GenomeNet

Database: UniProt
Entry: A0A124I1B4_9ACTN
LinkDB: A0A124I1B4_9ACTN
Original site: A0A124I1B4_9ACTN 
ID   A0A124I1B4_9ACTN        Unreviewed;       475 AA.
AC   A0A124I1B4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:KUN76996.1};
GN   ORFNames=AQJ64_36065 {ECO:0000313|EMBL:KUN76996.1};
OS   Streptomyces griseoruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN76996.1, ECO:0000313|Proteomes:UP000052982};
RN   [1] {ECO:0000313|EMBL:KUN76996.1, ECO:0000313|Proteomes:UP000052982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN76996.1,
RC   ECO:0000313|Proteomes:UP000052982};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT   for the species Streptomyces griseoruber.";
RL   Submitted (OCT-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:KUN76996.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMWW01000063; KUN76996.1; -; Genomic_DNA.
DR   RefSeq; WP_059203332.1; NZ_KQ948780.1.
DR   AlphaFoldDB; A0A124I1B4; -.
DR   STRING; 1943.AQJ64_36065; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000052982; 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; 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};
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          188..474
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         291..297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         342
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         359
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   475 AA;  51520 MW;  30CC118B6C5D048B CRC64;
     MSDQSHRPRK PARPYRRPQK DPVRMLAFEA LRAVDERDAY ANLVLPPLLR KAREKEGPDK
     FDTRDAALAT ELVYGTLRRQ GTYDAVISAC VDRPLREVDP PVLDVLSLGA HQLLGTRIPT
     HAAVSSAVEL ARVVLGDGRA KFVNAVLRKI AQHDLDGWLE QVAPPYDDDP EEHLAVVHSH
     PRWIVSALWD SLGGGRAGIE DLLEADNERP EVTLVARPGR AAPEELLREE AAVPGRWSPY
     AVRLTEGGEP GAVDAVREGR AGVQDEGSQL VALALANVPV EGRDEKWLDG CAGPGGKAAL
     LAALAAERGA VLLASEKQPH RAGLVARALH GNPGPYQVIA ADGIRPPWRP GSFDRVLMDV
     PCTGLGALRR RPEARWRRRP EDLEGFAPLQ RGLLRTALEA VRVGGVVGYA TCSPHLAETR
     AVVADVLKQF PRTDLVDARP LLPGVPALGD GPDIQLWPHV HGTDAMYLAL IRRTG
//
DBGET integrated database retrieval system