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Database: UniProt
Entry: A0A0P7HF90_9MICC
LinkDB: A0A0P7HF90_9MICC
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ID   A0A0P7HF90_9MICC        Unreviewed;       494 AA.
AC   A0A0P7HF90;
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:KPN18812.1};
GN   ORFNames=AO716_13670 {ECO:0000313|EMBL:KPN18812.1};
OS   Arthrobacter sp. Edens01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN18812.1, ECO:0000313|Proteomes:UP000054460};
RN   [1] {ECO:0000313|EMBL:KPN18812.1, ECO:0000313|Proteomes:UP000054460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edens01 {ECO:0000313|EMBL:KPN18812.1,
RC   ECO:0000313|Proteomes:UP000054460};
RA   Couger M.B.;
RT   "Draft Genome of Arthrobacter sp. strain Edens01.";
RL   Submitted (SEP-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:KPN18812.1}.
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DR   EMBL; LKIU01000005; KPN18812.1; -; Genomic_DNA.
DR   RefSeq; WP_055241497.1; NZ_LKIU01000005.1.
DR   AlphaFoldDB; A0A0P7HF90; -.
DR   STRING; 1732020.AO716_13670; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000054460; 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:UP000054460};
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          193..493
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         303..309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         355
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         373
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   494 AA;  52688 MW;  335B343722F5F4E1 CRC64;
     MSSSDRNAKG HQRSRPSVRS RTSAAPSQRT RAADPARLVA FEVLRAVSGE DAYANLVLPK
     SIRKHRLDKR DAGFATELAY GALRGQGIYD AILARCVDRP LEKLDPAVLD ALRIGAHQLL
     AMRVPAHAAL DQTVGLARAV IGAGPSALIN AVLRKVAARD LAEWTALLTE DEQDAVKRSA
     IEYSHPEWIV RALRQSLVAH GRSVEEITDL LQADNDAPVV NLVALPGLGS LDEAREAGAV
     EGGLVKDSAL FAAGDVGRLE SVRAGTTRVQ DAGSQLVARA LAELELDGVA PDEDGMEKWL
     DMCAGPGGKA ALLAALAHEK GAVILANEPA PHRAQLVRQA LEAVPGETWN VRTGDGRTVA
     EDYPETFDRI LVDAPCTGLG ALRRRPESRW RRQPGDVGDL GSLQRELLTT AVDAVKPGGV
     VAYVTCSPHP AETKAVVADV LRKRNDLELL DAGAALDAVS LTGSLEAGHE ATAQLWPHIH
     QTDAMFLALI RRKI
//
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