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Database: UniProt
Entry: A0A094I0A9_9PEZI
LinkDB: A0A094I0A9_9PEZI
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ID   A0A094I0A9_9PEZI        Unreviewed;       557 AA.
AC   A0A094I0A9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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};
GN   ORFNames=V498_06238 {ECO:0000313|EMBL:KFY89947.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY89947.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY89947.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
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:KFY89947.1}.
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DR   EMBL; JPKA01001518; KFY89947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094I0A9; -.
DR   HOGENOM; CLU_020346_3_1_1; -.
DR   Proteomes; UP000029270; 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; 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   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};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00023042};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          145..557
FT                   /note="MRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51562"
FT   REGION          1..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  61279 MW;  F67B42127ED3D584 CRC64;
     MASNGPVEVS EPQPQPFNAN KLEPAKRRNR TTSSATSTPT HVKSDAGESN PNDTKSKGPY
     EPQPEPFDAT KLEPARKRRR SSISPSRSTP RRDERPSSPK PAAAAAPPAN TGDDDDEDRP
     RKKRPTGRAR ITDTERDEIR QRQQQREKEQ RDAIAAHNAR GIHDAVRQHY NAVPERGRDW
     RRTDSRIKGL RSFNNWIKST IIQKFSPNED FTPGGQQPEY GAPPVKGLLV LDMGCGKGGD
     LGKWQQAPQP VDLYVGLDPA DVSIGQARER YSQMASRGGG GRGGRGGRGG YNNRPPPRLF
     HGEFAVQDCF GESIEKVPIV REVGFDASGG PSRFGGGQFD VVSMMFAMHY AFESEHKARI
     MLKNVAGALK KGGRFIGCIP DSDVLSARAV EFNEHQAAKK AAAPAQVDGA EEGKPAAAPA
     ATVGAEPADL DEGEIAETAE WGNDIYRVRF AGQTPADGVF RPPFGWKYNF FLHEAVEEVP
     EYVVPWEAFR AIAEDYNLEM QYHKSFGEIW RSEKDDPVLG PLSERMGVRG RGGGGLLVSD
     EEMEAAEFYV AFCFYKV
//
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