ID A0A094BCU1_9PEZI Unreviewed; 1036 AA.
AC A0A094BCU1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=V494_04761 {ECO:0000313|EMBL:KFY37423.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY37423.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY37423.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY37423.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJW01001609; KFY37423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BCU1; -.
DR STRING; 1420907.A0A094BCU1; -.
DR HOGENOM; CLU_006072_1_2_1; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000029288; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
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; 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; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000029288};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 158..447
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 18..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 391
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1036 AA; 116280 MW; 793EECEEFC3C8DDA CRC64;
MATFSGPDVE DVRTMINRCH GESSEAVTPK ASTTTTKKSS KKQAPQEIID EFWTKFNTKT
PGKATTILPT DSYAKKVGDS TPKGTITSLS SSASYDEAVR TCKLKVAKIV KECRRANQKY
RDPHFDIEFD LKWGRRDCLE TLKTPNREKS IFRPKSVKRV GDIFENPQFF INGPEAKDIR
QGQDGDCWLL AALCTLTNKK GLIEKVCVAR DETVGVYGFV FYRDSEWRSE IIDDKLYLTK
PDYDESILER LLWEDRERVS SEDEYKKVYQ TNSGALYFAQ CEDPNETWLP LLEKAYAKAH
GDFATIDGGY TGEGIEDLTG GVTMELFSTD ILDKDAFWTN ELLRVNEEFL FGCSSCLFAG
WGERKGIIEG HAYSIMRAVE MDGERLLLLK NPWGKGEWTG PWADGSKEWT PEWMTKLNHR
FGDDGAFWIS YADFLKKYQT FDRTRLFTDD WKVTHQWTSL TIPWSVDYNS TKFAFTINKP
SSVVVVLNQL DGRYFRGLEG QYTFELSFRI HKAGEEDYII RSHSNYSMRR SVAAELDLDE
TGEYLVLVKI SAKRDFTALP AHTVIRDNCK DRRDKLLRIG LAYDLAHAKG HVVESEEDKK
SREKAEARVK AKERKEVKDK LTEKKKKKKR SEAKTAKRER ARQNKAKARA EAREKKEADK
KKLDGETKKP EEETVAGTGA EKLEFEKAES DNADTDMADT EKTDTEKTGS ENAESEKPSE
EKSETKTADG QDEPPPEGSD PPHSQTPASS STRQAVTEAA LNQLVAATGD SSRSARSSRK
NADRGVSPFN TAGSASREKL SRREVPIYDS DDSDTDSCVS SVSDSTIDAE IEKAKLPTPA
VIKEEKKDKK AADDESEDEF EKDPWNAIAV VGLKVYAKAK EVEKEEEVKV GNLGCSGQAR
TDSDEKENVK TAVKSADTPR GQDDKAEEHA ESSTNDIEAD SGEKKGKSET TEMVTESKAQ
NGDGKTAAKD KEEDSQELEV CIRVIRPRTW EDGETSLDVD DSAMDATKNV VEEDDKKNSK
KKIIIGMKGS LGAVDN
//