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Database: UniProt
Entry: A0A068YCI9_ECHMU
LinkDB: A0A068YCI9_ECHMU
Original site: A0A068YCI9_ECHMU 
ID   A0A068YCI9_ECHMU        Unreviewed;       793 AA.
AC   A0A068YCI9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Calpain 7 C02 family {ECO:0000313|EMBL:CDS42303.1};
GN   ORFNames=EmuJ_001000650 {ECO:0000313|EMBL:CDS42303.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42303.1};
RN   [1] {ECO:0000313|EMBL:CDS42303.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CDS42303.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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; LN902842; CDS42303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YCI9; -.
DR   STRING; 6211.A0A068YCI9; -.
DR   MEROPS; C02.029; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   OMA; GDYRRGC; -.
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; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 2.
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; 2.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
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; 1.
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   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT   DOMAIN          233..519
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          152..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   793 AA;  90612 MW;  9697E88EAC33CB73 CRC64;
     MADPTSLEAD ADDFIKRAQH FENAKDFDLA VFYYAEAVQA WLNARNAGST NPDILTLARS
     YTKRAEELVE KRDAAGSAVK VPQQNVEVER AKCLLNEALE ADEQDNTVDA LNLYSQAIEV
     LLKVRNETND REFREKVERL ARQALERAEA LKSAVKSPPL SKASCTRTSS HRSRSGEGGN
     YTRNELRVLR KTSTINGREY LPFLDVIDSH ERFAFAQPFM DQHGLIALSS KQRSSFVKWV
     RPSDFLNNPT MIITVSCFPI RQTCVTDCSF VASMAVAAQY ERRFKKRLIT NIIYPQKKNG
     EPVYNPCGKY MVKLHLNGVP RKIIIDDRLP MGYHDELLCS FSTNKNELWV SLLEKAYMKV
     MGGYDFPGSN SNIDLHALTG WIPERISIKS SGTNEFDADR EFRRLEKRFH RGHCLVTVAT
     GLLTPEVEQR SGLVPTHAYA LLDMRQVDQT RLLLLKNPWS RTRWKGNFSD LDTEHWTPEM
     QRKLDYDLNS ARYVDNGVFW IDYKSLLYFF DVFYINWNPE LFPYTTCVHS EWSASEGPRK
     DVYSFANNPQ YTLEVQAKSQ APVWVLLTRH ITNKNDFAHN NEFIGLVVYK DIQSRKVYHP
     NDPVPLKDSV RINSPHCLIQ LVQEPGNVTY TLVVSQYEKN VTIQYTLRAY STAPMRFSPI
     IDPYTVTKTM NGEWKGETAA GCQNYANFHN NPTFELVWPN NEADNQVLVE VRGPRDFAIG
     FTWDVVSLTN SSPLNTARSL STGNYRRGYT MLEVAGLSGG RYKVTVATFE PLQEGPFILS
     VKSTRPLTLS RLQ
//
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