MCES_PICGU
ID MCES_PICGU Reviewed; 580 AA.
AC A5DDJ4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE AltName: Full=mRNA cap methyltransferase;
GN Name=ABD1; ORFNames=PGUG_01345;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs.
CC {ECO:0000250}.
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:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
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DR EMBL; CH408156; EDK37247.2; -; Genomic_DNA.
DR RefSeq; XP_001485674.1; XM_001485624.1.
DR AlphaFoldDB; A5DDJ4; -.
DR SMR; A5DDJ4; -.
DR STRING; 4929.XP_001485674.1; -.
DR EnsemblFungi; EDK37247; EDK37247; PGUG_01345.
DR GeneID; 5128071; -.
DR KEGG; pgu:PGUG_01345; -.
DR VEuPathDB; FungiDB:PGUG_01345; -.
DR eggNOG; KOG1975; Eukaryota.
DR HOGENOM; CLU_020346_2_0_1; -.
DR InParanoid; A5DDJ4; -.
DR OrthoDB; 1390749at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 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; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR PIRSF; PIRSF028762; ABD1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..580
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000303913"
FT DOMAIN 230..580
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280..281
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 308
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 376
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 406
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 411
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 311
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 317
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 342
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 410
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 503
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 571
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ SEQUENCE 580 AA; 66197 MW; A0D70748CA9F672E CRC64;
MSGSKQGSEK ASITSLIDSE EQGDEATSVS TQNQSPKTQI TQTENVEVQN SDLKVTENKP
KNTEMKPTDP NTNASTTENT PITTSNAQVS EKSEKTVPAW MREPEEAQNR YDRYVPRVDN
RRRGEPRVAE VRQDPRYAKY LRQDQEERRI RRPDDEYEGD HKRRRPEMVT QFDDRRQGTR
KNHPGQAGQS ESEENGDEQQ GDDEEETPGN EEPVEAQPYS RLATSVQSTQ HYHTFQSHIA
NKENKDINSI VRSHYNQRTI QSKMQGSRTK SPIYKLRNFN NAVKYMLLGN HVRKNPNPGS
PTVILDMCCG KGGDLNKAEF VGADQYVGID ISDASVKEAF HRYRRNKARF IPRDGGRAGQ
RDSRKYNFEA CFATGDCFQQ SIPEILEPNF PGIVNGLFPV DCVSIQFSMH YSFESEERVR
TMLNNVSKSL RPGGTFVGTI PSSDFIRDKI VNKDFLPGTN NKFGNELYSV TFDRTPPSDG
IFRPPFGNKY DYFLKDAVDN VPEYVVPFEV FRSMCEEVGL TLRYKKNFIE IFNQEIPKYF
HKLNRNLVDG MKRADGKYGA EGAEKEAVSF YLGFAFEKLG
