ID A0A5B0PWU8_PUCGR Unreviewed; 554 AA.
AC A0A5B0PWU8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 19.
DE SubName: Full=mRNA-decapping enzyme subunit 2 {ECO:0000313|EMBL:KAA1105368.1};
GN Name=DCP2_1 {ECO:0000313|EMBL:KAA1105368.1};
GN ORFNames=PGT21_004575 {ECO:0000313|EMBL:KAA1105368.1}, PGTUg99_021913
GN {ECO:0000313|EMBL:KAA1088382.1};
OS Puccinia graminis f. sp. tritici.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=56615 {ECO:0000313|EMBL:KAA1105368.1, ECO:0000313|Proteomes:UP000324748};
RN [1] {ECO:0000313|Proteomes:UP000324748, ECO:0000313|Proteomes:UP000325313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-0 {ECO:0000313|EMBL:KAA1105368.1}, and Ug99
RC {ECO:0000313|EMBL:KAA1088382.1, ECO:0000313|Proteomes:UP000325313};
RA Li F., Upadhyaya N.M., Sperschneider J., Matny O., Nguyen-Phuc H., Mago R.,
RA Raley C., Miller M.E., Silverstein K.A.T., Henningsen E., Hirsch C.D.,
RA Visser B., Pretorius Z.A., Steffenson B.J., Schwessinger B., Dodds P.N.,
RA Figueroa M.;
RT "Emergence of the Ug99 lineage of the wheat stem rust pathogen through
RT somatic hybridization.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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:KAA1105368.1}.
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DR EMBL; VDEP01000406; KAA1088382.1; -; Genomic_DNA.
DR EMBL; VSWC01000040; KAA1105368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B0PWU8; -.
DR OrthoDB; 18996at2759; -.
DR Proteomes; UP000324748; Unassembled WGS sequence.
DR Proteomes; UP000325313; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:TreeGrafter.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; NUDIX_Dcp2p_Nudt20; 1.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000324748};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 136..307
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 62754 MW; 5AD5C46A6FA91575 CRC64;
MPSSPSSSNN NHQHQHQQPR QSSSATLPAT SIASSASVFS RMPLEDVLED LASRFILNLP
IVELSHIERV CFQVEQAHWF YEDFVRPNSL LNLPSYHLKT FTGLFFEKCD FLTVDGAPLA
GWDPKTAYEK FMRYKERVPV CGAIMFNEDA TQVLLVRGFK SNSSWSFPRG KINENELPKD
CAIREVLEET GFNIEPYLSL PSSWSDDSKL SAIRKIRPTN PTPNGSNSQS HKPHQNCTLH
SEGDDHFIEI TIREQRLRMY LVTGIPNDTK FVTQTRQEIG RIAWFPLSDL PTFSASNGTL
GSKQLSKMIN VSCPSTVESQ RAHAKFYMVV PFVNDMRTWL TNNHLLAPIG QSLPTPREHH
QAYVQTNHPP TNQSYGGNPI GHPPSHHIRF ENEAAAVHER VSRLQAFDFF QEEPSSTEQV
NQDNRLNPST NRKKNRRKQP QQPRKPPKEA NHQRLTDNPS YHSDPQTSTD DEDITKVNND
TPWNDLAEGT RALQNFFFGS RNEELEGRGD QFGLLSDGPT ALLDLHLRHD AANNGVSPLI
ASQLHATPDR LVHF
//
