ID   K5VYH5_PHACS            Unreviewed;       583 AA.
AC   K5VYH5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PHACADRAFT_187232 {ECO:0000313|EMBL:EKM51840.1};
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:EKM51840.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM51840.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51840.1,
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; EKM51840.1; -; Genomic_DNA.
DR   RefSeq; XP_007399635.1; XM_007399573.1.
DR   AlphaFoldDB; K5VYH5; -.
DR   GeneID; 18910410; -.
DR   KEGG; pco:PHACADRAFT_187232; -.
DR   HOGENOM; CLU_013253_8_2_1; -.
DR   InParanoid; K5VYH5; -.
DR   OrthoDB; 1598969at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF92; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..583
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003885132"
FT   TRANSMEM        521..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..412
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          477..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  60010 MW;  54D5F9A6D96DB3BA CRC64;
     MVSSIASTSF VTLALCAALT HAAPSAPHAR RAAPSGLSMK ASGTGVRIMD LGASSAGGSG
     SDGGEAVTDV QDVLYKIEIG LAGGTYVVQM DTGSADLWIY APNDNLKLTN QSGITTNLTY
     GTGSAEGEIV FGELRLGNYT IPSQAFVSAS SAEDFSFFDQ GVVGILGLSF DDTNLSPINA
     AIEDAWGSSS TLGRTPISSI FAQDPSVPDS FDIQLDRSSD LDDTSTGTFL ISEHLDDFAN
     ITSQPQLPRQ AVGRWSVPLD GMSVNGQVFA FGPSSISTVP AGKIAALLDT GYSFPPLPPD
     AVDAIYSTVP GAVKFSDSIP QWLVPCDAGT NVTFTLGGKP FPVHPLDLTA VGQTVVTQNG
     QDQNVTYCYN SYQYLDLDPT DFSGFDAILG DAFLRNVYAS FNYGGSPSSG NESFVQLIST
     TDLDAAWPDF AASRAQTLAA LPPTIDPATL ASLVNGDDGD TTDDSVAGAD AVSSSVSASS
     TVPSTSTTAV RGTSLPTGAA SSAGDSADDK LYALVDKYGP VIVGLLAGNI VVGVILCAIA
     LAACMRGVVK GGAQTRNINS SYAPVRFKEA EVHGGGDSRS YQD
//