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Database: UniProt
Entry: A0A2S4Y559_9ACTN
LinkDB: A0A2S4Y559_9ACTN
Original site: A0A2S4Y559_9ACTN 
ID   A0A2S4Y559_9ACTN        Unreviewed;       375 AA.
AC   A0A2S4Y559;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:POX43964.1};
DE   Flags: Fragment;
GN   ORFNames=C3488_34560 {ECO:0000313|EMBL:POX43964.1};
OS   Streptomyces sp. Ru72.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080747 {ECO:0000313|EMBL:POX43964.1, ECO:0000313|Proteomes:UP000237426};
RN   [1] {ECO:0000313|EMBL:POX43964.1, ECO:0000313|Proteomes:UP000237426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru72 {ECO:0000313|EMBL:POX43964.1,
RC   ECO:0000313|Proteomes:UP000237426};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:POX43964.1}.
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DR   EMBL; PQSR01000122; POX43964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4Y559; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000237426; 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:UP000237426};
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          185..375
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   BINDING         288..294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         356
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   NON_TER         375
FT                   /evidence="ECO:0000313|EMBL:POX43964.1"
SQ   SEQUENCE   375 AA;  40419 MW;  2603F02F77F75CF3 CRC64;
     MTEQSRRPRK PGKPYRRPKK DPVRILAFDA LRAVDERDAY ANLVLPPLLR KAREKGDIDG
     RDAALATELV YGTLRRQGTY DAILSACVDR PLRDVDPPVL DVLSLGVHQL LGTRIPTHAA
     VSATVELARV VLGDGRAKFV NAVLRKVAQD DLDAWLERVA PPYDEDPEDH LAVVHSHPRW
     VVSALWDSLG GGRAGIEELL AADNERPEVT LVARPGRSTT EELLDEPAAL PGRWSPYAVR
     LTEGGEPGSV DAVREGRAGV QDEGSQLVAL ALANAPLDGP DRAWLDGCAG PGGKAALLAA
     LAAERGAVLL ASEKQPHRAG LVAKALAGNP GPYQVVAADG TRPPWRPGTF DRVLMDVPCT
     GLGALRRRPE ARWRR
//
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