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Database: UniProt
Entry: A0A137Q7P0_9AGAR
LinkDB: A0A137Q7P0_9AGAR
Original site: A0A137Q7P0_9AGAR 
ID   A0A137Q7P0_9AGAR        Unreviewed;       761 AA.
AC   A0A137Q7P0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00012917};
DE            EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
DE   AltName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=AN958_01643 {ECO:0000313|EMBL:KXN83272.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN83272.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN83272.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN83272.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC         terminus of a polypeptide.; EC=3.4.19.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000721};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
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DR   EMBL; KQ962842; KXN83272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137Q7P0; -.
DR   STRING; 1714833.A0A137Q7P0; -.
DR   OrthoDB; 2877590at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR045550; AARE_N.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF4; ACYLAMINO-ACID-RELEASING ENZYME; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT   DOMAIN          25..245
FT                   /note="Acylamino-acid-releasing enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19283"
FT   DOMAIN          507..604
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   DOMAIN          665..755
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   761 AA;  83463 MW;  B3033A9E609372FF CRC64;
     MSLYNRLAEI PVPLSATFLN NEVVQIGYSA RNHLANTKKT LTKIVPLTSG VPTNFPLQEV
     GEVVGSAVSP SYNLRANLRE SKQGTTTKRY VEIWSGNRTE VSFEVTDHHQ AFYLDENLST
     LVFSPSETAL LYTAEANAPE NGSDDPYAKF RYRPSFGEGF GGKKRPHFFL LRWKSPTDST
     STVLKPRLYE IHSESDDILF GQGIFFPTAE ETTIYATGYE YTPNGRLLGI KGCFNRPSGI
     WELRFQTQSG DGHDDNHDKK QDSIIYSARK ISGTNSGRSP RILQEGSTSI LYWFASDNGG
     PHMSTTTLHS LDITILDTIS TEIVSRTKTV VPVPEALSPN FPGLYPPFNL VIRPFLQPDG
     GPTEIITQSQ WGSRTTILSI SPSTGTVRHL TPPEPALFSW SLLATDGKNQ IICSRGSSSI
     PYQIVLGTFS DKGLQWLVLD QPDLAPDVLS ALKSIRTSIH PIPGRYPVET IVIRSVEEDD
     AQAKPAPLIT VPHGGPHGAM TTAFAAANTA LVLEGYTLSF PNFTGTPGYG QSNIYKLLGQ
     CGTLDVEDVH ASTLFLVNDL QLARFGPGEI FVMGGSHGGF ITAHLISQYP DVYSAAVMRN
     PVTCCGEVAG TDIPDWYFAE FGFQDDFPIK SSPPLSDLST AQKSPAIPNF DPAPHVTPSI
     FNKLYEASPT TALYNYLKER SQAPKASKHL PPVLLHIGLS DQRVSPTQGI TFYHLLKGAG
     EEVDMLMFEG EGHPLEGIEA TRVGWESTRD WFKKYGRKVS S
//
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