ID A0A078AFW0_STYLE Unreviewed; 709 AA.
AC A0A078AFW0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Ribosomal rna methyltransferase nop2-like {ECO:0000313|EMBL:CDW80726.1};
GN Name=Contig11261.g12031 {ECO:0000313|EMBL:CDW80726.1};
GN ORFNames=STYLEM_9730 {ECO:0000313|EMBL:CDW80726.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW80726.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW80726.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW80726.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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}.
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DR EMBL; CCKQ01009257; CDW80726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078AFW0; -.
DR EnsemblProtists; CDW80726; CDW80726; STYLEM_9730.
DR InParanoid; A0A078AFW0; -.
DR OMA; FRNIMTG; -.
DR OrthoDB; 1268at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
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; IPR023273; RCMT_NOP2.
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 PRINTS; PR02012; RCMTNOP2.
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:UP000039865};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
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 187..474
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 279..285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 709 AA; 81451 MW; 1938FB3F4187C7C5 CRC64;
MSSSEDYDEE ANSSQQEEDE VQLDSQDDEE LDEDLDDEGL DDDEEGEGED EDEEMDDDES
AEESEEKPKA KAQKKPAQVQ QSTTQDDYDE DEYNDDVADE EAITNIEAKR DKMIKDLLSK
EDLGIIQMRL KETVKVLTNF KDLRDPNKTR QDYLEELRND ICAAFDYNPD LVELLLDLFP
PSECIEFIEA NENQRPMTIR TNTLKTKRKD LAKTLIQRGV NLDPVAEWSK VGLKIYDSQV
PIGATPEYLA GHYILQSASS FLPVIALAPQ PNEKILDMAA APGGKTTYIA QLMKNTGILM
ANDLKKERLK SLNANLHRLG VSNCVVMNYD GRKIPQIFNK FDRVLLDAPC SGLGVIARDP
SIKVQKTRDD VKKLSHLQKE LIKAAIDSVD AHSKTGGYIV YSTCSISVEE NEWVVDYALK
TRYVKLVESG VEVGEPGFTK HKEKRFHPSL NLTRRIYPHT HNMDGFFVAK LKKFANGEKN
AEENVVNPEE LERKIKQQEE QKKKKLNQKK KKQRKEKKNK NKQGDDKKEK KEGEDNKSTD
KTEKSESNGE KKEKKNKKDK KDKKDKKKDK KRPAEQTTES LEKSVKQTDA KTNDKKQGDE
KTQKNKDQKS DKKESQSQPN KSADKKEQQK QPEQKQQAAV VKQDKNQKQQ QQAPKQEQKQ
QQPQKQEQKP QKQQEQPKAK VEQQPVKKAE VKAQEKQQQK DKMHKKQHK
//
