ID K5VYG6_PHACS Unreviewed; 383 AA.
AC K5VYG6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PHACADRAFT_31478 {ECO:0000313|EMBL:EKM51654.1};
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:EKM51654.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM51654.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51654.1,
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; JH930476; EKM51654.1; -; Genomic_DNA.
DR RefSeq; XP_007399254.1; XM_007399192.1.
DR AlphaFoldDB; K5VYG6; -.
DR MEROPS; A01.019; -.
DR GeneID; 18919678; -.
DR KEGG; pco:PHACADRAFT_31478; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; K5VYG6; -.
DR OrthoDB; 656651at2759; -.
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:SF87; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
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..383
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003890377"
FT DOMAIN 80..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 383 AA; 40417 MW; 2965C015518D0ECE CRC64;
MIFFAVSILT LAALLAAFPT NTRNNAASIP LTRRLNVPSG QTLPEIDKAR AQAFKSTAAQ
RAQKDSSITP VPVTNTAVLY TAEVLIGEPP QTFDLIVDIG SSSTWIGANT SNPYTPTNTS
TATSTILCVQ FIEYGSGLFI GLEYNDTVTI GGLSIPNQTI GDAQWALGFE AGVDGILGLG
LLDAYEVGIA FAPPNSTSDP NGELTFGGVD SSKFNGDLTY TNITTTYPAM DYVGFNQSVT
FGNQTLLSNT AGIVDTGTTL VELASDAFAT YQNLTGAVLD STTGLLTISS AQLDNLPSLF
FIIENATFEL TSNAQLWPRA LNSAIGGKND SIYLIVSDLG TPSGEGLDFV NGYAFLERFY
AVYDTGNSRV GFATTPFTFS TSN
//
