ID K5WRI8_PHACS Unreviewed; 355 AA.
AC K5WRI8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 08-NOV-2023, entry version 47.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PHACADRAFT_180873 {ECO:0000313|EMBL:EKM61849.1};
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:EKM61849.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM61849.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM61849.1,
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; EKM61849.1; -; Genomic_DNA.
DR RefSeq; XP_007391242.1; XM_007391180.1.
DR AlphaFoldDB; K5WRI8; -.
DR MEROPS; A01.019; -.
DR GeneID; 18909982; -.
DR KEGG; pco:PHACADRAFT_180873; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; K5WRI8; -.
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}.
FT DOMAIN 40..345
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 355 AA; 38086 MW; 5C72869F2386CD14 CRC64;
MERDQARAKF LQQSAMQKST NATFSDTIPT ASPTNTAFQF TVFTEVGSDP TTYVLIVDTG
SANTWLGAGR PYTVMPSSHD TGVEMFVQYE TGSFIGEEFL DQLSFTEFVT IPQQAIGVAS
SFEGFEGVDG ILGLGPTDLT AGTTSNGALV PTVLDNAFSL GLIDSKEIGI FFEPVTSLSG
SDGQLALGGT DPSAIDLTSD ILFVPMTTTF PANQFVGIDQ SVAYGSTTIL SETAGIVDTG
TTLLLLASDA FATYQQLTGA VLDPTTGLLS ITPAQFANLQ SLFFNIGDTT YEFIPNAQIW
PRVYLSRNRG HWFTSGEGLD FVNGFVWLER FYFVWDAGNN QVGFATTRDT NVTSN
//