ID B8PKJ7_POSPM Unreviewed; 416 AA.
AC B8PKJ7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 08-NOV-2023, entry version 63.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED78605.1};
GN ORFNames=POSPLDRAFT_102180 {ECO:0000313|EMBL:EED78605.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED78605.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; EQ966428; EED78605.1; -; Genomic_DNA.
DR RefSeq; XP_002476205.1; XM_002476160.1.
DR AlphaFoldDB; B8PKJ7; -.
DR KEGG; ppl:POSPLDRAFT_102180; -.
DR HOGENOM; CLU_013253_8_3_1; -.
DR InParanoid; B8PKJ7; -.
DR OMA; WEVRCEK; -.
DR OrthoDB; 1611889at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..334
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 22
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 220
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 35..40
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 416 AA; 44405 MW; E31C8D48A12CC172 CRC64;
MYGSAYLVQV SIGGQEFQVL LDTGSADLWV VSSDCTTSDC QGIATFDISE SNSLNLTSTD
FHLDYLIGSV SGTVGTDTVT FGPYEISSQV FALASNTTGL DLSGTGYSGI LGLAFPAEAS
IPSTTGRTLV ENIFASLNDT DRFFAFKLGS NATGSSFTIG QLDPAYANTT SALTYTPVSS
DGSGYNYWKL PLQSLTINST TFDLSKSRVK GASSPIAVLD TGTTLVLGPT SDVDRFWQSV
GGARKTDAGW QVRCNRAVIV GFVIGDDSSQ KEYVLDPADV SWDENTAQGD WCMGGIQGND
GVFSGDWLLG DTFLRTSLKH HIQNVYVAQR VFASNQSASI GLLGTTNATS ALTQFRQTRG
DDSTPPARVR AHAPNHNLTG ADVCGIAVSC GFVFGVLLTL VWYSCMEWRA KKRRMY
//