ID MCES_ASPFU Reviewed; 668 AA. AC Q4WN42; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 04-NOV-2026, entry version 114. DE RecName: Full=mRNA cap guanine-N(7) methyltransferase; DE EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148}; DE AltName: Full=mRNA (guanine-N(7))-methyltransferase; DE AltName: Full=mRNA cap methyltransferase; GN Name=abd1; ORFNames=AFUA_6G07690; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). CC -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; CC Evidence={ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE- CC ProRule:PRU00895}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU00895}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000006; EAL88622.1; -; Genomic_DNA. DR RefSeq; XP_750660.1; XM_745567.1. DR AlphaFoldDB; Q4WN42; -. DR SMR; Q4WN42; -. DR FunCoup; Q4WN42; 1017. DR STRING; 330879.Q4WN42; -. DR EnsemblFungi; Afu6g07690-T; Afu6g07690-T-p1; Afu6g07690. DR GeneID; 3508761; -. DR KEGG; afm:AFUA_6G07690; -. DR VEuPathDB; FungiDB:Afu6g07690; -. DR eggNOG; KOG1975; Eukaryota. DR HOGENOM; CLU_020346_3_0_1; -. DR InParanoid; Q4WN42; -. DR OMA; AAEWDIV; -. DR OrthoDB; 10248867at2759; -. DR Proteomes; UP000002530; Chromosome 6. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central. DR FunFam; 3.40.50.150:FF:000231; mRNA cap guanine-N7 methyltransferase; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom. DR InterPro; IPR039753; RG7MT1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1. DR PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1. DR Pfam; PF03291; mRNA_G-N7_MeTrfase; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51562; RNA_CAP0_MT; 1. PE 3: Inferred from homology; KW Methyltransferase; mRNA capping; mRNA processing; Nucleus; KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..668 FT /note="mRNA cap guanine-N(7) methyltransferase" FT /id="PRO_0000303902" FT DOMAIN 310..668 FT /note="mRNA cap 0 methyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT REGION 1..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 524..547 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..19 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 44..65 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..88 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 100..129 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 148..157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..279 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..547 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 319..320 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 323 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 366 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 390 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 428 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:O43148" FT BINDING 471..473 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 476 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:O43148" FT SITE 369 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 375 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 402 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 475 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 592 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 660 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" SQ SEQUENCE 668 AA; 74939 MW; 0BA01453C114F2E7 CRC64; MYDPARDSWE ERDGDEARSC RGRLASDQPH AVFSPPEQIH GASGENNNTT DLQQHPDPSS KTTASAEVLY AESQPAQPTT QTPPSVSTRI QSPVDPAAQK ASNPQSLTST AQNQLNKSNT TMENTSGSAT PKPRADPSDK PNRPVQVASP TDQNGSQGDK KRKLPAEENA SEKSQPAPDR PVSKRKRMEE RHQKLRKRGR TPPSAYSRRD AEETSSAADR NGPTYRSTSP LPPPRSPTPE DQPRQRKRPG GGARMGLVDR ETLRRRQEER ERAQVEEAMR ASQSRGVADV VRQHYNAVPQ RGREWRKTES KIKGLRSFNN WVKSTLIQKF SPDEEFLARF NGTKEWAEDG GVPPVEEKRL LVVDLGCGKG GDLGKWQLAP QPVDLYVGLD PAEVSIVQAR ERYNGMKSGR GNRGRRNPIF HAEFRPKDCF GEWLGDVDIV QQVGIDPNVG PGGSVMSSRW GGGGFDVVAS MFTIHYAFES EEKARQMLRN VAGCLKKGGR FLGVCPNSDV ISARVSEINA KKKARQAQAK KEKSDEAPED GEVEEDDGKV EWGNQIYRVR FPITPPEDGV FRPPFGWKYS YFMEEAVEEV PEYVVPWEAF RALTEDYNLE LQYRKPFLDI WRDEKDDPEL GPLSERMGVR DRVTGKLLMT EEEKEAASFY HAFCFYKV //