SUB1_ARTBC
ID SUB1_ARTBC Reviewed; 533 AA.
AC D4AKU9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Subtilisin-like protease 1;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB1; ORFNames=ARB_04944;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
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).
RN [2]
RP INDUCTION.
RX PubMed=19942661; DOI=10.1099/mic.0.033464-0;
RA Staib P., Zaugg C., Mignon B., Weber J., Grumbt M., Pradervand S.,
RA Harshman K., Monod M.;
RT "Differential gene expression in the pathogenic dermatophyte Arthroderma
RT benhamiae in vitro versus during infection.";
RL Microbiology 156:884-895(2010).
CC -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC activity that contributes to pathogenicity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is up-regulated during infection.
CC {ECO:0000269|PubMed:19942661}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE36008.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000002; EFE36008.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_003016653.1; XM_003016607.1.
DR AlphaFoldDB; D4AKU9; -.
DR SMR; D4AKU9; -.
DR STRING; 63400.XP_003016653.1; -.
DR EnsemblFungi; EFE36008; EFE36008; ARB_04944.
DR GeneID; 9522137; -.
DR KEGG; abe:ARB_04944; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_5_1; -.
DR Proteomes; UP000008866; 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 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000397778"
FT CHAIN 117..533
FT /note="Subtilisin-like protease 1"
FT /id="PRO_0000397779"
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..512
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..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..501
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 533 AA; 55699 MW; 32B69B347BD37D4E 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 FPGESFPGES
FPGESAPAPA PMPPSPQHPH TPYPGGDNFD FDGLWKKYFG GEHWRKMFSS FWN
