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Database: UniProt
Entry: A0A419HPC3_9PSEU
LinkDB: A0A419HPC3_9PSEU
Original site: A0A419HPC3_9PSEU 
ID   A0A419HPC3_9PSEU        Unreviewed;       476 AA.
AC   A0A419HPC3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=rRNA small subunit methyltransferase B {ECO:0000313|EMBL:RJQ78189.1};
GN   ORFNames=D5S17_13470 {ECO:0000313|EMBL:RJQ78189.1};
OS   Pseudonocardiaceae bacterium YIM PH 21723.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=2340915 {ECO:0000313|EMBL:RJQ78189.1, ECO:0000313|Proteomes:UP000285726};
RN   [1] {ECO:0000313|Proteomes:UP000285726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM PH 21723 {ECO:0000313|Proteomes:UP000285726};
RA   Miao C.;
RT   "YIM PH21274 draft genome.";
RL   Submitted (SEP-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:RJQ78189.1}.
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DR   EMBL; QZFT01000032; RJQ78189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A419HPC3; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000285726; 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:UP000285726};
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          189..476
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296..302
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         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         361
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   476 AA;  50688 MW;  631BC25329F149C4 CRC64;
     MNRRDQSGDP GRKPSHPRRS HPPRGKRGPA RPPIEDAARQ AALDTLRAVR ERDAYANLAL
     PGLLRQRKIT GRDAALATEL AYGTSRAQGL LDAILAACID RTLAKVESRV LDVLRLGAYQ
     LLRTRIPTHA AVSATVDLMR AENGSGAAGF VNAVLRKVGA RTEAEWVAEL APADEVGAAA
     FAHAHPLWIA EAFRDALGGT GELAAALAAD DERPAIHLAA RPGEISADEL SAITGGDLAP
     YSPYGVHLET GAGDPGELDP VKEGLAVVQD EGSQLCALAL TRVPVEGTDA RWLDLCAGPG
     GKAGLLGALV RMQGGTLDAV EQSEHRAELV RKVTGDLPVI VHVADGRKSG LEPGFDRVLV
     DAPCTGLGAL RRRPEARWRR SAEDTAELTG LQRDLLHAAL DLVRPGGVVA YVLCSPQVSE
     TREVVEAVLA DRGDVEQLDT REYFPDVPQL GDGPHVQLWP HRQGTDAMFC SLLRKL
//
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