ID A0A0G4KLR8_9PEZI Unreviewed; 478 AA.
AC A0A0G4KLR8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|ARBA:ARBA00021751};
DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00032772};
DE AltName: Full=mRNA cap methyltransferase {ECO:0000256|ARBA:ARBA00033387};
DE Flags: Fragment;
GN ORFNames=BN1708_002253 {ECO:0000313|EMBL:CRK09727.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK09727.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK09727.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK09727.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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)-(ribonucleoside) in mRNA +
CC S-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:0000256|ARBA:ARBA00024288};
CC -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
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DR EMBL; CVQH01002224; CRK09727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4KLR8; -.
DR STRING; 100787.A0A0G4KLR8; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR016899; mRNA_G-N7_MeTrfase_euk.
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; 2.
DR PIRSF; PIRSF028762; ABD1; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042, ECO:0000256|PIRSR:PIRSR028762-
KW 2};
KW mRNA processing {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|PIRSR:PIRSR028762-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 99..478
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137..138
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 178
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 184
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 211
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 282
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 402
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 470
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT NON_TER 478
FT /evidence="ECO:0000313|EMBL:CRK09727.1"
SQ SEQUENCE 478 AA; 54343 MW; E44BAC2944E3FCA5 CRC64;
MADDRYGYEG NPQPYSANNL DPPRKRKADN AEELPQPYNA KELQPAKRRA MSPNEHQPRK
QKRPGARARI SEAEREAIRQ RALDRDRALE AAASAVPLEP RQRGINDVVT QHYNSVPERG
RDWRRTDSKI KGLRSFNNWV KSCIIQKFSP DEDYTPASRE QGRSGGHELL VLDIGCGKGG
DLGKWQQAPQ PVQLYVGLDP ADVSIDQARE RYRQMSSRGG GGRGGRGGHR RPPPRIFDCQ
FHVKDCYGES IEDIDVVRQV GFEPGPINRR GFDVVSMMFC MHYAFESEEK ARTMLRNVAG
ALKKGGRLVG CIPNSDVLGE HVRKFNERMK EKKRLKEENP EPPAEAEDGE LEEGEAEETA
EWGNSIYRVR FPGKTPEDGI FRPAFGWKYN FFLDEAVEEV PEYVVPWEAF RALAEDFNLE
LQYQKNFMDV WNSEKGDPTL GPLSERMGVR ERGGGDLLVS PDEQEAASFY IAFCFYKV
//
