ID A0A0V0R263_PSEPJ Unreviewed; 834 AA.
AC A0A0V0R263;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=PPERSA_01175 {ECO:0000313|EMBL:KRX08245.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX08245.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX08245.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX08245.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX08245.1}.
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DR EMBL; LDAU01000067; KRX08245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R263; -.
DR EnsemblProtists; KRX08245; KRX08245; PPERSA_01175.
DR InParanoid; A0A0V0R263; -.
DR OMA; SGDIMQK; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000054937; 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:0001510; P:RNA methylation; IEA:InterPro.
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; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
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 161..535
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 259..265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 292
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 834 AA; 97258 MW; A30D110E2713F1AC CRC64;
MGKFKSQRKK AAQKRLENQE NQENQTKQFE PKISKRVKPE YFNDIKNQPE KYFVNPMFET
YYKTVLASEF ENDEEFKRFW SVMKEKLPVT FRVSPNIVGY EQYQNKLLSG KEYLMKFAQE
AIEVKKQEEE LKQKQQEKEQ EKQNENQEKI EEEQKEQKTE NQEQNQNQQK GGYRVTFPVE
NKYDIDDVKL VSKDWYPNQL AFQLDISKYQ LRKEGVLKKF HLELTKASDA GLLTRQEFVS
MLPPLLLDVQ PTDKVFDMCA APGSKTSQIL EIMSSKAKSA KKEVTGCVIA NDVDTNRAYM
LTHQIDRNST SAMMVVNHQA QFFPTLKDPQ TKQRIQFDKV LCDVPCTGDG ATRKIPKKFQ
DWATRDAISL YQVQLSILMR ALQLCKVGGL VVYSTCSINP IEDEAVVIDA LKKAVPGSLE
LLDCHRRLPN FKGRKGMLSW PVICSKFKKS KLHDKTTEQI EQLTFDEMFK TVKKEEIGNF
SNELTKEDGQ YAHIQPGMFP ESEEIMKKFG IEKTMRVLPH DQNTGGFYLA IFRKKSNKVF
VQGQEFDPSK IVPSSEDSEE GNVINNEDQE LEVDQETLQK EEFDIIKEID QQEIFEKNLQ
KTKLESKLKQ QEEQQKEKQE EKQSEKQENE AEKQEGEQKK SDKKDINLDS KYEFYEEIGE
EEFQALQRDY GLEGLDRSLL LTNKKGGQKL IKLVTPSTRD IIRSDVKEHI NYINCGSRAF
KRDSRQYSTD QCLYRICNDA IKELFPYITK RKHKISREDF LSILGKQNIK FDEIPNENYV
KQIKEMGTGS CILYFESFNG EIDAFAAQIF GSSIQYMISK ETIEGYKLIY QNKK
//
