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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//