ID A0A177EJ39_9MICR Unreviewed; 375 AA.
AC A0A177EJ39;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ribosomal RNA methyltransferase Nop2 {ECO:0000313|EMBL:OAG31994.1};
GN ORFNames=NEDG_00469 {ECO:0000313|EMBL:OAG31994.1};
OS Nematocida displodere.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=1805483 {ECO:0000313|EMBL:OAG31994.1, ECO:0000313|Proteomes:UP000185944};
RN [1] {ECO:0000313|EMBL:OAG31994.1, ECO:0000313|Proteomes:UP000185944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUm2807 {ECO:0000313|EMBL:OAG31994.1,
RC ECO:0000313|Proteomes:UP000185944};
RA Luallen R.J., Reinke A.W., Tong L., Botts M.R., Felix M.-A., Troemel E.R.;
RT "Discovery of a natural microsporidian pathogen with a broad tissue tropism
RT in Caenorhabditis elegans.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {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:OAG31994.1}.
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DR EMBL; LTDL01000014; OAG31994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177EJ39; -.
DR STRING; 1805483.A0A177EJ39; -.
DR EnsemblFungi; OAG31994; OAG31994; NEDG_00469.
DR VEuPathDB; MicrosporidiaDB:NEDG_00469; -.
DR OrthoDB; 1268at2759; -.
DR Proteomes; UP000185944; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0070475; P:rRNA base methylation; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
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:UP000185944};
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 46..331
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 336..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 137..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 375 AA; 42076 MW; BE3D17BDFBB70755 CRC64;
MHGEVEEIHE RIQNLERLGT AIEATYNDYL LDKITEMFSP EEKDAFIVAS DKKRPATLRT
NTLFDKRSTI LHKLSTRGVN VEGIEWSDCG AVVYNTDVPI GATPEYLAGF YMLQSPSSML
PVMALSPQPN EKVVDMCAAP GGKTTHIAAL MSNTGVLYAN DVSKERVCSL AANIQRMGVT
NTVCMNMDGL ALPIDKADKV LLDAPCSGTG VLSKDPAAKR NKDAEIIKRI QMKQKRLILK
AFDMLDSHKP ETATLVYSTC SILVEENEYV VDYLLRKRPN ARVVDTDLPI GREGFKSFRG
LHFHPSLRLT RRFYPHVHNT DGFFVSKIRK TGLNQKEIED RRKAQDASRK RQGLEPYQKK
QKTVSNEPKT SKTSK
//
