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
//