ID A0A3M7BFV9_HORWE Unreviewed; 338 AA. AC A0A3M7BFV9; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 02-JUN-2021, entry version 11. DE RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|ARBA:ARBA00018112}; DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926}; DE AltName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|ARBA:ARBA00021751}; DE AltName: Full=mRNA cap methyltransferase {ECO:0000256|ARBA:ARBA00018092}; DE Flags: Fragment; GN ORFNames=D0865_13055 {ECO:0000313|EMBL:RMY38576.1}; OS Hortaea werneckii. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea. OX NCBI_TaxID=91943 {ECO:0000313|EMBL:RMY38576.1, ECO:0000313|Proteomes:UP000270230}; RN [1] {ECO:0000313|EMBL:RMY38576.1, ECO:0000313|Proteomes:UP000270230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EXF-151 {ECO:0000313|EMBL:RMY38576.1, RC ECO:0000313|Proteomes:UP000270230}; RX PubMed=29764372; DOI=10.1186/s12864-018-4751-5; RA Gostincar C., Stajich J.E., Zupancic J., Zalar P., Gunde-Cimerman N.; RT "Genomic evidence for intraspecific hybridization in a clonal and extremely RT halotolerant yeast."; RL BMC Genomics 19:364-364(2018). CC -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs. CC {ECO:0000256|ARBA:ARBA00003378}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973, CC ChEBI:CHEBI:143974; Evidence={ECO:0000256|ARBA:ARBA00000033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971, CC ChEBI:CHEBI:143975; Evidence={ECO:0000256|ARBA:ARBA00000905}; CC -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA CC guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}. 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:RMY38576.1}. 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; QWIN01001619; RMY38576.1; -; Genomic_DNA. DR Proteomes; UP000270230; Unassembled WGS sequence. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom. DR InterPro; IPR039753; RG7MT1. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR12189; PTHR12189; 1. DR Pfam; PF03291; Pox_MCEL; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51562; RNA_CAP0_MT; 1. PE 3: Inferred from homology; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 93..338 FT /note="MRNA cap 0 methyltransferase" FT /evidence="ECO:0000259|PROSITE:PS51562" FT REGION 1..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 49..68 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 84..111 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 338 FT /evidence="ECO:0000313|EMBL:RMY38576.1" SQ SEQUENCE 338 AA; 37213 MW; 612A6F070320C7C4 CRC64; MAGDDLPSNV TAPRPIQKRK RPQDNAARAN KSARTSTPNA YARRTPPPEP KPIDPEQEDN DGDQSPPRKL KRPGAGARVA REQRQAAEAV RHRREEDQRR QAQEERQRSG ADLVAEHYNA VPQLGREWRK TDSQIKGLRN LNNWIKSTLI QKFARPETIP QHGYLVLDMA CGKGGDLGKW SKASPPPGLY VGCDIADVSI EQARGRWAET RRKVMDAEFY VQDTFGRPLF EVPIVRQVGF NPNCGPGNGI IQGGMPTGGF DVVSMMFALH YSFEREDLAR GMLKNVAGAL KKGGRFIGCM PNSDVISATV KRSLQAEAPG TTPARKSATP ARTAEADA //