ID A0A010RJW5_9PEZI Unreviewed; 889 AA.
AC A0A010RJW5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=NOL1/NOP2/sun family protein {ECO:0000313|EMBL:EXF78169.1};
GN ORFNames=CFIO01_11685 {ECO:0000313|EMBL:EXF78169.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78169.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF78169.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF78169.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:EXF78169.1}.
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DR EMBL; JARH01000659; EXF78169.1; -; Genomic_DNA.
DR RefSeq; XP_007598179.1; XM_007598117.1.
DR AlphaFoldDB; A0A010RJW5; -.
DR STRING; 1445577.A0A010RJW5; -.
DR KEGG; cfj:CFIO01_11685; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_2_1; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 65..480
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 184..190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 308
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 889 AA; 98804 MW; 8E94C0E364A1BFC4 CRC64;
MGRKFRGGKK GKSRGGSNAE GGGDRGRQPR SESWQNYPAV KKENERLQRY YNTIFGLSEE
EQGPFWDALR RDLPNSFRFC GSKGHALAVK KLLQTRYMPE IQNIQHADGR TVEPPKPLSW
YPNELAWWMT TPKNIIRKYP PFAAFQKFLV SETTVGNISR QEVVSMIPPL LMDVRPGMTV
LDMCAAPGSK AGQLLEMIHQ GEEARVRKVL RAFAKEDGLD LGDETEEERQ ADLSADPSDS
GRTTGLLIAN DSDYKRGHML VHQLKRLGSP NLLVTNHDAT QYPAIRLPPS PETPTKPRYL
KFDRILADVP CSGDGTLRKN MNLWKDWQPG SALGLHVTQV RILLRALAML KVGGRVVYST
CSMNPVENES VVAAAIDRAG GPDKVEIVDC SNELQGLVRA PGMKKWQIMD KSGRLWSSQA
EVDEWTKNST EGVAPGRLVE TMFPPLEGSV CADLPLERCM RVYAHQQDTG GFFITVLQKK
AEVKIRPEDQ KQGDESTKSN GATAAATPAE ATPATETDNA ETNMEVDVPV KTEEAVEAAP
EAALETAPET TTEATEEVKS EEKAEEAEQD ATNGVKRPRE DETADGETQE TKKAKLETTT
QEKPKNSNRN IHGRVEEPFK YLDPKHEVIK NIRDFYHISS RFPDDRYMVR NATGEPAKAV
YYTSALARDI LTENEGRGIK VIHGGVKMFM KQDAPSAEIC RWRIQSEGMP ILQGYVGEQR
VVRLTKKETL RRLLIEMFPR IADGEWEQMG EIGERVRDIG MGCCVLRVEP DGSDPAFSER
MALPLWKSIH SLNLMLPKED RTAMLLRIFD DTTPLINNSL QKQRAIDEAA RKKAAAEDAY
VAEKELIDIE DAPTPEEMDL EPAPAAAAAA EAEDADAAAI AAAPTTEEA
//
