ID   B0D7V7_LACBS            Unreviewed;       734 AA.
AC   B0D7V7;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=LACBIDRAFT_319100 {ECO:0000313|EMBL:EDR09470.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR09470.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547099; EDR09470.1; -; Genomic_DNA.
DR   RefSeq; XP_001879819.1; XM_001879784.1.
DR   AlphaFoldDB; B0D7V7; -.
DR   STRING; 486041.B0D7V7; -.
DR   MEROPS; S09.004; -.
DR   GeneID; 6075300; -.
DR   KEGG; lbc:LACBIDRAFT_319100; -.
DR   HOGENOM; CLU_014230_1_1_1; -.
DR   InParanoid; B0D7V7; -.
DR   OrthoDB; 2877590at2759; -.
DR   Proteomes; UP000001194; 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; 1.
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:UP000001194}.
FT   DOMAIN          63..142
FT                   /note="Acylamino-acid-releasing enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19283"
FT   DOMAIN          499..722
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   734 AA;  79211 MW;  CBCB66245A51EBC9 CRC64;
     MHYTTLAEIP VPTSAQFLGK DTAQVRYSVR NHVRNVNTTL IKTITGLLAS DGPSLSPLLD
     FDLVASVVSP SGKRRAVLRE VKSGAAQGSR FVEIWCDDLL EASVDVSERH GAFYADEYLS
     SLAFSPSELA IVYTAESIQP KSNNPYHRFR FQPDFGEGLD GKKRSTTFVL RWKPSTLEND
     QNDTPVIALL PLSIPSHICL GQAIFSPNSE NIIYGTGYEY SRDGRMLGLK GCYNRPTGIW
     QVIIKNDSTE SITCTSQKLT PSHLSCRSPR SISSAGSSTL LWLSCKTGGA HISTSTLHAL
     DITSDKSPID PAAIEAAVDP IVDVVMNPIR NRFPGLYPSY NMPYSPVVKL QSQNHILISS
     AWGSRFTILL VSVKDRSVRD LTPASEELFS WSILAADGSC RFICSRSSPS IPYEIILGTL
     NDDGDVAWKV LDRPMLTEQV SNKLSTIRTS IVEIPGRYPT ETIVVQSINS GASCLAPCIT
     VPHGGPHGTT TTAFAAATTA MVLEGYTLSL PNYTGSLGFG ESSVQALIGN CGALDVQDCV
     ASINHLIDLG VAEHGPGKQF VMGGSHGGFL TAHLIGQYPS IFSAAVMRNP VISSGEISTS
     DIPDWYYSEF GFDYPVSTAP FSHLSDSGPI PLMPAETFSK LRAASPIAHI NNVTVPVLLL
     IGNCDRRVAP TQGIEYYHAL KSHFGSEGAV EMLVFEGESH PLDGVEAGKV VFEAGRDWFK
     NCKSKFSSLG DGLA
//