ID A0A0D2FX42_9EURO Unreviewed; 811 AA.
AC A0A0D2FX42;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=PV04_03237 {ECO:0000313|EMBL:KIW71015.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW71015.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW71015.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW71015.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; KN846957; KIW71015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2FX42; -.
DR STRING; 5601.A0A0D2FX42; -.
DR HOGENOM; CLU_006072_3_1_1; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000054266; 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:UP000054266};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 214..515
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 439
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 459
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 811 AA; 91672 MW; 71EC480BBD840623 CRC64;
MTSRPLFVRD GHPDRPPRVI YQDDDRDESA SIDFEMKSQR RGSANGRQEN NDIDITAHPT
GNDPAVPKDG LVLGGGQTIK LMLVPDKPPA PPPPPAKEKK PHPQAKMKKF WKNFDPEYTG
KVTRVLPDRI TEKDLSAVTL VGEIAHKAIK SYEDAKESCI RDVKRIVKEC RAANQKYTDS
HWDIERDLKI TRIRDCLDGL VIDDDDKEHP ADAKRVTDIF DEPKFYVNGA SYDDILQGSA
GDCWFLAAIS ALGCNQEFID RVCVIQDEAV GVYGFVFHRD GEWHQCIIDD KLYLRAPAYD
ESGDVVLTQY GIRRPDQEDQ YQELFQRGSK SLYFAQCRDQ NETWVSLLEK AYAKAHGDYA
SISGGQTGEA IEDLTGGVTT EIYTTNILDT EAFWKNELSR IGKDFVFSCA AARWREWRPY
LVANEKVREE RRSGIVSQHA YAVLDVYEGH GQRLVKIRNP WGRKEWTGAW SDGSKEWTAE
WLIRLNHQFG DDGIFWMTYK DMLSKYKYID RTRIFGPDWH VAQQWMSVQV PWSTLDYQTN
HFSIDVPDDT DAVIVLSQLD DRYFKGLQGK YNFTMQFRVQ KDDDDDEEYL SRSKLNYELV
RSVNVELHLT KGTYTVLVKV EAHATSRGEV EDVIRKNIHR RDKITQIGKL YDLAHQKGQL
PVGSSAAASG TSSASASGTS TPVPSGVCTP ASTSPSIPST SEPAKKDEDD NEKDPNRNPW
NASCVIGLRV YSKQPDLGLK VIVPSKDDVN EMPTLDRDDV AKSALDEVQA VADKVDDVVG
EKKEGEDEEE KGNDDDKDND KEAEEAKATS Q
//