ID   DAPB_AJEC8              Reviewed;         917 AA.
AC   F0U7H7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=HCEG_00116;
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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; DS990636; EGC40754.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0U7H7; -.
DR   SMR; F0U7H7; -.
DR   STRING; 544711.F0U7H7; -.
DR   ESTHER; ajecn-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; F0U7H7; 5 sites, No reported glycans.
DR   VEuPathDB; FungiDB:I7I53_08556; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
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; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 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..917
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412123"
FT   TOPO_DOM        1..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..917
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        756
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        833
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        866
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        815
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        902
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   917 AA;  103412 MW;  0C1A7AD5D755FFC9 CRC64;
     MATEKGHGRD DEERVPLTRG STEFRNSIDS FDYSSSTASL SLAVIDRINN STQDAALGEK
     GPRDDDDDRY WDDDVEYDVE DADYIPSGGK PMHKSVKIAL WTLLFLSLGG WSLAFVLFIF
     RSHDTYETPI SSEDNISSGG LRGDRITLDD VLGEEWMPRH HFISWFPGPN GEDGLLLEKD
     GLGSTGYLRV EDIVSRKDTK SSKGSIVLMQ KNTFTVGGET VICSQVWPSP DLKTVLVLSE
     KKQNWRHSFT GKYWLFDVDT QTGQPLDPAA QDQRIQLASW SPQSDAVVFT RDNNMFLRKL
     SSKEVTTITS DGGVDLFYGV PDWVYEEEVF SGNSATWWAH DGNYIAFLRT NESAVPEYPV
     QYFVSRPSGE DPNLGEENYP EVREIKYPKA GAPNPIVDLQ FYDVRKGEIF SVDVADRFPD
     DYRLIIEVLW ASNGKILVRE TNRESDILII AAIDVLSRTG KIVRKEDINA LDGGWVEPTQ
     STRFIPADPS NGRPEDGYID TVIHEGRDQL AYFTPLDNPK PLILTKGPSE IVNSPSGVDL
     KRGLVYFVVA GNEPWERHVY SVKFDGTALQ PVTNVSESSY YDVSFSDGAG YALLNFQGPK
     VPWQKVISTP ANENPFEEII EQNNHLSRKL RLFSLESKVF QYINIDGFSL PVLERRPPNF
     DPTKKYPVLF YLYGGPGSQT VDKKFRVDFQ SYVASTLGYI VVTVDGRGTG YIGRKSRSIV
     RGKLGHYEAR DQIEVAKKWA AKPYVDESRM AIWGWSYGGF MTLKTIEEDG GRTFQYGMAV
     APVTDWRYYD SIYAERYMHT PQHNPQGYDS SAISNTTALA NNVRFLVMHG TADDNVHIQN
     TLTLLDKLDL ANVDNYDVHV FPDSNHNINF HNAHKIVYTR LADWLVNAFN GQWLKTNNPT
     PNDSLFRRAA TWAGLSI
//