ID A0A099NWZ0_PICKU Unreviewed; 433 AA.
AC A0A099NWZ0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=JL09_g4412 {ECO:0000313|EMBL:KGK36447.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK36447.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
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:KGK36447.1}.
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DR EMBL; JQFK01000070; KGK36447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099NWZ0; -.
DR VEuPathDB; FungiDB:C5L36_0A00730; -.
DR eggNOG; KOG1975; Eukaryota.
DR HOGENOM; CLU_020346_2_2_1; -.
DR Proteomes; UP000029867; 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; 1.
DR PIRSF; PIRSF028762; ABD1; 1.
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 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 109..433
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 14..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..159
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT SITE 183
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 189
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 214
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 263
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 357
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 425
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 433 AA; 50074 MW; 0C87777588080B7A CRC64;
MSFYNDDASR YKRRRVVKNR VGSSRRRTTD IEQTPNEANE DGDQNGNNNE LLSNEKTNMT
VSTPDVLKEK PVWMSDAEWA IQQASVKRAI EPLVQGDKDD KEVDKMAYED INVKMKYLKD
IKDSGKDEIV KEYYNTQTFH SRQSKRTESP IYRLRSFNNC IKYILINKYG IPEGSTLDLG
CGKGGDLAKW GMNNTRQYVG IDLSDESIRE AIKRYKNGRY SFQAVFATGD AFKVELPEIL
KDFSMEQVSF LQFDNISMQF CMHYAFSSEA SVESMLNNVS KSLRVGGMFV GTIPSSDFIK
WKINKMKEGE KGWGNSLYSV TFPDLEGCWD REKKNFKKPF GNVYNYFLKD AVEDVPEYVV
PFEKFRSMCE DHGLELRYKK NFFDMFNKEI ATFFPMLPGP LVQSLRQEDG TYGVSGEERE
ACSFYLSFAF ERV
//
