ID SED2_ARTBC Reviewed; 596 AA.
AC D4ANG0;
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=Probable tripeptidyl-peptidase SED2;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-B;
DE Flags: Precursor;
GN Name=SED2; ORFNames=ARB_05765;
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; ABSU01000003; EFE35721.1; -; Genomic_DNA.
DR RefSeq; XP_003016366.1; XM_003016320.1.
DR AlphaFoldDB; D4ANG0; -.
DR SMR; D4ANG0; -.
DR STRING; 663331.D4ANG0; -.
DR GlyCosmos; D4ANG0; 3 sites, No reported glycans.
DR GeneID; 9521849; -.
DR KEGG; abe:ARB_05765; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_3_0_1; -.
DR OMA; WIYSKGF; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
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 PANTHER; PTHR14218:SF35; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397829"
FT CHAIN 204..596
FT /note="Probable tripeptidyl-peptidase SED2"
FT /id="PRO_0000397830"
FT DOMAIN 210..596
FT /note="Peptidase S53"
FT ACT_SITE 286
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 501
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 64861 MW; 7DC4728C1C55D1CE CRC64;
MRLLKFVCLL ASVAAAKPTP GASHKVIEHL DFVPEGWQMV GAADPAAIID FWLAIERENP
EKLYDTIYDV STPGRAQYGK HLKREELDDL LRPRAETSES IINWLTNGGV NPQHIRDEGD
WVRFSTNVKT AETLMNTRFN VFKDNLNSVS KIRTLEYSVP VAISAHVQMI QPTTLFGRQK
PQNSLILNPL TKDLESMSVE EFAASQCRSL VTTACLRELY GLGDRVTQAR DDNRIGVSGF
LEEYAQYRDL ELFLSRFEPS AKGFNFSEGL IAGGKNTQGG PGSSTEANLD MQYVVGLSHK
AKVTYYSTAG RGPLIPDLSQ PSQASNNNEP YLEQLRYLVK LPKNQLPSVL TTSYGDTEQS
LPASYTKATC DLFAQLGTMG VSVIFSSGDT GPGSSCQTND GKNATRFNPI YPASCPFVTS
IGGTVGTGPE RAVSFSSGGF SDRFPRPQYQ DNAVKDYLKI LGNQWSGLFD PNGRAFPDIA
AQGSNYAVYD KGRMTGVSGT SASAPAMAAI IAQLNDFRLA KGSPVLGFLN PWIYSKGFSG
FTDIVDGGSR GCTGYDIYSG LKAKKVPYAS WNATKGWDPV TGFGTPNFQA LTKVLP
//
