ID   DAPB_AJECN              Reviewed;         922 AA.
AC   A6RBI0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=HCAG_06318;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476661; EDN10515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6RBI0; -.
DR   SMR; A6RBI0; -.
DR   STRING; 339724.A6RBI0; -.
DR   ESTHER; ajecn-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; A6RBI0; 6 sites, No reported glycans.
DR   VEuPathDB; FungiDB:HCAG_06318; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000009297; 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..922
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412126"
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..922
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        200
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   922 AA;  104147 MW;  34932E3C1D124CDE CRC64;
     MATEKGHSRD DEERVPLTRG STEFRNSIDS FDYSSSTASL SLAVIDRINN STQDAGLSEK
     GPRDDDDDRY WDDDVEYDVE DADYIPSGGK PMHKSVKIAL WSLLFLSLGG WSLAFVLFIF
     RSHDTYQTPI LSEDNISSGG LRGDRITLDD VLGEEWMPRH HFISWFPGPN GEDGLLLEKD
     GPGSTGYLRV EDIVSRKDTN SSKGSIVLMQ KNTFTVGGET VICSQVWPSP DLKTVLVLSE
     KKQNWRHSFT GKYWLFDVDT QTGQPLDPAA QDQRIQLASW SHKSDAVVFT RDNNMFLRKL
     SSKEVITITS DGGVDLLYGV PDWVYEEEVF SGNSATWWAH DGNYIAFLRT NESAVPEYPI
     QYFVSRPSGE DPNLGEENYP EVREIKYPKA GAPNPIVDLQ FYDIRKGEIF SVDVADRFPD
     DNRLIIEVLW ASNGKVLVRE TNRESDILII AAIDVLSRTG KIVRKEDINA LDGGWVEPTQ
     STRFIPADPS NDRPEDGYID TVIHEGRDQL AYFTPLDNPK PLILTKGHSE VVNSPSGVDL
     KRGLVYFVVA GNEPWERHVY SVKFDGTALQ PVTNVSESSY YDVSFSDGAG YALLNFRGPK
     VPWQKVISTP ANENPFEEII EQNNHLSRKL RLFSLESKVF QYINIDGFSL PVLERRPPNF
     DPTKKYPVLF YLYGGPGSQT VDKKFGVDFQ SYVASTLGYI VVTVDGRGTG YIGRKSLSLV
     RGKLGHYEAR DQIEVAKKWA AKPYVDESRM AIWGWSYGGF MTLKTIEEDG GRTFQYGMAV
     APVTDWRYYD SIYAERYMHT PQHNPQGYDS SAISNTTALA NSVRFLVMHG TADDNVHIQN
     TLTLLDKLDL ANVDNYDVHV FPDSNHNINY HNAHKMVYTR LADWLVNAFN GQWLKTNNPT
     PNDSLFRRVA TWAGLYKFKH LC
//