DAPB_PYRTR
ID DAPB_PYRTR Reviewed; 880 AA.
AC B2WC36;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=PTRG_07545;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
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 -!- FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC Pro nor hydroxyproline.; EC=3.4.14.5;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type
CC II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; DS231622; EDU50464.1; -; Genomic_DNA.
DR RefSeq; XP_001937877.1; XM_001937842.1.
DR AlphaFoldDB; B2WC36; -.
DR SMR; B2WC36; -.
DR STRING; 45151.EDU50464; -.
DR ESTHER; pyrtr-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR PRIDE; B2WC36; -.
DR EnsemblFungi; EDU50464; EDU50464; PTRG_07545.
DR GeneID; 6345817; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; B2WC36; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..880
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412160"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..880
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 724
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 801
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 834
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 880 AA; 99739 MW; 2EBBF7438A194B42 CRC64;
MPRQRAPKEE EAELLTKQER SARSSEDASD TSISSISTTS LVLEHINDPA INGTSRSRRG
EKYTDEDDEA QEAFDVEGGR YKSPISVDKK TRRWLWIVGI ACVTGWALAL VFFLMSGSYK
HVSTRPHDPL ASSTKGSGKK ITMDDVFGGR FYAREQSLKW IAGPNGEDGL LLERDAGNAE
YLVVEDIRNK GDGDSSAKKT KLMQKSGFNV NGYFVRPVEV WPSKDFKKTG EPLDPENQDG
RVQLASLSPQ SDAVVFTRNN NMYLRKLDSK EVIQITRDGG SELFYGIPDW VYEEEVFQTN
SATWWSEDGK YIAFLRTDES TVPTYPVQYF VSRPSGDKPK AGEENYPEVR NIKYPKAGAP
NPIVTLQFYD VEKAEVFSVE IEDDFRDNNR LITEIVWAGK TKQVLVRETN RESDILKVVL
MDVEKRTGKT VRTENVAELD GGWFEVSQKT TFVPADPANG RKDDGYIDTI IHEGYDHIGY
FTPLDNDKPI VLSQGEWEVV DAPSRVDLKN NIVYYISTAK SSMERHAYSV FLNGTGTSEV
VENSGSGYYG ASFSAGGSYA LITYQGPGIP WQKIISTPSS KDKFEKVLEE NKALDRFVRE
REMPILNYQT IEVDGFKLNV LERRPPHFNE KKKYPVLFYQ YSGPGSQEVN KKFHVDFQAY
IAANLEYIVV TVDGRGTGFL GRKLRCITRG NIGYYEAHDQ IAAAKIWASK KYVDADRLAI
WGWSYGGFNT LKTLEQDAGQ TFKYGMAVAP VTDWRYYDSI YTERYMHTPQ NNAAGYNNST
ITDVASLAKN TRFLLMHGVA DDNVHMQNTL TLLDRLDLAG VENYDVHVFP DSDHSIYFHN
ANRIVYDKLR WWLINAFNGE WAKIKTAEPK AQVDARMERR
