ID A0A5B0NM76_PUCGR Unreviewed; 714 AA.
AC A0A5B0NM76;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=rRNA (Cytosine-C5-)-methyltransferase nop2 {ECO:0000313|EMBL:KAA1090435.1};
GN Name=NOP2_1 {ECO:0000313|EMBL:KAA1090435.1};
GN Synonyms=NOP2_3 {ECO:0000313|EMBL:KAA1127824.1};
GN ORFNames=PGT21_001169 {ECO:0000313|EMBL:KAA1090435.1}, PGTUg99_008598
GN {ECO:0000313|EMBL:KAA1127824.1};
OS Puccinia graminis f. sp. tritici.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=56615 {ECO:0000313|EMBL:KAA1090435.1, ECO:0000313|Proteomes:UP000324748};
RN [1] {ECO:0000313|Proteomes:UP000324748, ECO:0000313|Proteomes:UP000325313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-0 {ECO:0000313|EMBL:KAA1090435.1}, and Ug99
RC {ECO:0000313|EMBL:KAA1127824.1, ECO:0000313|Proteomes:UP000325313};
RA Li F., Upadhyaya N.M., Sperschneider J., Matny O., Nguyen-Phuc H., Mago R.,
RA Raley C., Miller M.E., Silverstein K.A.T., Henningsen E., Hirsch C.D.,
RA Visser B., Pretorius Z.A., Steffenson B.J., Schwessinger B., Dodds P.N.,
RA Figueroa M.;
RT "Emergence of the Ug99 lineage of the wheat stem rust pathogen through
RT somatic hybridization.";
RL Submitted (MAY-2019) 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}.
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:KAA1090435.1}.
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DR EMBL; VSWC01000092; KAA1090435.1; -; Genomic_DNA.
DR EMBL; VDEP01000149; KAA1127824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B0NM76; -.
DR Proteomes; UP000324748; Unassembled WGS sequence.
DR Proteomes; UP000325313; 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:UP000324748};
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 296..584
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 513
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 388..394
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 412
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 439
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 456
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 714 AA; 78548 MW; 56858E70EC84AA8F CRC64;
MGGFGFKSRH KQSAPEPLRV KGQSKDPKKI DAVVAADEPS SLPKKSRSKV PRSGGKSVAS
KIKQRTLRQQ EEAKQKDLPK PKHSKKGTSE QSDSDSDDGS DKDEDDENGN EDEEHVDEGL
EEARKAFFST KDLVEPHNDM DSADDQNDFQ SASGSSHSHA ESIEELNESE AGDGIEGSAV
PDDEDDEEDN DDEASEGSDM VGEGSNDEED EDDNALDADI MNHNKGVPDL RKLYSRIQES
VRVLGNWSVL GKKAKGKSRA DVTEQTLNDV CEYFGYNAFL SDLLWQLFDP EEALAFFEAN
ETARPVTIRT NTLRTNRRDL AQSLINRGVN LEPIGKWSKV GLQVFESSVP IGATPEYLAG
HYMLQAASSF LPVIALDPQP GEKCLDMSAA PGGKTTFMSA MMKNTGKLFA NDSSKARCKS
LMANVSRMGC HNVIISNHDA RDFPKVMGGF NRVLLDAPCS GTGVISKDAS VKNNKSEKDL
LLLSHLQKQL ILSAIDSVSP HSTNGGYLVY STCSVTVEEN ESVVDYALKK RPNVKLVETG
IGFGKEGFVR FRGKIFNPSL KMTRRFYPHV HNVDGFFVAK LKVNPKAKTA PIQEEEEDDV
EETLSQDDIP DKKQKAPKAK DEPVAFDDSE DAAIIASAKI AQLKAKGIHV TRPNPEKKQS
KKHQDDQPDA TEKKQAAKQQ SDGPTLTEKV NSKKHQRDEQ DGKEKKKKTR VKAS
//
