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).
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; 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
//