ID A7EPL9_SCLS1 Unreviewed; 669 AA.
AC A7EPL9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Peptidase S53 domain-containing protein {ECO:0000259|PROSITE:PS51695};
GN ORFNames=SS1G_07268 {ECO:0000313|EMBL:EDO04785.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO04785.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; CH476629; EDO04785.1; -; Genomic_DNA.
DR RefSeq; XP_001591822.1; XM_001591772.1.
DR AlphaFoldDB; A7EPL9; -.
DR MEROPS; S53.007; -.
DR EnsemblFungi; EDO04785; EDO04785; SS1G_07268.
DR GeneID; 5487945; -.
DR KEGG; ssl:SS1G_07268; -.
DR VEuPathDB; FungiDB:sscle_06g050510; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; A7EPL9; -.
DR OMA; EFYEHEH; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 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 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..669
FT /note="Peptidase S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030164939"
FT DOMAIN 233..668
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 190..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 586
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 669 AA; 72966 MW; 05BC55C49A0E94AC CRC64;
MLVPVSVVCL AIAAIANAAP SSTKYVVHEK RNAAPSDWVK GSRIEGSAVV PMRIGLTQTN
LDNGYEYLME LSDPESPKYG KYWSSKEVHE KFAPPEETLK SVKDWLTSSG IHHSRISHYE
NKGWLAFDAS VEEAERLLQA KFHEHEHKYS SSVRVGCDEY HLPEHLVPHI DYITPGVKLA
PVKKRSVKTK RSTSYLSKRR NRLTKGNAPS KNYEWTPSAA AGLSSDLQGC GSNMTPTCIK
AMYKIPTATL NASGNSLGLY EQGDYFAKSD LDLFYAHHAP WVPQGTYPIP ALIDGANFSV
PPYSSLNGGE SNIDIDMAFA LLYPQTVTLY QVDDQIYEPE EIATTNLFNT FLDALDGSYC
NFKAYGETGD NPSIDPVYPD PQPGGWNGTR QCGVYKPTKV ISASYGQAES DLPIAYTKRQ
CNEFMKLGLQ GHSILTASGD YGVASFPGDG DANGCLGPEG KIFNPQYPGN CPYITSVGGT
MLYADQTVKD AESVMHVDLG GTASNFTSSG GFSNYFPIPS YQKSAVETYF ETAKLSYPYY
SELEVNVNTT KGLYNRIGRG YPDISANGAE FRAYLNGVDE HWYGSSLASP LFASVFTLIN
EERFAVGKGP IGFVNPTLYK NPGALNDIVN GTNVGCGTEG FAAVKGWDPA TGLGTPNYPK
LLKLFLSLP
//
