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Database: UniProt
Entry: C4R2N3_KOMPG
LinkDB: C4R2N3_KOMPG
Original site: C4R2N3_KOMPG 
ID   C4R2N3_KOMPG            Unreviewed;       436 AA.
AC   C4R2N3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   OrderedLocusNames=PAS_chr2-2_0167 {ECO:0000313|EMBL:CAY69757.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69757.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY69757.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY69757.1; -; Genomic_DNA.
DR   RefSeq; XP_002492037.1; XM_002491992.1.
DR   AlphaFoldDB; C4R2N3; -.
DR   SMR; C4R2N3; -.
DR   STRING; 644223.C4R2N3; -.
DR   EnsemblFungi; CAY69757; CAY69757; PAS_chr2-2_0167.
DR   GeneID; 8198743; -.
DR   KEGG; ppa:PAS_chr2-2_0167; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   InParanoid; C4R2N3; -.
DR   OMA; SFKSRIY; -.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000000314; Chromosome 2.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR048889; NSUN5_RCM1_N.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF21153; NSUN5_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
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:UP000000314};
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          127..433
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        353
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         227..233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         298
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   436 AA;  49854 MW;  50883D20518FEAEB CRC64;
     MNLYREAEQF IEHNPKSGSL QNRIFDASRN KKIKNNPKHV YALVYSASRY KKFLKQIIRN
     SKLLEDKKIR AKEPLLILMA HDLLFSKNGR IQSGKHPLKD AFLAHKTRLQ AELTKLKIKY
     KVKDLEELIE DDDTPVRWVR ANLLKTSREK FLNEFKHLIQ VESFQELEVG KIYHDQYIPN
     LFGVHPREKI TSTDAYLKGR LIIQDRASCF PAHILHPSPG DKIIDTCSAP GNKTTHLASY
     LGNRPDSIIA FEKDPKRAEV LKTLCAKAGG LSCIDIQVGD FTATNPEDYT DIDGFVIDPS
     CSGSGIFGRA FEENEQDETY DDTRLSKLAS FQFTIVRHAM MFPNAKKLTY STCSVHPQEN
     ERVVVDLLKD SQVQAKGWKL CTRDEVIPDW NRRGFEEEFS TFENPKELAE GCIRSKPKED
     GGIGFFVVAF KRDIGI
//
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