ID N4V0C6_COLOR Unreviewed; 479 AA.
AC N4V0C6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 Name=ABD1 {ECO:0000313|EMBL:TDZ17014.1};
GN ORFNames=Cob_v010061 {ECO:0000313|EMBL:TDZ17014.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ17014.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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:TDZ17014.1}.
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DR EMBL; AMCV02000032; TDZ17014.1; -; Genomic_DNA.
DR AlphaFoldDB; N4V0C6; -.
DR STRING; 1213857.N4V0C6; -.
DR EnsemblFungi; ENH81468; ENH81468; Cob_09875.
DR eggNOG; KOG1975; Eukaryota.
DR HOGENOM; CLU_020346_3_1_1; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
DR GO; GO:0070693; C:P-TEFb-cap methyltransferase complex; IEA:EnsemblFungi.
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; 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; 2.
DR PIRSF; PIRSF028762; ABD1; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000014480};
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 BINDING 140..141
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 181
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 187
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 285
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 403
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 471
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 479 AA; 54918 MW; 950B3338594D8BE2 CRC64;
MADYHDESNE SYDARKRKRS RSPAKNGNSS RRREDENEQL PQPYNAKELQ PAKRRALSPS
EQPRKQKRPG ARARISESER EAIRQRALDR EKQLEAASHA EVERQRNIND VVTQHYNSVP
ERGRDWRRTD SKIKGLRAFN NWIKSCIIQK FSPDEDHAPG SREQGTSTEK DLLVLDIGCG
KGGDLGKWQQ APQPVELYVG LDPADISIDQ ARERYRQMGS RGGGGRGGRG GYRRPSPRLF
EARFHVKDCY GEPIEDLEIL RQVGFDTNPL SRRGFDVVSM MFCMHYAFET EKKARMMLRN
VAGSLKKGGR LIGCIPNSDV LGEHVRKFNE EAEQKKKKAA EEPPQEAEEG ELEDGEAEQS
AEWGNSIYRV RFPGKTPQDG VFRPAFGWKY NFFLDEAVEE VPEYVVPWEV LRALAEDYNL
ELQYHKTFME VWDSEKDDET LGPLSERMGV RERGGGRLLV SPEEMEAASF YSAFCFYKV
//
