ID   DAPB_ASPFU              Reviewed;         919 AA.
AC   Q4WX13;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=AFUA_3G07850;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000002; EAL92790.2; -; Genomic_DNA.
DR   RefSeq; XP_754828.2; XM_749735.2.
DR   AlphaFoldDB; Q4WX13; -.
DR   SMR; Q4WX13; -.
DR   STRING; 746128.CADAFUBP00004042; -.
DR   ESTHER; aspfu-q4wx13; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   EnsemblFungi; EAL92790; EAL92790; AFUA_3G07850.
DR   GeneID; 3512523; -.
DR   KEGG; afm:AFUA_3G07850; -.
DR   VEuPathDB; FungiDB:Afu3g07850; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; Q4WX13; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 269253at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
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..919
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412135"
FT   TOPO_DOM        1..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..919
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        757
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        834
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        867
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        643
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        811
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   919 AA;  103079 MW;  41A93F5575C44F80 CRC64;
     MRRSDGHEET SEFLPMTHSR SVSAASQTST DSSLSTESLF PREQKPFPNA MGGMALADDD
     KYRDLEDGEA EQSEPFLSSS KKAATGGGRA RRIFWILVLL CLGGWLLAFV LFLTGGRANY
     QTASDALQAH GADSALGSTS TSSGKPVTLH QVLGGQWNPR YHAIGWVAGP NNEDGLLVEK
     GGDEKQGYLR VDDIRSRKGN NTGRESRVLM RKPIVHVDGQ AIVPSNVWPS PDLKKVLLIS
     EQQKNWRHSF TGKYWVLDVD SQTAQPLDPS APDGRVQLAL WSPASDAVVF VRDNNLYLRR
     LSSDSVVAIT KDGGENLFYG VPDWVYEEEV ISGNSVTWWS NDAKYIAFFR TNETSVPEFP
     VQYYISRPSG KKPLPGLENY PDVREIKYPK PGAPNPVVDL QFYDVEKNEV FSVQVADDFA
     DDDRIIIEVL WASEGKILVR STNRESDILK VYLIDTQSRT GKLVRSEDVA GLDGGWVEPS
     QSTRFVPADP NNGRPHDGYI DTVPYNGYDH LAYFSPLDNP NALMLTSGEW EVVDAPAAVD
     LQRGLVYFVG TKEAPTQRHV YRVQLDGSNL NPLTDTSKPG YYDVSFSHGT GYALLTYKGP
     SIPWQAIINT HGDEITYEDR IEDNAQLTKM VEAYALPTEV YQNVTVDGYT LQVVERRPPH
     FNPAKKYPVL FYLYGGPGSQ TVDRKFTVDF QSYVASSLGY IVVTVDGRGT GFIGRKARCI
     VRGNLGFYEA HDQIATAKMW AAKSYVDETR MAIWGWSFGG FMTLKTLEQD AGRTFQYGMA
     VAPVTDWRFY DSIYTERYMH TPQHNPNGYD NSTITDMAAL SESVRFLVMH GASDDNVHLQ
     NTLVLIDKLD LSNVENYDVQ FYPDSDHSIY FHNAHMMVYH RLSDWLVNAF NGEWHLIAKP
     VPDESMWERM KRSLRLLSP