ID A0A0F4Z7A1_9PEZI Unreviewed; 455 AA.
AC A0A0F4Z7A1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|ARBA:ARBA00021751, ECO:0000256|PIRNR:PIRNR028762};
DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926, ECO:0000256|PIRNR:PIRNR028762};
GN ORFNames=TD95_001399 {ECO:0000313|EMBL:KKA26382.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26382.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA26382.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26382.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR028762}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family.
CC {ECO:0000256|PIRNR:PIRNR028762}.
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:KKA26382.1}.
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DR EMBL; LAEV01002193; KKA26382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4Z7A1; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd02440; AdoMet_MTases; 1.
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 ECO:0000256|PIRNR:PIRNR028762};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|PIRNR:PIRNR028762};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR028762};
KW Nucleus {ECO:0000256|PIRNR:PIRNR028762};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR028762};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR028762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR028762}.
FT DOMAIN 75..455
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..125
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 159
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 165
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 192
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 251
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 379
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 447
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 455 AA; 52721 MW; 9A9DC2C58D98E7DF CRC64;
MSDSHNSKRK RSPSPLHNTD DLPQPYNAQS LQPAKKRAIS PSEQPRKQKR PQTRSHMTSA
DREAIRQRQI EREREREREL TVQEERFRHR GINDVVRQHY NNVPERGRDW RKTDSKIKGL
RSFNNWVKSC IIQKFSPDEY WRPGDRREPL RVLDIGCGKG GDLGKWQQAP QPLDLYVGLD
PADVSISQAH DRYRQMQNNR RRGRLFEGRF MVKDCFGESL EDIEIIRQVG WDQPPGSQRG
FDVVSMMFCM HYAFESEVKA RQMLKNVASS LKKGGRFLGC IPNSDILSER VREFNASRAA
SKAAAAEAKK NEQAEQGEEG EEGEAGEDGE VEEEKTAEWG NSIYRIRFPT KTPDDGIFRP
AFGWKYNFFL DEAVEEVPEY VVPWEAFRAL AEDYNLELQY HKTFEDVWEA EKDDAVLGPL
SERMGVRNRG QGTLQMSADE VEATRIYVAF CFYKV
//
