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Database: UniProt
Entry: K5VTJ9_PHACS
LinkDB: K5VTJ9_PHACS
Original site: K5VTJ9_PHACS 
ID   K5VTJ9_PHACS            Unreviewed;       269 AA.
AC   K5VTJ9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE   Flags: Fragment;
GN   ORFNames=PHACADRAFT_200973 {ECO:0000313|EMBL:EKM50130.1};
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:EKM50130.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM50130.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM50130.1,
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}.
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DR   EMBL; JH930479; EKM50130.1; -; Genomic_DNA.
DR   RefSeq; XP_007401321.1; XM_007401259.1.
DR   AlphaFoldDB; K5VTJ9; -.
DR   GeneID; 18911546; -.
DR   KEGG; pco:PHACADRAFT_200973; -.
DR   HOGENOM; CLU_1036479_0_0_1; -.
DR   InParanoid; K5VTJ9; -.
DR   OrthoDB; 1469204at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF89; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 2.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT   DOMAIN          1..269
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   NON_TER         269
FT                   /evidence="ECO:0000313|EMBL:EKM50130.1"
SQ   SEQUENCE   269 AA;  28638 MW;  F0AFF846E7ACA105 CRC64;
     TFGNVLVDTG SSSLWVGASS PYIPGPNSKA TGETYSVGYD EGGATGLVYL DTVTIGSATV
     TNQHIGAANQ TSLPADLYPL DGFIGLSFNG SNAHTISGIS EPTNTFLDSL VEEGVIGQAL
     WSMVVPALDV AAGQQVGEGE ILFGGYDASK VEGEITWLDV TNEFGLFAWS FNMDGIYFGD
     SQISSDDFRT VSSTIHYSMG GQNFTLTSEQ YVIPPNAYAA LNITDDGRHY TWFSSAGYQA
     DAILGQAWLQ FFYSIYDVGN TKIGFANYA
//
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