ID SUB1_TRIVH Reviewed; 518 AA.
AC D4DIW9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Subtilisin-like protease 1;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB1; ORFNames=TRV_07130;
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; ACYE01000415; EFE38217.1; -; Genomic_DNA.
DR RefSeq; XP_003018862.1; XM_003018816.1.
DR AlphaFoldDB; D4DIW9; -.
DR SMR; D4DIW9; -.
DR MEROPS; S08.025; -.
DR GlyCosmos; D4DIW9; 2 sites, No reported glycans.
DR GeneID; 9581506; -.
DR KEGG; tve:TRV_07130; -.
DR HOGENOM; CLU_011263_1_5_1; -.
DR OrthoDB; 380531at2759; -.
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; 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..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000397780"
FT CHAIN 117..518
FT /note="Subtilisin-like protease 1"
FT /id="PRO_0000397781"
FT DOMAIN 34..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 126..400
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 175..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 54189 MW; 94D53CA76461E701 CRC64;
MGVFRFISIS LAAVSAANAA QILSMPHAQT VPNSYIVMMK DDTSDDDFNH HQSWLQSTHT
HNITRRATIQ NAGMRHKYNF SKMKGYSGIF DEETIKDIAK DPKVMFVEPD TIISVHGKVE
QSNVPSWGLA RISNPQPGAG SYIYDSSAGE GITVYSVDTG VDVNHEDFEG RAIWGSNQVN
DGDDRDGSGH GTHTSGTMVG KEFGIAKKAK LVAVKVLGND GSGPTSGIVA GINWSVEHAR
QNGGTKKAVM NMSLGGSSSS ALNRAAAQAV EQGMFLSVAA GNDNQDAQSS SPASEPSVCT
VGSSAEDDSR SSFSNWGPAI DLFAPGSNII SARPGGGSQS MSGTSMAAPH VAGLAAYLMA
LEGISGGAVC DRLKELGTSS ITDAGPGTPT NVLINNGGAK GGKPNPNPAP SPSPSPSQPS
EPQQPTPSQP GQPGEPFPGE PQQPTPSQPG QPGEPFPGEP FPGEPFPGEP FPGESAPAPA
PQHPHTPYPG GDNFDFDGFW KKYFGGEHWR KMFSSFWN
//
