ID   DAPB_AJECG              Reviewed;         923 AA.
AC   C0NUQ8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=HCBG_06672;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) 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; GG663372; EEH04721.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NUQ8; -.
DR   SMR; C0NUQ8; -.
DR   STRING; 447093.C0NUQ8; -.
DR   ESTHER; ajecn-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; C0NUQ8; 5 sites, No reported glycans.
DR   VEuPathDB; FungiDB:I7I50_12559; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; C0NUQ8; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000001631; 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..923
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412124"
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..923
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   923 AA;  104146 MW;  5C27FFBC9F38335B CRC64;
     MATEKGHGRD DEERVPLTRG STEFRNSIDS FDYSSSTASL SLAVIDRINN STQDAALGEK
     GPRDDDDDRY WDDDVEYDVE DADYIPSGGK PMHKSVKIAL WTLLFLSLGG WSLAFVLFIF
     RSHDTYETPI SSEDNISSGG LRGDRITLDD VLGEEWMPRH HFISWFPGPN GEDGLLLEKD
     GPGSTGYLRV EDIVSRKDTK SSKGSIVLMR KNTFTVGGET VICSQVWPSP DLKTVLVLSE
     KKQNWRHSFT GKYWLFDVDT QTGQPLDPAA QDQRIQLASW SPQSDAVVFT RDNNMFLRKL
     SSKEVTTITS DGGVDLFYGV PDWVYEEEVF SGNSATWWAH DGNYIAFLRT NESAVPEYPL
     QYFVSRPSGE DPNLGEENYP EVREIKYPKA GAPNPIVDLQ FYDVRKGEIF SVDVADRFPD
     DNRLIIEVLW ASNGKVLVRE TNRESDILII AAINVLSRTG KIVRKEDINA LDGGWVEPTQ
     STRFIPADPS NGRPEDGYID TVIHEGRDQL AYFTPLDNPE PLILTKGPSE VVNSPSGVDL
     KRGLVYFVVA GNEPWERHVY SVKFDGTALQ PVTNVSESSY YDVSFSDGAG YALLNFQGPK
     VPWQKVISTP ANENPFEEII EQNNHLSRKL RLFSLESKVF QYINIDGFSL PVLERRPPNF
     DPTKKYPVLF YLYGGPGSQT VDKKFRVDFQ SYVASTLGYI VVTVDGRGTG YIGRKSLSIV
     RGKLGHYEAR DQIEVAKKWA AKPYVDESRM AIWGWSYGGF MTLKTIEEDG GRTFQYGMAV
     APVTDWRYYD SIYAERYMHT PQHNPQGYDS SAISNTTALA NNVRFLVMHG TADDNVHIQN
     TLTLLDKLDL ANVDNYDVHV FPDSDHNINF HNAHKIVYTR LADWLVNAFN GQWLKTNNPT
     PNDSLFRRAA TWAGLSYNFK HLH
//