DPP5_ASPFU
ID DPP5_ASPFU Reviewed; 721 AA.
AC P0C959; O13479; Q4X1R6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Dipeptidyl-peptidase 5;
DE EC=3.4.14.-;
DE AltName: Full=Dipeptidyl-peptidase V;
DE Short=DPP V;
DE Short=DppV;
DE Flags: Precursor;
GN ORFNames=AFUA_2G09030;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: May be involved in metabolism of dipeptides or may affect
CC host defense mechanisms. Has a substrate specificity limited to the
CC hydrolysis of X-Ala, His-Ser, and Ser-Tyr dipeptides at a neutral pH
CC optimum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in mycelia and conidia.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; AAHF01000001; EAL93199.1; -; Genomic_DNA.
DR PIR; T09631; T09631.
DR RefSeq; XP_755237.1; XM_750144.1.
DR AlphaFoldDB; P0C959; -.
DR SMR; P0C959; -.
DR STRING; 746128.CADAFUBP00002435; -.
DR Allergome; 8984; Asp f DPPV.
DR ESTHER; aspfc-dpp5; Prolyl_oligopeptidase_S9.
DR MEROPS; S09.012; -.
DR EnsemblFungi; EAL93199; EAL93199; AFUA_2G09030.
DR GeneID; 3512867; -.
DR KEGG; afm:AFUA_2G09030; -.
DR VEuPathDB; FungiDB:Afu2g09030; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_008615_0_1_1; -.
DR InParanoid; P0C959; -.
DR OMA; STRWNPK; -.
DR OrthoDB; 265965at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IDA:AspGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..721
FT /note="Dipeptidyl-peptidase 5"
FT /id="PRO_0000027223"
FT REGION 271..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 643
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 675
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 721 AA; 79745 MW; A9B250EE98EA4922 CRC64;
MGAFRWLSIA AAASTALALT PEQLITAPRR SEAIPDPSGK VAVFSTSQYS FETHKRTSWW
SLLDLKTGQT KVLTNDSSVS EIVWLSDDSI LYVNSTNADI PGGVELWVTQ ASSFAKGYKA
ASLPASFSGL KTAKTKSGDI RFVAYGQSYP NGTAYNEELA TAPLSSARIY DSIYVRHWDY
WLSTTFNAVF SGTLKKGHGK NGYSLDGELK NLVSPVKNAE SPYPPFGGAS DYDLSPDGKW
VAFKSKAPEL PKANFTTSYI YLVPHDASET ARPINGPDSP GTPKGIKGDS SSPVFSPNGD
KLAYFQMRDE TYESDRRVLY VYSLGSKKTI PSVAGDWDRS PDSVKWTPDG KTLIVGSEDL
GRTRLFSLPA NAKDDYKPKN FTDGGSASAY YFLPDSSLLV TGSALWTNWN VYTAKPEKGV
IKKIASANEI DPELKGLGPS DISEFYFQGN FTDIHAWVIY PENFDKSKKY PLIFFIHGGP
QGNWADGWST RWNPKAWADQ GYVVVAPNPT GSTGFGQALT DAIQNNWGGA PYDDLVKCWE
YVHENLDYVD TDHGVAAGAS YGGFMINWIQ GSPLGRKFKA LVSHDGTFVA DAKVSTEELW
FMQREFNGTF WDARDNYRRW DPSAPERILQ FATPMLVIHS DKDYRLPVAE GLSLFNVLQE
RGVPSRFLNF PDENHWVVNP ENSLVWHQQA LGWINKYSGV EKSNPNAVSL EDTVVPVVNY
N
