ID   DAPB_ASPOR              Reviewed;         902 AA.
AC   Q2UPW4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=AO090005001482;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE56401.1; -; Genomic_DNA.
DR   RefSeq; XP_001818403.2; XM_001818351.2.
DR   AlphaFoldDB; Q2UPW4; -.
DR   SMR; Q2UPW4; -.
DR   STRING; 510516.Q2UPW4; -.
DR   ESTHER; aspor-q2upw4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   EnsemblFungi; BAE56401; BAE56401; AO090005001482.
DR   GeneID; 5990348; -.
DR   KEGG; aor:AO090005001482; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   Proteomes; UP000006564; Chromosome 1.
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..902
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412138"
FT   TOPO_DOM        1..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..902
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        740
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        817
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        850
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        794
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        799
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   902 AA;  101664 MW;  682AE97AABC5F565 CRC64;
     MTRRRSTSGT SSRSSTDSGL SVDTAYLEDN KHNNFANGTS GLTDETKYRD VEDAEADVDE
     PFLPTSSKKL GSGSRTRQIF WALVILCLGG WVLALVLFLT HGRASSQTAS ETLQQQESDS
     GSTSAGRPVT LQQVLTGSWN PRAHAISWIA GPDGEDGLLV QRAEVDKEGY MRVDDIRSQE
     GDDVDSQSGR ILIDKAAVRV NGETLMPTFT WPSPDLNKVL LMSNHEKNWR YSFTGRYWIF
     DVATQTAQPL DPSVPDGRVQ LALWSPSSDA VVFVRDNNMY LRKLSSESVV SITKDGGEDL
     FYGIPDWVYE EEVITDKSVT WWSNDGKYVA FLRTNESAVP EFPVQYFVSR PSGKRPPPGL
     ENYPEVRQIK YPKAGSPNPV VNLLFYDVEK DEVFPVDVPD DFPDDDRIII EVLWASEGKV
     IVRATNRESD RVKVFLIDTK SRTGKLVRFE DIANLDGGWV EPSHYTKFIP ADPSNGRPDD
     GYIDTVIHDG YDHLAYFTPL DNPDPIMLTT GEWEVVEAPS AVDLRRGIVY FVATKESPTQ
     RHVYRVHLDG SNLQALTDTS KPGFYDVSFS DGAGYALLSY NGPSVPWQAI INTGGDEITF
     EKTIEKNPRL ASMVETYALP TEIYQNVTID GFTLQLVERR PPHFNPAKKY PVVFQLYNGP
     TSQRVDRKFT IDFQSYIASN LGYIVVTLDA RGTGYSGRKV RCAVRGNLGH YEAHDQITTA
     KMWAKKPYVD ETRMAIWGWS YGGFMTLKVL EQDAGETFQY GMAVAPVTDW RFYDSVYTER
     YMHTPEHNPS GYENSTITNV SALSKATRFL LIHGASDDNV HIQNTLTFVD KLDLLNVQNY
     DMHFYPDSDH NIYFHNAHFM IYERLSNWLI NAFNGEWHQI ANPVPEDSIW DSVKRSVPAF
     AH