ID A0A5C3E3D4_9BASI Unreviewed; 662 AA.
AC A0A5C3E3D4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Probable NOP2 - nucleolar protein {ECO:0000313|EMBL:SPO24625.1};
GN ORFNames=UTRI_01589_B {ECO:0000313|EMBL:SPO24625.1};
OS Ustilago trichophora.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=86804 {ECO:0000313|EMBL:SPO24625.1, ECO:0000313|Proteomes:UP000324022};
RN [1] {ECO:0000313|EMBL:SPO24625.1, ECO:0000313|Proteomes:UP000324022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC100155 {ECO:0000313|EMBL:SPO24625.1,
RC ECO:0000313|Proteomes:UP000324022};
RA Guldener U.;
RL Submitted (MAR-2018) 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|PROSITE-ProRule:PRU01023}.
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DR EMBL; OOIN01000008; SPO24625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C3E3D4; -.
DR Proteomes; UP000324022; 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 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; 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; 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:UP000324022};
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 312..600
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 404..410
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 428
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 455
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 472
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 662 AA; 73151 MW; 2590E4A3F0E42381 CRC64;
MGRRSKNKQA PPQPLPEDRP VNKGKRKAPE SSVPAKKAKT STTAAASARG AHGKARATAS
ANASSSKVGV NGKSKARAAP VELQENEDED DEEDEEVEED EEEEEEEEEE EDEEEEEDPL
AALGLPKNGK LTDRQRKKAL AEAERLEELL KSQGLSLDSD DDEEEAGEGS ELEEADDDEG
SEQELGDEFD LGEDDEDLDA EEGDEVELDG EDDEDEDEDE DDSEAGGAEF MLPTLEEREA
EKMRGADLQL VHMRIQEIVT VLSNFKKLAI DGRSRSEYVE QLLADICTYY GYNAFLAEKL
FELFTPAEAI EFFEANETPR PVTIRANTLR TRRRDLAQAL INRGVNLEPI GAWSKVGLQV
FESSVPIGAT PEYLAGHYML QAASSFLPCI ALAPQPNERV LDMASAPGGK STYLSALMQN
TGTVFANDSN KNRIKSLVAN IHRLGCKNVV VCNYDGRQFP KVIGGFDRVL LDSPCSGTGV
IHKDQSVKVN KSERDFALLT HLQKQLLLCA IDSVNPRSST GGYVVYSTCS VMVEENEEVV
QYALRKRSNV KIVDTGIQFG RDGFKSFGRS KFDERMVYAR RIFPHVHNLD GFFVCKLKVN
PPSNNAHSKS EKKESKSTAA ANVEGDEEEQ EAVEADDGLV SLDNPEDQKL MQKSLKKAKS
RR
//
