GenomeNet

Database: UniProt
Entry: A0A0Q8PKL3_9ACTN
LinkDB: A0A0Q8PKL3_9ACTN
Original site: A0A0Q8PKL3_9ACTN 
ID   A0A0Q8PKL3_9ACTN        Unreviewed;       454 AA.
AC   A0A0Q8PKL3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:KRB74079.1};
GN   ORFNames=ASE01_19005 {ECO:0000313|EMBL:KRB74079.1};
OS   Nocardioides sp. Root190.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB74079.1, ECO:0000313|Proteomes:UP000050886};
RN   [1] {ECO:0000313|EMBL:KRB74079.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB74079.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB74079.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB74079.1,
RC   ECO:0000313|Proteomes:UP000050886};
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:KRB74079.1}.
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; LMIA01000012; KRB74079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8PKL3; -.
DR   STRING; 1736488.ASE01_19005; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000050886; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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; IPR001678; MeTrfase_RsmB/NOP2.
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; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF53; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B-RELATED; 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:UP000050886};
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          176..454
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          200..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        391
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         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   454 AA;  48139 MW;  7BA00F396EF75407 CRC64;
     MGPRRATARH GAVRVSKQVD PARLAAFEVL KAVRVDDGYA NLLLPAALQR HALTGRDAAF
     VTELVSGTIR RQGTYDAILG ACIDRSLAKV EAKVLDGLRL GTHQLLAMRV PTHAAIDTTV
     TLVRDQVSQG AAGFANAVLR KVAAQELDAW IAQVAPRNLA VSHSHPQWVV DELKRALRDS
     SKELPALLEA DNLAPRVTLV SRPGRSERSE LPGTPTSYSP YGSVLDGGDP AAVPAVAQRR
     AGVQDEGSQL VAIAAAQAPV SGRDEVWVDL CAGPGGKASL LAALASQRGA RLLAVERHHH
     RAQLVRRAVG RDAGVLVVQS DGTRSPLADG SVDRVLIDAP CTGLGALRRR PEARWRRTPR
     DLKDLVQLQG ALLADGLRVL RPGGALVYAT CSPLLAETSE VVASALETSG AVIDDLRPVL
     GEVPDADGPL PGTVQMWPHR HGTDAMFIAL LRKP
//
DBGET integrated database retrieval system