ID G2Y5J4_BOTF4 Unreviewed; 1022 AA.
AC G2Y5J4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Similar to calpain {ECO:0000313|EMBL:CCD47934.1};
GN ORFNames=BofuT4_P112440.1 {ECO:0000313|EMBL:CCD47934.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD47934.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
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; FQ790289; CCD47934.1; -; Genomic_DNA.
DR AlphaFoldDB; G2Y5J4; -.
DR STRING; 999810.G2Y5J4; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_006072_1_0_1; -.
DR InParanoid; G2Y5J4; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF397; CALPAIN CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 173..456
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 376
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1022 AA; 115331 MW; 1313A3709CA7A6D3 CRC64;
MSSTASSSDS DNSRRRRRQG PRPSPPPPPP PFQGNNKKSK KRNKYVAPQD TIDKLWSRFS
VSKFSKATKV LPNAAPFAKG TSAKTVIVPP PGPQNQLVSE DFERAVQECR AKVKKLVKEC
RRVNMRFRDA SFDIDWDLKW EKGNCLNTLD EIRFEVCKQA LLNPTSSGPK AVKRVHEIFD
KPTFLGDKIS PSDVKQGSLG DCWLMASLTA LANTDDGIQR ICVEWDTNGE WIISIIDDKL
YLKSPDWDSP SVHRHLLEQT DREDVEKDYR KTYQTGSQSL FFAQCKDPNQ TWLPLLEKAY
AKAHGDFFSL SGGWIGEGLE DLTGGVTTEL LTSDILDTDE FWHNEILKVN KEFLFGCSTG
LLDYGYGNRD GISEGHAYVI MEARELSTGE RLLKLRNPWG KIKKGNWEGP WSDGSKEFTP
EAQIELNHKF GNDSVFWISY QDLLRKYQHF DRTRLFMDSP DWRLTQDWVS VEVPWRSEFE
QKFTITLKKE SPIVLVMSQL DDRYFIGLHG QYNFRLQFRV HEINSPDEED YIVRSHGNYL
MRRSVVAELK SLSAGTYTVY MMVIAERDKD RQSVEDVVKD ELSQREDNEK LAKVGLAYDL
AHQKGLSHME LRIKSRKALD KAKARESRIA KRKVLWEKRH IAREILRKQK KKNYEKREGK
AAKDTEWAKE QEERELKDQG VQTEDIPEVQ VEKQDKSMQT EDLNEESMNT TVDTQPTNER
DKAVQTEGFT PSSNESQTTP VTPKSNGSSP RSPYTMISRS GSNRRKSLPP PPSFVNLRRN
PSRPPNHGRG PPPPSSKPGL YVTSEGESSA SPLSDYDMYS DDDPTLKPRN QSTEPKRPKE
REAGEDEPEP WNAVCIVGFR VYSKDEGLVL TVCEEGMEEV IELKEDSEAG TDGDVEDAED
EDCHEKKGGN GEDLKLKDTA AGNDSTPSDV AIKIEPDKDL NVAISDSPHE ITGTSSSVNN
GLEEIPTETQ SQVATKSLEI ETNGDAQQKS ALGISEGATD DIVKESDSQS GIATSSASSN
CT
//
