ID A0A1E1LC37_9HELO Unreviewed; 764 AA.
AC A0A1E1LC37;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE AltName: Full=Dipeptidyl peptidase IV {ECO:0000256|ARBA:ARBA00030567};
GN ORFNames=RCO7_09569 {ECO:0000313|EMBL:CZT08096.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT08096.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZT08096.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZT08096.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline. Contributes
CC to pathogenicity. {ECO:0000256|ARBA:ARBA00037607}.
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 Evidence={ECO:0000256|ARBA:ARBA00001257};
CC -!- SIMILARITY: Belongs to the peptidase S9B family.
CC {ECO:0000256|ARBA:ARBA00006150}.
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DR EMBL; FJUW01000045; CZT08096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1LC37; -.
DR STRING; 914237.A0A1E1LC37; -.
DR InParanoid; A0A1E1LC37; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000178129; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF162; DIPEPTIDYL PEPTIDASE 4-RELATED; 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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..764
FT /note="dipeptidyl-peptidase IV"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009447008"
FT DOMAIN 106..460
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 549..747
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 764 AA; 85482 MW; 1B9F0EA55E4DAF64 CRC64;
MRSFNTLSTA VCLLIAATVD ALPPQARRSP ADKKVVSFED AFSGKFRVNR TSLRWTSQGA
DGTYVEAGSN GDLTLANIVT GNSSKFVTAS EIGAAAQEYH DYSIQPGGEH VLFIANYTKL
YRHSFYADYF IYNIKDKTTV PLAADQAGDI QFAGWSPVGN TIAYARGNNL FIWENGTSTQ
ITKDGGPDVF NAIPDWGYEE EIYGDTSLLW FSPDGKQLAY LSTDETGVPT YQIPYYMNGS
TAGVYPHYLQ LRYPKVGETN PTVKFNLLGL ENLSAGPTTI KFDSFAPEDL IIGEVAWVTD
DSSHVIFRSF NRVQDQEKLI LVDTATKSSS VVRERKTSPG WIDNNLAISY IPGTQTYVDL
SDESGWQHIY LYPVNGSTPV AITQGEWEVD SILYIDAANK TLYYTSTEQN SMERHLYSIG
LDGQGKKALV DTSKPGVWTA SFSANGGYYI LSYNGPDLPY QELYSTQSHL EKIKTINDNS
VLEAKLANYT LPKTTWFEME GADGYIYNVM ERLPPNFDPA KKYPVIFDPY GGPGNQRTTK
TFRQVDFRAY LASDPELEYI VLVVDNRGTG FKGRAFREVV AGRLGTLEAI DQVHAAKEYG
KRSYVDASKI TIFGWSYGGY LAGKVLELDS DAFSFAILTA PVSDWRFYDS FYTERFMKRL
SDNEEGYNTT AIRKTAGFQN VRGGFLIQHG TGDDNVHFQN SAVLVDTLTV GKVSPKKFHV
QWFTDSDHSI DFHGAGTLIY KQMARYFWLE KTRKEEGKHQ FDKK
//
