ID A0A0J8RGI5_COCIT Unreviewed; 663 AA.
AC A0A0J8RGI5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=CIHG_01504 {ECO:0000313|EMBL:KMU83721.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU83721.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS016983; KMU83721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RGI5; -.
DR STRING; 396776.A0A0J8RGI5; -.
DR VEuPathDB; FungiDB:CIHG_01504; -.
DR eggNOG; KOG1975; Eukaryota.
DR Proteomes; UP000054563; 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 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 ECO:0000313|EMBL:KMU83721.1}; mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW mRNA processing {ECO:0000256|ARBA:ARBA00023042};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMU83721.1}.
FT DOMAIN 271..663
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 74543 MW; 79373AFEE36CDC81 CRC64;
MYDPARDSFT TSDESPSRKT GSSTKCSPFH SQGNVLGATD LDSEQGNEPH PSMLSNAIDA
TAPKPLHPIM SPVPTTVENR RHTSSKVQSN LPLDAMESSK IENSSSPSED VTAEQNSIDR
KGSQVRDAET SKDDHQNSTQ GAASPIGKTE KPVTAERASP DGAHSDKKRK LTDEPAENPA
LDKDQHRTKR KRLQERLQKN RRRGKTPPSA YSRRDDGPRI QPDARPPRSP SPITRSPSPS
AAPIRQRKRP GGGARINSAN MEALKRRQEE RERKREEEAQ RELRDRGVHD VVRQHYNAVP
ERGREWRKTD SKIKGLRSFN NWIKSTIIQK FSPDEDFLAR NNGNGWTGGP PTAPDEEKRL
IVLDVGCGKG GDLGKWQQAP QPVELYVGLD PAEVSIDQAR DRYNGMRHDR RRRRGNPLYH
AEFHVKDCFG ESLANLSIIQ RVGIDTNIGP NGSLMSSRWG GGGFDLVASM FTMHYAFESE
EKARQMLQNV AGALKKGGRF LGVGPNSDVL SAKVVEFHKK RKEQLAAAGA QEADSKEEGK
YASEVLEWGN SIYRVRFPRA TPEDGIFRPA FGWKYSYFME EAVEEIPEYV VPWEAFRALT
QDYNLELQYR KPFLDVWREE KDDPILGPLS ERMGVRSRDG TLMVNEEELE AASLYHAFCF
YKV
//
