ID A0A1B9IR42_9TREE Unreviewed; 854 AA.
AC A0A1B9IR42;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=L486_04043 {ECO:0000313|EMBL:OCF58016.1};
OS Kwoniella mangroviensis CBS 10435.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF58016.1, ECO:0000313|Proteomes:UP000092583};
RN [1] {ECO:0000313|EMBL:OCF58016.1, ECO:0000313|Proteomes:UP000092583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF58016.1,
RC ECO:0000313|Proteomes:UP000092583};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Kwoniella mangroviensis CBS10435.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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}.
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DR EMBL; KI669462; OCF58016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9IR42; -.
DR STRING; 1331196.A0A1B9IR42; -.
DR Proteomes; UP000092583; 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 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000092583};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 529..854
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 94940 MW; F6D471B55FFCC649 CRC64;
MVYDPIRDCE VPSPSVVRND PFKYPTPPSG YGGGYDRDRD EVMSNGGRPS LTQHSSSYSP
PPPSGPGPSN LRGLLNDGPT SESRRGSDRT ASISSMPEEG DEGAGSSRHH IHRLLNNTST
QPISKTNSNS SLPRSSPSNP SPGSRSHMLD PNGFLTPATP ASAYPRSRST TSRSPHPPTQ
MSPQRASVPL PLQQSHDQGY SPQYGEPSHI YRRDSTASLV GQRPMLPPQQ PIHPHEMYGY
EQRTPGGGHY QNLPMRSPSI SVSPRSQHQS LPHTSSRPGS ASSASHPFGY QPYPQATAIS
PSTSTRRLSE DQPRPTSSSS AIGRRYTDPN AQIPTPARRS SQTSTTGYPA PRLTPIRSPS
PVVRGIPYNP NRLSAPVNVT RPIEADELAY YRSLSQQNNP LRKRKPKRPL PSWSGPSPGP
RSSFPNEEGT SYFPPQQNQN EDDPARYNRS QSYADDRASI GRHPSVTPTP GSAYGGGGHG
VYPPAFDDPL ATPGALPRGG TLTRGRRPTG NGVENHLKRP SERDEDEYNG HDVQRRKVSE
RQYVGNNAAV ADHYNSRPEV GVEGREFSPI IGLKKFNNWI KSVLIGKFAH RPQGKILDIG
CGKGGDLNKW KQARIMLYVG LDLAETSVQQ AAERYQRMQG RFDGFFFAYD CFSKPLGDIL
PEQLQQKDLY DNVTMQFCMH YAFESASKVR MMIENVSRYL RKGGIFIGTI PNAELLLSKL
NELPEDDEEL RFGNSCYYVQ FSERKHKGIY GHQYRFFLMD AVEDVPEYVV DWENFVNLAM
EYRLRLIYKK PFHDILQEEK ESRDFGPLLG KMGVVNDQGE SSMDEDQWEA ASECKLLLCM
PVGLEKGQDN MLII
//
