SUB12_TRIVH
ID SUB12_TRIVH Reviewed; 397 AA.
AC D4D1U5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Subtilisin-like protease 12;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB12; ORFNames=TRV_01047;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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}.
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DR EMBL; ACYE01000060; EFE44154.1; -; Genomic_DNA.
DR RefSeq; XP_003024765.1; XM_003024719.1.
DR AlphaFoldDB; D4D1U5; -.
DR SMR; D4D1U5; -.
DR EnsemblFungi; EFE44154; EFE44154; TRV_01047.
DR GeneID; 9580255; -.
DR KEGG; tve:TRV_01047; -.
DR HOGENOM; CLU_011263_1_3_1; -.
DR Proteomes; UP000008383; 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; -; 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; 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; 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..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000406410"
FT CHAIN 117..397
FT /note="Subtilisin-like protease 12"
FT /id="PRO_0000406411"
FT DOMAIN 35..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 125..397
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 43239 MW; AEBAD71E7A4284D2 CRC64;
MSIFKMMLIY FAILWVVNAA QLLDIDPQGV IPGAYIVVMK DRVSSLEFSS HVRWLKRTHR
RNLAKRAIPF TEGLSATWDI AGWQAYSGSF DEDTVQEILN HENVEFVEPN KEMQVASTIK
QGNVTWGLSR ISHKENSSHD YVSTYGEGEN ITFYGIDSGI DINQADFTGR ARWGINLADH
VDTDCNGHGT HTAGTVAGQK FGILKKASIV SIKILDCYGY GDITRYINGL NWAINDAKER
GLLGKSVMNI SLKTGRSRAV NEATVRAQEA GIFIAVAAGN QATSAEFYSP GSAPEVCTVG
ASTRNDTKAI FSNYGELVDL FAPREYIRST LPHNLTGLMS GTSMATPHVC GVGGLIMATE
GLAPEKVCDR LKELANPTIQ NPGFNTTNKL LYNGSGA