ID U6H689_9EIME Unreviewed; 692 AA.
AC U6H689;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Calpain-1 catalytic subunit, related {ECO:0000313|EMBL:CDI87417.1};
GN ORFNames=EPH_0007240 {ECO:0000313|EMBL:CDI87417.1};
OS Eimeria praecox.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI87417.1};
RN [1] {ECO:0000313|EMBL:CDI87417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI87417.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI87417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI87417.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR EMBL; HG697395; CDI87417.1; -; Genomic_DNA.
DR AlphaFoldDB; U6H689; -.
DR EnsemblProtists; CDI87417; CDI87417; EPH_0007240.
DR VEuPathDB; ToxoDB:EPH_0007240; -.
DR OrthoDB; 213015at2759; -.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 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 PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 3: Inferred from homology;
FT DOMAIN 66..361
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 692 AA; 75153 MW; 6F37A8AFE59D6696 CRC64;
MEPQSTLPES SYPGSGNGDA REGATVQSPV LTREPQQQHH QLAQEHNSLP TCACKALLQS
SEEGGLLEDP EFPRPQSGDS TQPPENGGQP ADILKGLLWV RPDEIVQRIQ RQQSKAQRAS
RPPPQQQQQE QPAQQQQAEK TAVLFSNNRI ASTVAQGILP SHAFAAAASG LAASNPRVIK
EALVHPQEWR FSHCHAFEEV WLPLLEKAYA KFLGSYEAVA QRAFRDIAVD LTGGIVEERE
IQCFDAAVLW AKLRKAFNVG GCFLSCLARG ADVEKDNILP DRHYTIVDVV RVEELRLLRL
HNPWKVPTWR GEFSDYHRSW TQYPDLKDKL NYKFGDTPAA FWMKFETFLE VFTDICFCHS
LPPQHKAPLL LQPLRSPRLT LAEAAVFTGQ SYGRNDLTAS NWDIQEATRC IQTPSKCETG
LRPPAQGEVW SYAEGAEVYV TVQEETWKGL SLCGLPREWS RNPSAAAAVS RPAATPQQTP
RSTLMPGNVT SSDGNAFCTS RRTFSGASCN TWGLQQIETT AGAAFQIGSK NAGSSAAAHA
APAAAAAASG PGAGSATTAA ATPAAQQIRS STVRSCTYTA VSRPSAFVRY ERQAEGFDTA
WVNAPMFLVS VPPPPSAAGG AACAAGSPVS AADDDDPKDP EQQQQQKERQ QQQQQVDILL
AITQDCSLDV APISMAVFRT RVAAAPSTCE LQ
//
