ALP_ACRCH
ID ALP_ACRCH Reviewed; 402 AA.
AC P29118;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alkaline proteinase;
DE Short=ALP;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=ALP;
OS Acremonium chrysogenum (Cephalosporium acremonium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1368696; DOI=10.1271/bbb1961.55.471;
RA Isogai T., Fukagawa M., Kojo H., Kohsaka M., Aoki H., Imanaka H.;
RT "Cloning and nucleotide sequences of the complementary and genomic DNAs for
RT the alkaline protease from Acremonium chrysogenum.";
RL Agric. Biol. Chem. 55:471-477(1991).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; D00923; BAA00765.1; -; Genomic_DNA.
DR PIR; JU0332; JU0332.
DR AlphaFoldDB; P29118; -.
DR SMR; P29118; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..120
FT /evidence="ECO:0000255"
FT /id="PRO_0000026986"
FT CHAIN 121..402
FT /note="Alkaline proteinase"
FT /id="PRO_0000026987"
FT DOMAIN 32..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 128..402
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 382..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 402 AA; 42099 MW; 8D030CCD42D918E1 CRC64;
MVTLRRLAVL LGAIPAALAA PTTQKREVVP NKYIVTLKEG ASNFDSHISW VSDIHKRSLS
RRSTAGIEKE FHIDTFNAYV GEFDETTIEE IKNNPDVLEV EEDQIWHLFD EQDEGEFSTA
ALVTQNGAWG LGTISHRQPG STSYIYDDSA GSGTYAYVVD TGILESHNEF SGRAITGYNA
VGGSNADTNG HGTHVAGTIG GRTYGVAKNT NLIAVKVFRG SSSSTSIILD GFNWAVNDII
NRGRQNKAAI SMSLGGGYSS AFNNAVNTAY SRGVLSVVAA GNDNQNAANY SPASAANAIT
VGSIASNWAR SSFSNYGSVL DIFAPGTSIL SAWIGGNSAT NTISGTSMAT PHVTGVVLYL
QALEGLTTSG AAARLNALAT TGRVSNPGSG SPNRILYNGN GA
