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Database: UniProt
Entry: K5WRJ2_PHACS
LinkDB: K5WRJ2_PHACS
Original site: K5WRJ2_PHACS 
ID   K5WRJ2_PHACS            Unreviewed;       410 AA.
AC   K5WRJ2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   08-NOV-2023, entry version 45.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PHACADRAFT_248741 {ECO:0000313|EMBL:EKM61854.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM61854.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM61854.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM61854.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; JH930468; EKM61854.1; -; Genomic_DNA.
DR   RefSeq; XP_007391247.1; XM_007391185.1.
DR   AlphaFoldDB; K5WRJ2; -.
DR   MEROPS; A01.019; -.
DR   GeneID; 18914428; -.
DR   KEGG; pco:PHACADRAFT_248741; -.
DR   HOGENOM; CLU_038846_0_0_1; -.
DR   InParanoid; K5WRJ2; -.
DR   OrthoDB; 656651at2759; -.
DR   Proteomes; UP000008370; 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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..410
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003885884"
FT   DOMAIN          84..400
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   410 AA;  43049 MW;  7BBF78B8787D949A CRC64;
     MFSQLFVAVY LALFAAATPL TVRNSPVTVS LARRFNQTGS KTVLELDQAR ARFFQRTTAR
     KGAKASTFAA AADSDPVTNG AVSYTAEVNV GSPPTTFSLI VDTGSSNTWV GADRAYTETS
     TSRDTGAEVE VEYGSGFFFG EEFIDEVSVG GLTIPQQSIG VAEFFEGFSG VDGILGIGPT
     DLTEGTTSSG ETVTVPTFLD NAFSQGLLSS KEIGISFEPT TSDSITNGEL TFGGTDSSKF
     TGELHFVPIT STSPANEFVG IDQSVAYGST TILSETAGIV DTGTTLTLLA SNALATYEEL
     TGAVLDDVDT GLLTITAAQF ANLQSLFFTI GSTTFEFTPN AQLWPRALNT AIGGNADSIY
     LVVGDLGSDS GEGLDFINGQ TWLERFYFVF DAATPQAGFA TTQFTDATTN
//
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