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Database: UniProt
Entry: B2WPX1_PYRTR
LinkDB: B2WPX1_PYRTR
Original site: B2WPX1_PYRTR 
ID   B2WPX1_PYRTR            Unreviewed;       572 AA.
AC   B2WPX1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=X-Pro dipeptidyl-peptidase protein {ECO:0000313|EMBL:EDU46187.1};
GN   ORFNames=PTRG_12031 {ECO:0000313|EMBL:EDU46187.1};
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:EDU46187.1, 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).
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DR   EMBL; DS231640; EDU46187.1; -; Genomic_DNA.
DR   RefSeq; XP_001942362.1; XM_001942327.1.
DR   AlphaFoldDB; B2WPX1; -.
DR   STRING; 426418.B2WPX1; -.
DR   EnsemblFungi; EDU46187; EDU46187; PTRG_12031.
DR   GeneID; 6350349; -.
DR   eggNOG; ENOG502QZDY; Eukaryota.
DR   HOGENOM; CLU_015590_2_1_1; -.
DR   InParanoid; B2WPX1; -.
DR   OrthoDB; 1780329at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR038717; Tc1-like_DDE_dom.
DR   InterPro; IPR013736; Xaa-Pro_dipept_C.
DR   PANTHER; PTHR43056:SF10; COCE/NOND FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G00600)-RELATED; 1.
DR   PANTHER; PTHR43056; PEPTIDASE S9 PROLYL OLIGOPEPTIDASE; 1.
DR   Pfam; PF13358; DDE_3; 1.
DR   Pfam; PF08530; PepX_C; 1.
DR   SMART; SM00939; PepX_C; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT   DOMAIN          328..565
FT                   /note="Xaa-Pro dipeptidyl-peptidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00939"
SQ   SEQUENCE   572 AA;  66331 MW;  0E2A2D6E7CAC77B6 CRC64;
     MSDQLEVNSE HHFDHSAWET PDPGFWTKHD YIVVRADERG LGQSPDFLDT IKSTLYRTLK
     RTGLGHFRCK KRPKLNRIRA RARLRFCKEY RNFPWRRRPL KFSDECSVQV GSGASAEWCF
     RYEAEKWSHR MITETTTARQ RAQMVWAAVW LDRRGHPQRS ELIIMERDPN AAKGGYSGQS
     YIQTLRRGLL PHWRRSQLFM HVNAPIHRAR VVAEFMRVKD IRPIEWPAYS PDLNPIEHLW
     WVLKKRVHAY YPQYSRLDHT AEQWEAFCEV LKKCWREIPS PLITRLIGSM PRRIAACTKA
     GSEFKYLRMI TGRHGLPFLY KEEVEIQRSF LDAFLKSDDR VGWSVKGKLP PVDIVLRKGD
     VGFDNAEKEK AYKRRTENEW LIAPLGTLDN PKLLQFTTAP FDEEIEITGH IVAHLNVSLS
     PYATGATPSD IDLFLTLRYI SPEGKEVHYT GTAGDPIPLV KGWLRVSFRN TNPNHPKHRE
     YLPWRDYFST DVRPVIPGDI YSVDVEVCPT NVVVEKGSKI VFEVSSGDTQ GSGIFQHNHP
     QDGSEEVFAG FNHLHFGEKF VNYVTLPIVP PK
//
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