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Database: UniProt
Entry: K5WFK9_PHACS
LinkDB: K5WFK9_PHACS
Original site: K5WFK9_PHACS 
ID   K5WFK9_PHACS            Unreviewed;       424 AA.
AC   K5WFK9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   08-NOV-2023, entry version 48.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PHACADRAFT_265944 {ECO:0000313|EMBL:EKM48967.1};
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:EKM48967.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM48967.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM48967.1,
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; JH930614; EKM48967.1; -; Genomic_DNA.
DR   RefSeq; XP_007402480.1; XM_007402418.1.
DR   AlphaFoldDB; K5WFK9; -.
DR   GeneID; 18919254; -.
DR   KEGG; pco:PHACADRAFT_265944; -.
DR   HOGENOM; CLU_013253_1_4_1; -.
DR   InParanoid; K5WFK9; -.
DR   OrthoDB; 4946at2759; -.
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; 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:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..424
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003885560"
FT   DOMAIN          109..420
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        140..144
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   424 AA;  44548 MW;  4E01034144420E58 CRC64;
     MQTKLSIALL ALVPLLAMAS PAPAEPARVP FARKRSFQNE NGVVDIEALK THVAEVQAKV
     ARGFNAFKAN TGKVHPNDNG VRPAPVKRNY VKRATGKDPL TDDLDGDLWQ GGVSVGTPLS
     AFTVDFDTGS SDFFLPGPDC TENCEGHKVF ETGQSSTAVD QHKTFEIEFA DDSTVSGEIF
     TDTVNLAGLT ATKQAVVAAT QYSSGFAIAN SPPDGLLGLA FESIASTGDS PVFQTLVTQG
     QTTESVFGVT LLDNGGELFL GGTDTTAFTG SLAFANLIVT DPPAFWEITA SGVSVGSRRV
     VTEAQDAIVD TGTTLLIVDP NSANEIFAAI PGAENAERTL GEGFFTIPCD EIPSDVSFTV
     AGKAFTLSAD TLNFGQLEEG SSQCVAGIMG ADEGFWILGD VFLRNLYTEF DFGNLRVGFA
     PVVS
//
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