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Database: UniProt
Entry: K5UK79_PHACS
LinkDB: K5UK79_PHACS
Original site: K5UK79_PHACS 
ID   K5UK79_PHACS            Unreviewed;       411 AA.
AC   K5UK79;
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_200857 {ECO:0000313|EMBL:EKM50006.1};
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:EKM50006.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM50006.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM50006.1,
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; JH930479; EKM50006.1; -; Genomic_DNA.
DR   RefSeq; XP_007401202.1; XM_007401140.1.
DR   AlphaFoldDB; K5UK79; -.
DR   MEROPS; A01.019; -.
DR   GeneID; 18911538; -.
DR   KEGG; pco:PHACADRAFT_200857; -.
DR   HOGENOM; CLU_038846_0_0_1; -.
DR   InParanoid; K5UK79; -.
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; 1.
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..411
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003887170"
FT   DOMAIN          83..401
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   411 AA;  43686 MW;  ACBB0CDE48219943 CRC64;
     MFSQLFVAVY LALFAGATPL TVRSPPMTIS LARHLNSTGS RTVLELDQMR MEFLKQSATR
     KGPKSASSDT AASIPVTNGI ISYFAEVQVG YPPTNFSLIV DTGSSNTWVG GNPGNPYTPT
     STSHDTGMEV FVEYGTGLFE GEEFIDQVSL AEGLLIQNQS IGVAGFALGF SNTTDGVMGI
     GPTDLTSDTI EIGELVPTLL DNAFAQGLID EKKIGIFLKP TNNESVTTGE ITFGSIDRSK
     LTSDIHFVNI TSTFPANMSI GVNQSIAYGN TPILNNSAGI MDTGTTLILL ATDAFNMYQQ
     LTGAVLDEST GLLTITPAQY DNLQSLFFTI GGCTFEFNSN AQIWPRGLNA AINGVANMIY
     LVIGDSGSGS GSEGLSFLNG QVFLERFFLA FDAENSRVGL ATTRFTNATT N
//
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