ID W2L3X0_PHYPR Unreviewed; 603 AA.
AC W2L3X0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=L914_09531 {ECO:0000313|EMBL:ETM45395.1}, L915_09664
GN {ECO:0000313|EMBL:ETK85545.1}, L916_09567
GN {ECO:0000313|EMBL:ETL38974.1}, L917_09492
GN {ECO:0000313|EMBL:ETL92096.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL92096.1};
RN [1] {ECO:0000313|EMBL:ETL92096.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL92096.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETK85545.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK85545.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETL38974.1, ECO:0000313|Proteomes:UP000053864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL38974.1,
RC ECO:0000313|Proteomes:UP000053864};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ETM45395.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM45395.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica IAC_01/95.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
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DR EMBL; KI686553; ETK85545.1; -; Genomic_DNA.
DR EMBL; KI673198; ETL38974.1; -; Genomic_DNA.
DR EMBL; KI679946; ETL92096.1; -; Genomic_DNA.
DR EMBL; KI693148; ETM45395.1; -; Genomic_DNA.
DR EnsemblProtists; ETK85545; ETK85545; L915_09664.
DR EnsemblProtists; ETL38974; ETL38974; L916_09567.
DR EnsemblProtists; ETL92096; ETL92096; L917_09492.
DR EnsemblProtists; ETM45395; ETM45395; L914_09531.
DR VEuPathDB; FungiDB:PPTG_01374; -.
DR Proteomes; UP000053236; Unassembled WGS sequence.
DR Proteomes; UP000053864; Unassembled WGS sequence.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR Proteomes; UP000054532; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:InterPro.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 426..454
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 426..454
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 385..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 67515 MW; E7A4C7050C79DD7C CRC64;
MTSAGPAGTQ TIAGVPVELG QPVHVNTKKQ LQRQINAIVG WNELDRAPMN VAQTMLRGNE
QQIGEHPYFV CEKSVGVRYL ALLVQGRCYL ISQNYEIREV TLFCPVRPDR LQPGVDRNTV
VPHQWTILDG LMVCDKDGNK SVLTLLLYDI LALNGSPVMT SKLQDRLKLI QNDVVGPRKQ
LPPPKGQPPD MFQLVLQSMY PINRVGHVIR SILPRVSQTR QNAGLVFTPV LLPYTPGYSK
GLYNWTPSSV LFADFQLGVE WRGRPPKPGF KLVIHDKRTQ IFHDWITFAP DDFEAFRQDK
KASSRIVECV YDPEWLTYIP SHDKSTWTSG STEFNATDRG IGWRKGGWKF IRCRPDRSMP
LERSYLAMIE KAIGEDIKLD EIERFFPDDP SKKPQQKSRH DTPSTADDFA PPSKKKRGSG
AGGGQGPGTG VCYDFQNKGV CQRGRFCHFS HCACNSTCSC TPTKNTYGQR PSYRRTDYDA
PPSPEVTPSS IADASSIPDK PPSLRHTNSF ERDSSLKTDG NTGEEEEAGE LTDNNNLHIN
SIYAPLENFD KETIAAKRAQ LTALGNRRIW ASLGLEDKPQ RTRPCGLIVS KSGEVAYVRP
LEK
//
