ID A3M089_PICST Unreviewed; 625 AA.
AC A3M089;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Nucleolar RNA methyltransferase {ECO:0000313|EMBL:ABN68674.1};
GN Name=NOP2 {ECO:0000313|EMBL:ABN68674.1};
GN ORFNames=PICST_91345 {ECO:0000313|EMBL:ABN68674.1};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68674.1, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68674.1, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000502; ABN68674.1; -; Genomic_DNA.
DR RefSeq; XP_001386703.1; XM_001386666.1.
DR AlphaFoldDB; A3M089; -.
DR STRING; 322104.A3M089; -.
DR GeneID; 4840914; -.
DR KEGG; pic:PICST_91345; -.
DR eggNOG; KOG1122; Eukaryota.
DR HOGENOM; CLU_005316_3_2_1; -.
DR InParanoid; A3M089; -.
DR OMA; PIGSWTK; -.
DR OrthoDB; 1268at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
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:UP000002258};
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 272..560
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 364..370
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 388
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 415
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 432
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 625 AA; 70234 MW; 7AFDECFC1C7DF367 CRC64;
MGRRAKNKQG VPPSFEEFQA KKEKRDKKRK LADEPERPAK ATKKSKDDYK NNKEANNKKK
TSNNKKKQSV EDEFEEPEDL PEVDLEELSN AKKALFDDSD EEEGLDALED DEEVGNDDEF
EIEDGEEFYD SDEEERAKPM FSDDEDEDIE DLNAANMEAF SRKLDEEAEL EAEEAEKELL
ESQTNQPRAK VLPSAEEAQI MEQGPQDVTM VRTRMIEIVK VLENFKDLAE EGTSRNDYIS
RLLKDICEYF GYSEFLAEKL FNLFSPSEAM EFFEANEIAR PITIRTNTLK TRRRDLAQTL
VNRGVNLQPI GSWTKVGLQV FDSQVPIGAT PEYLAGHYIL QAASSFLPVI ALAPQENERV
LDMAAAPGGK TTYISALMKN TGCVFANDAN KARTKSLIAN IHRLGCKNTI VCNYDAREFP
KVIGGFDRVL LDAPCSGTGV IAKDESVKVS RTEKDFIQIP HLQKQLLLSA IDSVDANSAT
GGIIVYSTCS IAVDENESVV DYALRKRPNV KLIEAGLEIG KEGFTSYRGK HFNPSLNLTR
RYYPHTYNVD GFFVAKFKKI AASPHDVSKA GAKEKESIAR AEAEEEGIIH DDFAEFENDE
DKSLIDQSVK RNLKRKGINP NAAKK
//
