DAPB_AJECG
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 03-AUG-2022, entry version 48.
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 EnsemblFungi; EEH04721; EEH04721; HCBG_06672.
DR VEuPathDB; FungiDB:HCBG_06672; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; C0NUQ8; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
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..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
