ID SU11B_COCP7 Reviewed; 400 AA.
AC C5PFR5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Subtilisin-like protease CPC735_047380;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN ORFNames=CPC735_047380;
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC activity that contributes to pathogenicity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACFW01000049; EER23368.1; -; Genomic_DNA.
DR RefSeq; XP_003065513.1; XM_003065467.1.
DR AlphaFoldDB; C5PFR5; -.
DR SMR; C5PFR5; -.
DR GeneID; 9690983; -.
DR KEGG; cpw:CPC735_047380; -.
DR VEuPathDB; FungiDB:CPC735_047380; -.
DR HOGENOM; CLU_011263_1_3_1; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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; 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; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Virulence; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..118
FT /evidence="ECO:0000250"
FT /id="PRO_0000407004"
FT CHAIN 119..400
FT /note="Subtilisin-like protease CPC735_047380"
FT /id="PRO_0000407005"
FT DOMAIN 35..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 128..400
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
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 346
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 42313 MW; 3F541573BE484FAC CRC64;
MARINVVVSF LAALAVVQAA QLLNLDGQKD AVPGSYVVVM NDGLSGLDFE SHVKSMAKVQ
KANALKRDFD NTADGVKFKY NINGWQAYSG KFDNKTIQSI LDDPRVNYIE PQRTFRAFGW
VTQDNAPSWG LGRISHTSRG RMDYVYDSSA GENVTVYSVD SGVDISHPEF EGRAIWGVNA
ADNSDVDQIG HGTHTSGTIA GKTYGVAKMA KIVAVKVLDA GGQGTNGGII QGINWAVNHA
RQNNVTGKAV MNMSFGGGLS RAINEAASSA VRAGIFMVAA AGNNNEDARY TTPASARGVC
AVGASTQNDL KARFSNWGPT LAVYAPGDRI WSAMPDGGRD VMRGTSMAAP HVAGVAAVLI
SSEKIGTDRL CERIKELSVS SIQSPGADTT DKLLYNGSGQ
//
