ID A1D158_NEOFI Unreviewed; 560 AA.
AC A1D158;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=NOL1/NOP2/sun domain protein, putative {ECO:0000313|EMBL:EAW22151.1};
GN ORFNames=NFIA_008280 {ECO:0000313|EMBL:EAW22151.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22151.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22151.1; -; Genomic_DNA.
DR RefSeq; XP_001264048.1; XM_001264047.1.
DR AlphaFoldDB; A1D158; -.
DR STRING; 331117.A1D158; -.
DR EnsemblFungi; EAW22151; EAW22151; NFIA_008280.
DR GeneID; 4591638; -.
DR KEGG; nfi:NFIA_008280; -.
DR VEuPathDB; FungiDB:NFIA_008280; -.
DR eggNOG; KOG2360; Eukaryota.
DR HOGENOM; CLU_005316_7_4_1; -.
DR OMA; SFKSRIY; -.
DR OrthoDB; 102852at2759; -.
DR Proteomes; UP000006702; 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; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006702};
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 140..526
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 346..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 247..253
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 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 560 AA; 60738 MW; BADFAD078983D04D CRC64;
MSLYYDAVSV LTAPSSTGGS FKSRIYSSRN LKSSPAQIYA LVIEASKWDI LLKEVIEAAG
ILKQEPKLTP LLALLLVHDH LLAKNGIAAN ANHPLRQAIE RHKTRLKGEF AKARVRRGCA
SIPDLKAAVL REKQAAQSAL GTSSTAVYPR WVRINNLRTT MEEQLQFTFK AYTRVNSLAE
LGEKDEAKLY VDPHVPDLVA VAPGVDFTSS PAYKNGQIIL QDKASCFPAY LLLGDSEDWS
GDLLDGCAAP GNKTTHMASL LAKHAAGKGV THHIFSMDAS KVRSKTLQKM VTAAGADDIV
TVLQGQDFLA LDPTEDRFAN VTGLLLDPSC SGSGIVGRDD VPKLALPAAA STQTGKSQGK
KRKRRHDEEE ETQPGNVATS ASTSASATDE NEFASATLDP DRLTKLSNLQ ARIVEHALSF
PAATRVTYST CSIHLIENEA VVSRVLASDV ARSRGWRIMR REEQPRGMKA WPHRGVRTEG
RYGDAKGDGE AAAVDLSDEE LEACLRCWAD DEEGLGGFFV AGFVRDEGSV NRPTTEEPAS
QDTDEDTEAS DEDEWEGFSD
//
