ID   B2WM67_PYRTR            Unreviewed;       479 AA.
AC   B2WM67;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Exopolyphosphatase {ECO:0000313|EMBL:EDU44127.1};
GN   ORFNames=PTRG_11077 {ECO:0000313|EMBL:EDU44127.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU44127.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS231629; EDU44127.1; -; Genomic_DNA.
DR   RefSeq; XP_001941408.1; XM_001941373.1.
DR   AlphaFoldDB; B2WM67; -.
DR   STRING; 426418.B2WM67; -.
DR   EnsemblFungi; EDU44127; EDU44127; PTRG_11077.
DR   GeneID; 6349389; -.
DR   eggNOG; KOG4129; Eukaryota.
DR   HOGENOM; CLU_019358_1_0_1; -.
DR   InParanoid; B2WM67; -.
DR   OMA; TMTIFFN; -.
DR   OrthoDB; 1342473at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF39; EG:152A3.5 PROTEIN (FBGN0003116_PN PROTEIN); 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   4: Predicted;
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:UP000001471}.
FT   DOMAIN          268..427
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
SQ   SEQUENCE   479 AA;  52943 MW;  024BFF8EC91F2B52 CRC64;
     MALPRNSLRG FLTHAKGALR QAVDNSQKIT FVIGNESADL DSMSCSILYA YIRSMSPPKT
     AFSPVYVPIT NIPASDVQLR PEYLAVFQHA NIEPKHLITL DDLPALADIQ SKLAPENTKW
     ILVDHNALQG QLGKVYSGRV AGVIDHHDDE EKVPSNTGDE PRVIIKSGSC TSLVANYCRP
     LWDTLSAAAM SSGAAHAQGD SLSNDAAFVQ RWDADIAQLG LASILIDTAD LKDKSKTTEH
     DRQAVEYLEA KIMLCPQLAG SFDRASFYKE IDAAKKDIGS LELQDILRKD YKQWVQGGHK
     LGISSVVKSI DFLEKKAGDE ASAQPSEALF GALEKFAKER DLDLYSVMTT STSSDGEFQR
     QLLLWAFNES AVSAAKAFAT NSSNELGLEE WQGASDVDGG NEWRRIWWQR QVQHSRKRVA
     PLLRQVMAHS GGWATKTSAQ GRSWVDPVGA FGRKVQMQSA ACLRELRFGG VEASWWWWW
//