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
//