ID A0A135UKL9_9PEZI Unreviewed; 1119 AA.
AC A0A135UKL9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NOL1/NOP2/sun family protein {ECO:0000313|EMBL:KXH60934.1};
GN ORFNames=CNYM01_11002 {ECO:0000313|EMBL:KXH60934.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH60934.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH60934.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH60934.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
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|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:KXH60934.1}.
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DR EMBL; JEMN01000458; KXH60934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UKL9; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
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:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018535; DUF1996.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR049561; NSUN5_7_fdxn-like.
DR InterPro; IPR048889; NSUN5_RCM1_N.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43662; -; 1.
DR PANTHER; PTHR43662:SF11; WSC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF09362; DUF1996; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF21148; NSUN5_fdxn-like; 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};
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}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1119
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007804975"
FT DOMAIN 678..1048
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 374..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 967
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 783..789
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 815
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 844
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 864
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1119 AA; 119916 MW; 28E21714E166E4F1 CRC64;
MKFSAATTLA ALLGAASAGS KSDDRTFAVL RFNNKQLVKT RVDPIINPGK PATHVHGVMG
GSNFGMSATG ETLSQSKCTN AMINGDNSAY WFPSLYFQDP KTKEFEAVDV FYVNVYYFFD
GTDDEIKAFP KGLQIFSGNS SARVAPSSGG KENLEPADGP IQPVQWTCPR SNYNPPSYPA
NSDGTTAGIV DPNNDGSGVG FPDQNCDGYA SPLRADVHMP SCYNPKAALT DYESMAWPSN
KGASNSRRKN CPAGWIHVPH MFFEVYWDTP KFASRWTPGQ GSQPFVLSNG DATGYSLHAD
FIAAWDETVL QQIIDNCNAG SSGMDKCPGL LKGLNTNKDC TISSPVDEVV DGLMSKLPGN
NLLTSFGAVV GGGSSSGSGS GSGSGSVASP SGSSASSAAT AASAKPSAIQ PSASKPATSG
YVSQEEVPKT SAVVSSELPI QVAPEKASTK AAETSAAVAV PTTNAVAPKP SASGCSRKTR
TVYKTVTVTS PAEESKAAAT PAGSTDNYKA RRHVHEHEHL HRHRSNRNRT PRHGCGDQRQ
YIRTAGKMSL YHEAADILSA SSDHGGSLKS RVFGKKGLKS PPAQVYALAL ETCKWSAILK
EVIEAADILR HERKLTPLLA LLLVHDFLLA KKGIALPQSH GLRTTIERHK ARLTSELTRA
RLRRKMSSLE LLRADVNANA DPEGRHPRWI RVNVLKSTVE DQLETTFKGY ERALSIEAVT
QATGKAIFID THIPFLLAAS PGTDVTKTQA YLKGEIILQD KASCFPAYLL DPHSEDGDVI
DSCAAPGNKT THLAAIAKSH EPEQGAQKQT IFAFERDSKR AQTLEKMVRI AGSRGMTKIG
PGQDFLDIDP TSDTYKDVGA LLLDPSCSGS GIVGRDSMPE LHLPEVPGPP GSKNAKGKPS
KQDDRKRKRD EKEEPGAVMV DDDGNTVEVQ SEQELQKRLD ALAGFQLTLL LHAMTFPGAK
KITYSTCSIH AEENEGVVIK ALASKVAKER GWTILPRQKQ VLGMREWPVR GLPEAAEGDE
TVAEACIRTY KGDGHGVMGF FVAAFAREEP VDGDGPYLRD DEGRIVRDMA GMPVLKSTGK
PVVLETANMS ATEEEKSSAE ESEDASDEGS GEDEWNGFE
//
