ID A0A178DPR3_9PLEO Unreviewed; 467 AA.
AC A0A178DPR3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=IQ07DRAFT_237139 {ECO:0000313|EMBL:OAL44773.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL44773.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL44773.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL44773.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441660; OAL44773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DPR3; -.
DR STRING; 765867.A0A178DPR3; -.
DR InParanoid; A0A178DPR3; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000077535; 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; 3.
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:UP000077535};
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 50..467
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..100
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 126
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 132
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 158
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 224
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 391
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 459
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 467 AA; 53171 MW; 6BD877A705849295 CRC64;
MSGNAPDRGR KRSLSRSRSR SPPRQRKRPG AAARLSAADR DAVRKRQQER EQEAERRAQA
EAASRGVHDV VKQHYNMVPE RGREWRQTDS KIKGLRSFNN WVKSSIINKF IGDERNLKIL
DIGCGKGGDL QKWQASRKVE LYVGCDPADV SIKQAKDRYA QMLKRSRRIF HAEFYAKDCF
GEWLGDIPII KDVGIDPGAG PGNAMAQRWG GGGWDMVTMM FCMHYAFESE AKAKGMLRNV
AGALKKGGRF IGCIPNSDVL TRKVIEYHKA KGTAIEEPQG AADEEDDRPT FASDDEDDWD
PEKSLDSPKP NESEHANGDS SKDKSKDQEG KDNQEKKEGQ EDGEVEEEGF SWGNSIYRVK
FPGKTPTDGV FRPPYGWKYS YFLEEAVEAP EYVVPWEAFR ALAEDYNLEL QYRRPFREVW
DEQKNDPELG PLSERMGVRD RVTGQLLTSE EELDAADFYH TFCFYKV
//
