ID A0A0D9QQD6_PLAFR Unreviewed; 1098 AA.
AC A0A0D9QQD6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00011926};
DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
GN ORFNames=AK88_00972 {ECO:0000313|EMBL:KJP89310.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP89310.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP89310.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ001652; KJP89310.1; -; Genomic_DNA.
DR RefSeq; XP_012334037.1; XM_012478614.1.
DR AlphaFoldDB; A0A0D9QQD6; -.
DR EnsemblProtists; KJP89310; KJP89310; AK88_00972.
DR GeneID; 24266286; -.
DR VEuPathDB; PlasmoDB:AK88_00972; -.
DR OMA; NFECLIN; -.
DR OrthoDB; 276948at2759; -.
DR Proteomes; UP000054561; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 715..1098
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 127561 MW; 2DA1EFBB8573F8D2 CRC64;
MMSENLNEDP ENINDANEHG DKFTNRANNV SEVNATGTEE AGEKDTSITG EKGNPKKRGT
EGNGEDSFRP SSPPHVKRKK DSAEYSQQGE KQSKGLRENA KKRGDAADVG ESKNSGKNKN
EEKKIFIDKN NLFHEINLLI KKKLKIHDAI KIDLFYKDNC TQIKPYAIFD EYKYVNIENK
INLEIVNFLR KSLQSEERKQ FLSIHSSVVE LRGSFNDELI NLPIVNQIIL QKISNNNYKY
KFNIDTEVLN YIYVDLFKIH KSKYKFKILE KKYELEEWYY YDTRKDRRKG GGTAQVIGEA
TAAEQEPVQE DEAADQKREE NKNDDQTRHE RASEQSDLEE NSTSSESNES DALINLYNEE
KKKEEMQLLN GKTRRKKKRK KRKKKIVDKD KVYMEKLKKL VEEDSDNEAN ATSSEHNSTE
SDDSSNDRNQ ILYRRKIIYS RDGDGTVISA FKEVESDTVC VYYPNSSYNQ CLNLSSFEPL
LGGVPSTEVP VPDGTNRPSV QRRTYDIYQH KNGQRVVGVS AGSNAGEPPN LQALHEENIR
IQKRYVRDIS IYNFCCDDKY KGCSLFLHVA KNKKLKNVNI DYNIDYSDFS SNLDIIKMYE
VKGEASASAK GVENRRKDVG KLFELEKDWK VNVDMYIDIE RVVREFRKGE EGSNIGQVSG
VSGGDDGDGD GNEDGCGDGR EKLDQREGRS NKLDYVIYNF YKNFECLINL LNKLKNNTTK
FDYFYPKMIG DVNEEIRKHY DKKKVILLKK SNIKYIRIFN NEVKRLMILF FVPYGSKILD
LACGHGQDML KYNTVKNKVY VGLDISKKEI ELAKERLSQN DVKGLCNHDN FLFLQGDILN
NKFFRKWKNK NITFDIISIN LAMHYVVYNE KSSKKFFKII ENFLESEGLL LATTISTITL
ADFLMKRSVT EVVSDSITLT LANDLFTIRF DQENLLKIFK NKMCLDEFIE FVNSNSTVSQ
VKYDYFHNLI KNALENTLGI KYYFYLYDTI DANEFVIPQK YLKHKLQELN MVELFNNSAI
MFLHYITNNL ETYEKYQNIN YFNLINKTIN KYIFDDIKMR INKIHGYNRD SQIYFDICSL
YHVYVYKKNF DASILGVV
//