ID W2KCK2_PHYPR Unreviewed; 371 AA.
AC W2KCK2;
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=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
GN ORFNames=L917_17052 {ECO:0000313|EMBL:ETL82858.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL82858.1};
RN [1] {ECO:0000313|EMBL:ETL82858.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL82858.1};
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.
CC -!- FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes
CC the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs
CC by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
CC {ECO:0000256|RuleBase:RU367113}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU367113};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367113}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family.
CC {ECO:0000256|ARBA:ARBA00006562, ECO:0000256|RuleBase:RU367113}.
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DR EMBL; KI682130; ETL82858.1; -; Genomic_DNA.
DR AlphaFoldDB; W2KCK2; -.
DR EnsemblProtists; ETL82858; ETL82858; L917_17052.
DR VEuPathDB; FungiDB:PPTG_04193; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395:SF9; DECAPPING AND EXORIBONUCLEASE PROTEIN; 1.
DR PANTHER; PTHR12395; DOM-3 RELATED; 1.
DR Pfam; PF08652; RAI1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU367113};
KW Metal-binding {ECO:0000256|RuleBase:RU367113};
KW Nuclease {ECO:0000256|RuleBase:RU367113};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367113};
KW Nucleus {ECO:0000256|RuleBase:RU367113};
KW RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT DOMAIN 239..301
FT /note="RAI1-like"
FT /evidence="ECO:0000259|Pfam:PF08652"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 43494 MW; 0B0338BEBC809200 CRC64;
MTEKRPRDDV GGDDRRQQRP RPHRAREFSS PRSLSYLRFA VPRAHELSQQ GRVSLSKPRE
IAYFSKYADD DVRFDRSNLL VYKQAEIGSN LLDGFEEYTA KDESNPTASP APIAPLLAAL
EHFQADNKDR ERAHFVTYRN NLNKIMGTPY NSKNGWTFEV EKRSGCVYLD VRRTQEDIDS
NRNPHENQRR GAFAGRRFEI YSTHPKADDE QRKVNEDEEY CSVSAMTLGD KRLVVAAEID
CYEDKSGQRE YIELKTFRLL QREKDQFVFE RFKLLTFWIQ SFLVGTPKIV CAFRSDDFEV
RKLQSFRVTE IPNFCRKHWT PVVCLNFTKA LLDWIYEHAD EGRVHRVTYI PQQHVVEMDL
SAQDSFLPTQ N
//
