ID A0A0F4ZAG2_9PEZI Unreviewed; 940 AA.
AC A0A0F4ZAG2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=TD95_000780 {ECO:0000313|EMBL:KKA26823.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26823.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA26823.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26823.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA26823.1}.
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DR EMBL; LAEV01001971; KKA26823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZAG2; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
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 CDD; cd00044; CysPc; 1.
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; 2.
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:UP000033483};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 154..451
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 940 AA; 107070 MW; C5F68218996CD173 CRC64;
MYGYSDSEES DDYRRPRVPP GVDPNKEQKK TLNRRYTPQE TINGVWKRFS VRTPSSVSAI
LPFDPVKPPA AEEERANEPV SASYERAKEE CARRVNRIIK ECRRINKRYS DSGWDISWDL
QTQVGNTLNS LCSTTFDVAE AAVNPKALAP KAVKRVHEIF EKPTFLEKVS PDQVKQGAVG
NCWAIGSLIG LSSIPEAIKR LCVAYDTRIG IYGFVFYRDG KWIYSIIDDR LFLTSPVWDA
PSMHRQLLQQ IDTDMDAEKT YRQTYHTGSK ALFFGSNTDE NETWVPLLEK AYAKAHGDYA
SLDGGWTGEG LEDMSGGVSS EILTADILDP DAFWENELRL VNKEFLFGCS TGITDGGGNG
SGSRDGIAER HAYVVTDVRT LSSGVRLVKL RNPWGKARSG LWHGPWSDGS AEWTAEVQKE
VGHRFGSDSS FWISYDDFLR KWQHIDRTRL FRDADWMCSQ HWIGVDVPWK AHYHERFRFE
LTHDSAVVIV LSQLNNRYFR DLRGQYSFRL HFRLHQVNAP GAEDYIVRSD SSNLMSRSVS
VELPDLPKGR YSVWVMVTGI RNSKRSSIEE IIQSRTRNRE DDPKLEQVGL AYDLAHSRAA
AYMAEAERIR KKMKQKKASE CRKKHRRERW EREYKYQMAQ IKQTHKRKTK IKAKGDKRRE
AEKKLEEEYK EKKEKRRAER KAREKKTEEN KGEKGDQKKP ETICNCACTN PKSKSPEPAS
GSDSDSEPRP TLPADPFDDL YSDSPVSDWE AIYSDDDYTR YAQDKDVKDK VPASIYDPVE
DTSATTAPWN AFCVVGLRVY SKDKDLSLGV VVPNGEEWGW PRGERDIDNA QMNASGQRRA
GKDEEDVVKI VKIDDGEVTE IDAENMSKMA DTSERKSQGK APIRVEEQSE EDDGDDESED
DETSRLKKTR KSTRRIDSDS TGGASGTITP TSESEQPVIV
//
