ID A0A1Y2HJA9_9FUNG Unreviewed; 403 AA.
AC A0A1Y2HJA9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Subtilisin-like protease PR1I {ECO:0000313|EMBL:ORZ33172.1};
GN ORFNames=BCR44DRAFT_118787 {ECO:0000313|EMBL:ORZ33172.1};
OS Catenaria anguillulae PL171.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ33172.1, ECO:0000313|Proteomes:UP000193411};
RN [1] {ECO:0000313|EMBL:ORZ33172.1, ECO:0000313|Proteomes:UP000193411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL171 {ECO:0000313|EMBL:ORZ33172.1,
RC ECO:0000313|Proteomes:UP000193411};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORZ33172.1}.
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DR EMBL; MCFL01000038; ORZ33172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2HJA9; -.
DR STRING; 765915.A0A1Y2HJA9; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000193411; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000193411};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012214944"
FT DOMAIN 30..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 149..384
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 403 AA; 42387 MW; A0BFB883E95BA938 CRC64;
MKLLSLVATL SLALLTSAAP TAQPDVVPNQ YIVTLKPSAN LAQFSRALQS EIAREREAIS
TAASTGTAVP KFGHQVSIGS SFKAVVGVFT QDMVDKLKAN GQVAHVEPDG IVRAFETTQL
NPPSWGLARI SRRPGGNQGH YTFAADKQGE GVDVYVIDTG VDVYHPEFIG MDTRRGKNVF
RSETQWPNTD ENGHGTHVAG TVAGVRHGVA KRARVNSVKV LDKNGKGTWS GLIRGLEFAA
EEIRKSGKTA VCNMSLGGGV NEAMDAAVAS LFEAGCVVVK AAGNEQQDAC NVSPARAPQG
LTVAALAANG QSIDTSYSNF GRCVNIAAPG SRIRSAWLNR SYDTIDGTSM AAPHVAGAAA
LILGEEPWLK PQEVVDRILS RASQGVITSG LNGSPNRVVY VGK
//