ID A0A136IUS0_9PEZI Unreviewed; 547 AA.
AC A0A136IUS0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B {ECO:0000256|ARBA:ARBA00014118};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE AltName: Full=Dipeptidyl peptidase IV {ECO:0000256|ARBA:ARBA00030567};
GN ORFNames=Micbo1qcDRAFT_166660 {ECO:0000313|EMBL:KXJ88593.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ88593.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ964258; KXJ88593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IUS0; -.
DR STRING; 196109.A0A136IUS0; -.
DR InParanoid; A0A136IUS0; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000070501; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
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: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; 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.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:KXJ88593.1};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 9..229
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 316..514
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 547 AA; 61406 MW; 43FB5800C1E526EB CRC64;
MDNQKIAPVY PKELELRYPK VGTTNPTVSL TLVNVATEDK TPVKIDAYAP DNLVVGEVAW
VTEEHGSLIY VAYNRVQDKS THIRVDVDSY GAVSTHKIRE RDGSDGWLDN NIAIQFVGDV
NGKPYYLDLS DESGWKHIYL YPLDGSEPII VTKGDWEVTA VLKVNLEKKL IYYQSTQGDS
TERHLFSVSW DTKETTPLVD VEVPAAWSAS FSSGGGYYIL SYQGPDVPYQ ELYATNDTAK
PLRTITSNQV LWDRLQEYKL PNITYFTLEH PDGYSMNVMQ RLPPNFDPSK KYAALFTPYG
GPGSQEVSKT YKTPSWNAYI ASDPELEYIQ YTVDNRGTGY KGRAFRSLVT SHLGGFEAED
QIWAASELSK RNSFVDADHI GIFGWSYGGY LSAKVVEADS GVFSLGLIVA PVSDWRFYDS
MYTERYMKTT QDNAEGYNGT AVRKTAGFKN IAGKAAIMHG TGDDNVHYQN AAALIDTLVG
AGVTAETVDW RSFTDSDHSI VYNGASSYLY KYMTGLLYEE KLRTKESALT HQWSKKSERR
HQWEAQL
//
