SED4_ARTBC
ID SED4_ARTBC Reviewed; 600 AA.
AC D4AIK6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable tripeptidyl-peptidase SED4;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-D;
DE Flags: Precursor;
GN Name=SED4; ORFNames=ARB_04101;
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], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at
CC acidic pHs and is involved in virulence. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:21247460}.
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DR EMBL; ABSU01000001; EFE36579.1; -; Genomic_DNA.
DR RefSeq; XP_003017224.1; XM_003017178.1.
DR AlphaFoldDB; D4AIK6; -.
DR SMR; D4AIK6; -.
DR EnsemblFungi; EFE36579; EFE36579; ARB_04101.
DR GeneID; 9522308; -.
DR KEGG; abe:ARB_04101; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_3_0_1; -.
DR OMA; YHEMASG; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..202
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397835"
FT CHAIN 203..600
FT /note="Probable tripeptidyl-peptidase SED4"
FT /id="PRO_0000397836"
FT DOMAIN 212..600
FT /note="Peptidase S53"
FT ACT_SITE 288
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 292
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 504
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 65404 MW; 23DCD1D17D32E386 CRC64;
MVSFTLRAIG ACLIGLPALI TAAPTSHVSN DFHVVEQLNG VPQGWVQEGS PAPSTQMKFK
LALVQGKTAE FEQRVMDISN PKHADYGKFM SREELDAFLQ PSSQVKDSVF NWLASEGISK
RSVKANTDWL TFTTSIATAE KLFNTRFYTF KNTADGSQII RTLKYSVAAS AAPYVQMVQP
TTKFSAPRPE LSSVFTSDLE ITSSANVDCN VTITPDCIRE LYKMGNTFAK KDPRNRLGIS
GYLEQYARLD DFSTFIDMFV PSLKGTTFDF KSIEGAKNEQ NSSLDSVEAS LDVDYAIGLS
GALSTYYGTA GRGKLIPDLD QPNITENNNE PYIEQLFYLL DLPDSELPAV LSTSYGENEQ
SVPPTYSSVV CSLFGRLGAR GVSVIFSSGD TGVGSACQSN DGKNTTKFNP IFPAACPFVT
SVGGTRQINP EVAIHFSSGG FSERFARPWY QELDVRHYLG HELEKGKWDG MYNPYGRGFP
DVAAQSYKFA TRDHGKTIGV SGTSASAPLF AGVVSILNSI RLAHNKPRMG FLNPWLYTIG
RSGFTDIVHG GSDGCTGTDM YSHLPTPYVP GASWNATKGW DPVTGLGTPN FEKLSKLVLI
