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Database: UniProt
Entry: A0A8T9AZ78_9HELO
LinkDB: A0A8T9AZ78_9HELO
Original site: A0A8T9AZ78_9HELO 
ID   A0A8T9AZ78_9HELO        Unreviewed;       904 AA.
AC   A0A8T9AZ78;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   SubName: Full=mRNA decapping complex subunit 2 {ECO:0000313|EMBL:TVY12994.1};
GN   Name=dcp2 {ECO:0000313|EMBL:TVY12994.1};
GN   ORFNames=LARI1_G008349 {ECO:0000313|EMBL:TVY12994.1};
OS   Lachnellula arida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Lachnaceae; Lachnellula.
OX   NCBI_TaxID=1316785 {ECO:0000313|EMBL:TVY12994.1, ECO:0000313|Proteomes:UP000469559};
RN   [1] {ECO:0000313|EMBL:TVY12994.1, ECO:0000313|Proteomes:UP000469559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 203.66 {ECO:0000313|EMBL:TVY12994.1,
RC   ECO:0000313|Proteomes:UP000469559};
RA   Giroux E., Bilodeau G.;
RT   "Whole genome sequencing for identification of molecular markers to develop
RT   diagnostic detection tools for the regulated plant pathogen Lachnellula
RT   willkommii.";
RL   Submitted (MAY-2018) 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:TVY12994.1}.
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DR   EMBL; QGMF01001163; TVY12994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8T9AZ78; -.
DR   OrthoDB; 18996at2759; -.
DR   Proteomes; UP000469559; 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   FunFam; 1.10.10.1050:FF:000003; Decapping enzyme Dcp2, putative; 1.
DR   FunFam; 3.90.79.10:FF:000003; M7GpppN-mRNA hydrolase isoform 2; 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:UP000469559};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          95..227
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   REGION          369..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..392
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..755
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  98632 MW;  A6B5D2C36FCBF71D CRC64;
     MTETNLKLEE WLDDLCVRFI INLPEDDLKD IPRICFQVEE AQWYYEDFIR ALDPSLPSMS
     LRNFCLRIFA HCPLLSSFSQ GHHMRAFEDF LAYKTRVPVR GAVMLNANMD SVVLVKGWKK
     GASWSFPRGK IAKDEDDLTC AIREVYEETG FDLDAAGLVP PNRDVKSIQV NMREQQMRLF
     VFRNVPMETH FEPKTRKEIS KIDWWQLSEL PAFRKKSQQQ QQKQAVPNSS KFYMVAPFLV
     PLRKWVIEQK KKDARRTTSN QYLPAGMSHD EFLTEEDQGA ESATQMPYEE PSALELDTLE
     GATTALSRLL KIQPATQGLQ AEAATQSSSK NSGEALLALL KPAASSQSLP ANAPPHTPLE
     HIVMQPAMPK TPHHQQPRPP HFSNMPPPPD FPIQPQDDSF SHREANHQNG RHNAAEFQQS
     HVGRQNPPRP QENPHSYQPQ HLIHPQPLPP HVQRALFTGG SVHSPMVPQS IQQNPPPVHT
     AISGPTGAPQ FPALHATMVP QTVQQTPKLT SHSLALLNAF KTRDQAADEV SGSNDLPLRR
     YTQAQNQASV PAPRGVPQEL PAEGSQPGQM LPPPQIKVQQ NVGHLTPTPL APRQSISATQ
     KSTLLDLFRS PTAQPASLAN SAGATSLPIS TTPSVVELSA VEPLSTGAST TSALLNSKRT
     PDNLASNGAV PVLNPESNLP FGAVSILGRP PNMSDKQSLS AAGSELDSKP KSNGKKPTAR
     MNTGSHTVKL PEKPFQPQIL KRPQQSSSKT QQSPPAIQSG VSSFASQPGA SRMQQSPTPV
     SPSSNFRSSQ GSLRMPHSAT AIQHPVSTFV PPPDRRPSQA VGHKQNLLSL FGKAQVGPIS
     PPGRDGPSME PLASTVKTSV RSRVGSLASG GDGTSRRGSQ TPISPADKGF LLGYLEEALA
     KGSR
//
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