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Database: UniProt
Entry: B0DA02_LACBS
LinkDB: B0DA02_LACBS
Original site: B0DA02_LACBS 
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
//
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