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Database: UniProt
Entry: A0A0D2FX42_9EURO
LinkDB: A0A0D2FX42_9EURO
Original site: A0A0D2FX42_9EURO 
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
//
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