ID A0A067NU04_PLEOS Unreviewed; 1174 AA.
AC A0A067NU04;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=PLEOSDRAFT_1097388 {ECO:0000313|EMBL:KDQ27101.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ27101.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; KL198009; KDQ27101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067NU04; -.
DR STRING; 1137138.A0A067NU04; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1097388; -.
DR HOGENOM; CLU_273755_0_0_1; -.
DR InParanoid; A0A067NU04; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000027073; 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; IPR022684; Calpain_cysteine_protease.
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: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.
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:UP000027073};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 98..349
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 526..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1174 AA; 128851 MW; 2342BFE24F5BE59E CRC64;
MSLFFNIFGR SQPVGEDIPQ GKGTFQQQER QAGLLVTAEL DKALEECKAR VAAISKLCRA
KNQKYRDIEF DLENDRELCL YGLQTENPPE PYTPSDVQRV TQVFDKPQFF VDGADANDIV
QGALGDCWFL SALAMMATAK GLVEKFCVAR DEVVGVYGFV FFRDSYWVPV VIDDMLYTSI
PKFEELNRSE KHLYHNSRDN YNKLARKGNK TLYFAKSGTE GETWVPLLEK AYAKLHGDYA
SLSGGEASEA VEDLTGGEPD VKVSGLIGGH AYSVLRAVEC RGKRFVILRN PWGKSEWTGP
WSDGSKEWSA EWLEILPEID HVFGEDGQFV MEYSDFLDCW DQIDRTLLFD SSWLMSSQWL
RVVTQPLPSA WTYGDVSFTI SVPEPTTAVI VLSKLDDRYF EDLSGQYWWN FNFILFKTGE
SEILAESSHA RLWSRSVNVE LELEAGDYVL HVRVDRKYRR DNSFAYNMNS DQNKRKLSRV
ETERAKGQSI ATNINSKSQA LSLPKPLAEL AGKDLKTLSL EKKAQEKAEK AKKKDEKPPV
PAEGGDVAKE PVVEPQTSNE TKVEAKDNDM PAPTDDDKGV VKDEPKSEGD AEEQGGEKSK
TDEAESEPSE AEEPKTDHGA AEGGTTSIPP DGEKESTEKD KVEDTKDDKD HKNDEGDGSS
SSSSSSESGS DSSDESVNGD YQADDENAVF LGLRVYTKKS APAAVAGQGY SPKCIGVYSV
TSRYTLCYVA PPYIMMRLVL YQSYIPAEAA LTTVAVAGAI AFGYVQVKSQ PPSSTPANSA
GTKASSDSTK KGKKKKRSDA PKPADQLEDK SGAQSSATPA VAAFSEVIPG QFDAGLLEKR
QTTTEPLSSK TKKKASKKNK KGKAKTALDS SVPGIVSRTS DTRSIASSED SDANLGHSLS
RTPQPAAAPS SGASQSRQLS RPHKQSTTSI DTDGSWTRVE TRRGKRRHAP DNVNTSIPAG
DPSSSFTLSH SMVDPTTSDA GVTTSVTTGN SSPVAERAME EDEDEGEPFL ASIAREQPQE
NRRTLAEKLL PKPRKTGVDD MTETPDYPQI ARVIRVQPRP DEKPASGFSW GDYGDVHVDT
SGTAENDADG EDDGWGVVRR SRPKRAAGET ATVHQSVSQK APESLTKRQR QNASRREAEK
AAQAEAEADR LARLAKHKSE LERTRMKEQL AGRK
//
