PRDVAELTGL QARLLDAAIA ALKPGGLIAY VTCSPHIAET RGIVSAALDA HDDIAAVDTP
     AVLQALASER LDLAGDGLAV QLWPHRHGTD AMFVALLEKR
//
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