ID A7EPM3_SCLS1 Unreviewed; 803 AA.
AC A7EPM3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=SS1G_07272 {ECO:0000313|EMBL:EDO04789.1};
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:EDO04789.1, 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 -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; CH476629; EDO04789.1; -; Genomic_DNA.
DR RefSeq; XP_001591826.1; XM_001591776.1.
DR AlphaFoldDB; A7EPM3; -.
DR STRING; 665079.A7EPM3; -.
DR EnsemblFungi; EDO04789; EDO04789; SS1G_07272.
DR GeneID; 5487949; -.
DR KEGG; ssl:SS1G_07272; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_006072_3_1_1; -.
DR InParanoid; A7EPM3; -.
DR OMA; HAYESYI; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF00648; Peptidase_C2; 2.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 185..489
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 653..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 413
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 433
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 803 AA; 91662 MW; 903B7512F5FF1FD6 CRC64;
MTKARSFDVG AIQLRCPNSW DDVLTKITTQ KSMTAVTSTS STQKALNTFW KNKLTSDEII
TQSPNVLPKH IYKRLAGQQK SKDNISGCSV NTSYDAAVKE CQAKVAAIVA ECRRNNIKYT
DNDFDLDDMD YCLKPLTVTV PGTLNGEEHT QTGPPKKTNN VKTVITRTGI VKLTAAEVRG
PACAKRVGDI FENPKFFIEH EAHVQDIRQG SEGDCWFISS LACLTIDEAF PRLINKLCPE
KARNEEIGVY GFVFYRDGEW VSEIIDDKLY LTNPDYDDCD DDRRSVWDRS HGRLDPEFSR
TEYKKAFQTG SNALFFGSCA DPNETWLPLI EKAFAKVHGD FDSINGGWPG EGVEDLTGGV
TTKLISSDIL DKDNFWTQGL LKVGNEFIFN AGTRNYTHPD LEELGRQGIE DDHAYSVLRA
VEYQGNRLCL LKNPWGETEW NGPWSDGSKE WTREALDALN HKFGNEGIFW MPYEDFLSRY
DEIWRTRLFH CDWLCWNVAQ HWTTVNVPWS GDYNETFFHF TIFEPTTTVV VLSQLDNRYF
GGFAGQYTYS LSFYLHSSGQ KSHIVRGYSS GDRSATTEIF LEAGTYEVFL QITGYRDDTL
PKVEDVVKQN WLSRRDKLIQ IGLKHDMAYA KGTIDENFSK KNERMSLATS AILTPPITPP
VTPSTPSSEN APEMDKHAWN ASCIIGLKVY TYQTIATIGL GKATDTDEVE TIENADEKGQ
AIRKILSTLD DTFSSNLHKM KIRTKKKSLK VKWKFHGRNW KEETGLCDEK KGGKRERKEK
KRERKRERKE EKSREKRKRK RKL
//
