ID A0A077MDK2_9MICO Unreviewed; 497 AA.
AC A0A077MDK2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative enzyme {ECO:0000313|EMBL:CCI53985.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:CCI53985.1};
GN ORFNames=BN13_1780001 {ECO:0000313|EMBL:CCI52466.1}, BN13_530015
GN {ECO:0000313|EMBL:CCI53985.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI53985.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI53985.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53985.1};
RA McIlroy S.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCI53985.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53985.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {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:CCI53985.1}.
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DR EMBL; CAJC01000088; CCI52466.1; -; Genomic_DNA.
DR EMBL; CAJC01000165; CCI53985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077MDK2; -.
DR STRING; 1193518.BN13_1780001; -.
DR Proteomes; UP000035720; 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; 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; 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:UP000035720};
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 201..496
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 300..306
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 358
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 376
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 497 AA; 52277 MW; BFA634C900BC26C0 CRC64;
MSQRPTRPRS ATPPRARGRS GDAARLAAYT VLRSVAAGGY ANLELPKELR RRHLRGRDAA
FATELTYGAC RLCGFYDPVI ALAADRPLER LDEAVLDTLR LGAHQLLGMR VPAHAAADET
VALARQVNGA GAAGLVNAVM RRISEADRET WLARVVPTEP LTARLAVEQS HPEWIVKALR
QALIGHGAST AGTVDEDLER LLAADNAAPE LHLVARPGLI EVEELVRAVE STAATAAAHP
HVPTAVVLDH GDPGAIAAIR DGRAAVQDAG SQVVAAALVA TPRTGPGHAP GGRERWLDLC
AGPGGKAGLL AALAVRHDAD LVANEVAPHR ATLVEQTLAA AIEAARGSAS RIEVRTGDGR
RIGAEEPAAY DRILVDAPCT GLGALRRRPE ARWRRTTADL AALGTLQREL LGGALPALAP
GGILAYATCS PHLAETTFVI ADVLKKHPNV QQIDARAAVA DVTTGWTEDL GPGPGVQLWP
HIHGTDGMFF ALLRREG
//
