GenomeNet

Database: UniProt
Entry: A0A498E4A9_9ACTN
LinkDB: A0A498E4A9_9ACTN
Original site: A0A498E4A9_9ACTN 
ID   A0A498E4A9_9ACTN        Unreviewed;       471 AA.
AC   A0A498E4A9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:RLL65724.1};
GN   ORFNames=D7M15_01100 {ECO:0000313|EMBL:RLL65724.1};
OS   Streptomyces sp. Z26.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2500177 {ECO:0000313|EMBL:RLL65724.1, ECO:0000313|Proteomes:UP000288048};
RN   [1] {ECO:0000313|EMBL:RLL65724.1, ECO:0000313|Proteomes:UP000288048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z26 {ECO:0000313|EMBL:RLL65724.1,
RC   ECO:0000313|Proteomes:UP000288048};
RA   Buchmann A., Cano-Prieto C., Baz M., Hassani L., Barakate M., Nafis A.,
RA   Niedermeyer T.H.J., Gross H.;
RT   "Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces
RT   sp. Z26, isolated from potato rhizosphere in Morocco.";
RL   Submitted (OCT-2018) 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:RLL65724.1}.
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; RCHV01000002; RLL65724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498E4A9; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000288048; 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}; Reference proteome {ECO:0000313|Proteomes:UP000288048};
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          184..470
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         287..293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         312
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"
FT   BINDING         355
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   471 AA;  50708 MW;  673A074FECE4532D CRC64;
     MSTRPRRPAK PYRRPRKDPV RILAFEALRA VDERDAYANL VLPPLLAKAR EQGDFDSRDA
     ALATELVYGT LRWQGTYDAI IAACVDRPLR EVDPPVLDVL ALGAHQLLGT RIPTHAAVSA
     SVELARVVLG DGRAKFVNAV LRRITADGLD LDGWLDRVAP PYDEDAEEHL AVRHGHPRWI
     VSALWDALGG GRAGMEELLT ADNERPEVTL VARPGRSEPA ELLAAGGVPG RWSPYAVRLT
     EGGEPGAVEA VREGRAGVQD EGSQLVALAL AAAPLDGGPD RRWLDVCAGP GGKAALLGAV
     AAGRGAALTA AEKQPHRARL VDRALAGNPG PYQVVAADGT RPAWRPGTFD RVLADVPCTG
     LGALRRRPEA RWRRRPEDLE RFAPLQRGLL ERALEAVRVG GVVGYATCSP HLAETRAVVD
     DVRRRHPGTE LLDARPLFEG VAALGDGPDV QLWPHLHGTD AMYLALLRRT A
//
DBGET integrated database retrieval system