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Database: UniProt
Entry: K5WML5_PHACS
LinkDB: K5WML5_PHACS
Original site: K5WML5_PHACS 
ID   K5WML5_PHACS            Unreviewed;       420 AA.
AC   K5WML5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   08-NOV-2023, entry version 42.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PHACADRAFT_132970 {ECO:0000313|EMBL:EKM60424.1};
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:EKM60424.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM60424.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM60424.1,
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; JH930468; EKM60424.1; -; Genomic_DNA.
DR   RefSeq; XP_007389884.1; XM_007389822.1.
DR   AlphaFoldDB; K5WML5; -.
DR   GeneID; 18908248; -.
DR   KEGG; pco:PHACADRAFT_132970; -.
DR   HOGENOM; CLU_013253_1_4_1; -.
DR   InParanoid; K5WML5; -.
DR   OrthoDB; 4946at2759; -.
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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..420
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003885713"
FT   DOMAIN          109..417
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        140..145
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   420 AA;  44318 MW;  755A0BB8E8456175 CRC64;
     MFCKATLVSV VLALLAIANP IAQNSGVSVA LGKRSTLTRP DGTFDHEKAV LHNVKTQKYY
     QRNIRNVLAN KGSLPEGWEA REFRSVPAGL QKRATGSVSL TDEDDDAEWL GGISIGTPSQ
     PFIVQFDTGS SDLWIPSSSC SSSICSGKHK YKASDSVTTS KKGGNFSLVY GDESSVSGPI
     YTDVVTVAGL TATGQHFSPA TTLSSEFADD PTDGVLGLAY LAASRLNATP FFNTLISQGR
     VSACEFGFKL ASKGSELYLG GTDTSLYTGS IEYHSINQSM GFWQTTGAKS VVGSTSPNTN
     LETIIDSGTT IMYGPPSAIK TFYAAVSGSE VVNATEGFYS YPCNSPPAVG FSWGNKTWQI
     SSDNFNLGQV NNGSSQCVGA LAGQDLGLGS NVWLLGDSFM KNVYTAFSFD KNAVGFASLA
//
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