GenomeNet

Database: UniProt
Entry: R7YRL4_CONA1
LinkDB: R7YRL4_CONA1
Original site: R7YRL4_CONA1 
ID   R7YRL4_CONA1            Unreviewed;       408 AA.
AC   R7YRL4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Subtilisin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=W97_03685 {ECO:0000313|EMBL:EON64454.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON64454.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; JH767568; EON64454.1; -; Genomic_DNA.
DR   RefSeq; XP_007779771.1; XM_007781581.1.
DR   AlphaFoldDB; R7YRL4; -.
DR   STRING; 1168221.R7YRL4; -.
DR   GeneID; 19900996; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_4_1; -.
DR   OMA; DQIWYLD; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000016924; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
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:SF68; ALKALINE PROTEASE 1; 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; SSF54897; Protease propeptides/inhibitors; 1.
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:UP000016924};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..408
FT                   /note="Subtilisin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004450022"
FT   DOMAIN          37..122
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          156..385
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        164
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        352
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   408 AA;  42047 MW;  06988C22278C85A6 CRC64;
     MLSLKRGLLL LGALIPLIAA APVPQDDTFG IQAIPGKYII TLKEGIAPPK AEAHVAWVTD
     VHRRSLELER RDGKNKANRK GIEQKYNGTF TGYAGEFDDA TINAIKASAD VAAVEIDQIW
     HTYALTTQTG APWGLGSISH RNPGFTSYAY DTTAGQGTYA YVVDTGINTA HTEFGGRASL
     GYNAVSGVTH ADRDGHGTHC AGTIGSARYG VSKNTNLISV KVFEGNSGST SVILAGYNWA
     VNDIVNKGRA SKAVISMSLG GGYSAAFNNA VQSAFTSGVS TVVAAGNSNV DAANTSPASA
     PNAITVGSIQ SNNARSSFSN FGAVLDVFAP GTSILSTWIG SNTATNTISG TSMACPHVAG
     LVVYLKALEG LASPQSVRDR IVALSTTGKI TNAGAGSPNR IAYNGNGA
//
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