ID   A0A074ZUH1_9TREM        Unreviewed;       942 AA.
AC   A0A074ZUH1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN   ORFNames=T265_13892 {ECO:0000313|EMBL:KER27035.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER27035.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER27035.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) 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; KL596733; KER27035.1; -; Genomic_DNA.
DR   RefSeq; XP_009169258.1; XM_009170994.1.
DR   AlphaFoldDB; A0A074ZUH1; -.
DR   STRING; 6198.A0A074ZUH1; -.
DR   GeneID; 20328059; -.
DR   KEGG; ovi:T265_13892; -.
DR   CTD; 20328059; -.
DR   OrthoDB; 230045at2759; -.
DR   Proteomes; UP000054324; 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; 2.60.120.380; -; 2.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 2.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR46143; CALPAIN-7; 1.
DR   PANTHER; PTHR46143:SF1; CALPAIN-7; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00648; Peptidase_C2; 2.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SMART; SM00745; MIT; 2.
DR   SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 3.
DR   SUPFAM; SSF116846; MIT domain; 2.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT   DOMAIN          249..621
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
FT   ACT_SITE        539
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        559
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   942 AA;  106867 MW;  A6C5C42EE002F309 CRC64;
     MVDPAALEAD AKNFADVAAT YEASKQYEAA VFFYTEAAQA LINAQTAGSS TPNIRDTAHR
     YIKRAEDLKA RSSTRDIDVG VEGRRPSVLQ NSLSRAKFIF HDAITEDEKG NVDEAVELYG
     AAVELLLSLR AQSPNESTMK EIKKLANEAL SRAEILKDRG KSKLTTAQVT AGASKSRRKV
     SCVEQPETGG YSAEELKVLK ATSTINGREY PPFLDFIDLR MRFAFPKPYT DKHGMLALSE
     KQKRQLDRWV RPSDYLENPK MIMAISCFSI RQTVVTDCSF VASMAIAAQY ERRFKKRLIT
     NIIYPQSRDG EAVYNPCGMY MVRFHINGVP RKVVIDDYLP MARNGELLCS FSTNRSELWV
     SLLEKAYMKV MGGYDFPGSN SGIDLHALTG WIPERISIRS NSMSFNKDRE FRRLLSRFHR
     GHCLCTVATG EMTEDVATRA GLVPSHAYAM LDIREIDLEC GGEKGLCKTL KMECDFERTG
     SASIHPGPAE TASNSMSFNK DREFRRLLSR FHRGHCLCTV ATGEMTEDVA TRAGLVPSHA
     YAMLDIREID DKRLLLLKNP WSHLRWKGNF SEHDSRNWTP QLQAKLNYDL SSAQAVDNGV
     FWIDYDSVCH YFDVFYVNWN PELFQHTTCV HEQFGDLHSC AVDNGVFWID YDSVCHYFDV
     FYVNWNPELF QHTTCVHDMW LAHDGPKKDS YSCANNPQYN LEVQATVEAP VWALLTRHIT
     DKEDFADNKE FIALVVYKDI KTRKVYCPYE VEPFRDSVRA NSPHCLVQFL QDPGTANYTF
     VVSQFEKNNT IRYTLRVYST APFVLSKITD PYKVEKQVTG QWKGANAGGC QNHPDTYDRN
     PCYQINLSNN EVDNQLLVEM RGPKDYAIGC ELIKVSATNP AAPNQMERKS SGSYRRGYVA
     LEQAGLSGGI YNLVVSTYYP NQEGPYILNF KSLRPFTLNC IR
//