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
//
