DAPB_PHANO
ID DAPB_PHANO Reviewed; 911 AA.
AC Q0UVK7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=SNOG_04207;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445330; EAT87967.1; -; Genomic_DNA.
DR RefSeq; XP_001794630.1; XM_001794578.1.
DR AlphaFoldDB; Q0UVK7; -.
DR SMR; Q0UVK7; -.
DR STRING; 13684.SNOT_04207; -.
DR ESTHER; phano-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; SNOT_04207; SNOT_04207; SNOG_04207.
DR GeneID; 5971498; -.
DR KEGG; pno:SNOG_04207; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; Q0UVK7; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000001055; 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; IBA:GO_Central.
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..911
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412158"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..911
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 832
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 865
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 911 AA; 103088 MW; 2B7D140A51D8324E CRC64;
MPRPRAAKEE ETELLAQHQE SPRPSSDGSE ASASSISTTS LVLEHINDGG FNGARSKVSE
KYTDDGNGDL GHARERFDIE DGKFHPLTPV DKKARRTLWI VGTICAVGWA LALVSFLMNG
NYKHSSTRPH DPDASVTKGS GKKITLDNVL GGQFYPQSQS VSWIAGPKGE DGLLLEKGVS
GKDYLVVEDI RSKGNTEAAG DKFTLMKKGN FQIGEDIFIY PSNVWPSADF KKVLVMSEQQ
KNWRHSYTGL YWIFDVETQT GEPLDPENQS ARVQYASFSP QSDAVVFTRD NNLYLRKLDS
QKVVKITHDG GSELFYGVPD WVYEEEVFQD NSATWWSEDG KYVAFLRTDE SMVPTYPVQY
FVSRPSGKQP DAGKESYPEV REIKYPKAGA PNPIVTLQFY DIEKSEMFRV DIDNDFTDKD
RLITEIVWAG KSGQVLVRET NRESDILKLI LIDVSKRTGK TIREENVAKL DGGWFEVSHK
TTFIPADSSL GRANDGYIDS VIHEGYDHIG YFTPLDSDKP ILLTKGEWEV VEAPSRVDLK
NNLVYYVSTE RGSMERHPYV VALNGTDKRE VMDHSGPAYY DSSFSTGGGY ALMSYQGPGI
PWQKIVSTPS NTEKFEKVLE ENKALEKMVQ KHELPILKYQ TIDVDGFKLN VLERRPPHFS
EKRKYPVLFY QYSGPGSQQV QRKFEVDFQS YIAANLGYIV VTVDGRGTGF LGRKLRCITR
DNIGYYEAYD QIAAAKMWAA KKYVDAEKLA IWGWSYGGFT TLKTIEMDGG RTFKYGMAVA
PVTDWRFYDS IYTERYMHTP QNNPTGYDNT SITDVHSLSQ NVRFLIMHGV ADDNVHMQNT
LTLLDKLDVA GVENYDVHVF PDSDHSIYFH NAHKIVYDKL TWWLTNAFNG EWLKIQKVRP
KAQADARSLG R