ID   A6RA87_AJECN            Unreviewed;       934 AA.
AC   A6RA87;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN   ORFNames=HCAG_05875 {ECO:0000313|EMBL:EDN10072.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10072.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   EMBL; CH476661; EDN10072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6RA87; -.
DR   STRING; 339724.A6RA87; -.
DR   VEuPathDB; FungiDB:HCAG_05875; -.
DR   HOGENOM; CLU_006072_1_1_1; -.
DR   OMA; WGERKGI; -.
DR   OrthoDB; 142935at2759; -.
DR   Proteomes; UP000009297; 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; 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   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT   DOMAIN          134..449
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          590..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..805
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..879
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   934 AA;  106946 MW;  8052CD857D7EA728 CRC64;
     MDGESESSRI DSIVSAVPSA WKDDVPQKLV DTFWKSFNSK YPGRVLKALS YRPGKTASQP
     VSNIAHGEAA LDSYDRAKRE CEHAVDRIVK QCLRINQKYT DPHFDIERDL KSGQRNFLDG
     LQGVNSEMKP KGVKRVTDIF EKPEFYVNNA TASDVRQGND GDCWLMAAIC TLGNMPGLID
     RVCVARNEKV GVYGFVFYRG MLYPYRFSVW TYILFILHGE WRHTIIDDKL YLRAPDYEDA
     AWEREVWDDI GRADTELNYR KTWQTGSRAL YFAQCSDDNE TWLPLLEKAY AKAHGDYSSI
     EGGFVGEAVE DLTGGVTSEI MARDILDKER FWNEDLMNVN KKFVFGCATG LYGSWLYPQY
     YGSKERSGIH ECHAYSVMDA KEIMGRRLLR LRNPWGHKEW SGPWSDGSEQ WTPEWMNILQ
     HKFGNDGIFW ISYEDFLLKY EHIDRTRLFG DGWTVAQKWT SLHVPWALEY HKTKFVIKVA
     KEGPVVIVLS QLDERYFKGL EGQYKFHLQF RLEKEGEEDY VIRNQNNIYM TRSVSTDITL
     EPGTYTVFVR VKATQFSNPP PEDVIREKAS KQREKLVQIG HSYDLAHAKG VELESEEEEA
     ERKKREKEKK AALKKQERGR AEAQLRKGWK RDKKIAAREN RKAKRAARAT EQRAAKLQAK
     NDKELKEGGN KVGQVVEGDA ERTDGSNREG DEEATETPRA VNLENKNEGL TPRTGDANGK
     LEGKATENND KDMESSEVPN QGKEVRAEED NKMKGEDLKP STEDAKGKEV QKGEDPERED
     EGNIESHPDS ENANDKEKRE IEMSTTSKLT KGTENEKQRH GHPGMPEENT ESLPELSQKL
     ETDSDTDSGS VFEFDSEIDM SPTEESESDS EEHEKDDDDN NDGEYSVKPP WNAVCVVGLR
     VCSKDRDLTI SIVKPKPWQE HIEVRRDCDD PAVE
//