ID B0DA02_LACBS Unreviewed; 463 AA.
AC B0DA02;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 08-NOV-2023, entry version 75.
DE SubName: Full=Aspartic peptidase A1 {ECO:0000313|EMBL:EDR08438.1};
GN Name=LbPR_A9 {ECO:0000313|EMBL:EDR08438.1};
GN ORFNames=LACBIDRAFT_190404 {ECO:0000313|EMBL:EDR08438.1};
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:EDR08438.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DS547101; EDR08438.1; -; Genomic_DNA.
DR RefSeq; XP_001880663.1; XM_001880628.1.
DR AlphaFoldDB; B0DA02; -.
DR STRING; 486041.B0DA02; -.
DR MEROPS; A01.013; -.
DR GeneID; 6076312; -.
DR KEGG; lbc:LACBIDRAFT_190404; -.
DR HOGENOM; CLU_013253_1_1_1; -.
DR InParanoid; B0DA02; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT DOMAIN 142..460
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 160
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 173..181
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 463 AA; 48634 MW; DDE8F0ADE134552B CRC64;
MVTLPLKRME QARNVHPLIL LQQHINRSNR RLARISGRTQ PTVEFLEREL QKRVYAVEGS
EGLERRFNRN GVPGSEENTL EKRYNRFGVP EKAKSPVGAD SLAVLKKGSG NAGQQKSNVA
VANTPTANSS LGLDIEAQDV GYLATVKMGT PPRDFLILMD SGSADLWVGA EACQSQNGGG
CGNHNFLGPL SSSSFADSQA PFKVTYGTGE VSGTIVQDNI NIAGLALDAH TFGVALVESV
DFSGAQTPFD GLMGLAQSTL SEQQTPTPIE SLAQAGLVTD AIVSYKISRL ADNKNDGEIT
FGGLDATKFD PKTLTTVPNV NKQGFWEAGM DAATVNGKDT GLKGRTAILD TGTTLIVAPA
SDAAAVHAAI PGAQSDGQGG FTLPCTTTAS VALTFGGQTF TIDPRDLAFQ PINANDPQGD
CVSGIASGNI GGAQEWLVGD VFLKNAYFST DVTKNTLSLA KLV
//