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Database: UniProt
Entry: E9GL65_DAPPU
LinkDB: E9GL65_DAPPU
Original site: E9GL65_DAPPU 
ID   E9GL65_DAPPU            Unreviewed;       803 AA.
AC   E9GL65;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN   ORFNames=DAPPUDRAFT_304374 {ECO:0000313|EMBL:EFX79800.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX79800.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX79800.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   EMBL; GL732550; EFX79800.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9GL65; -.
DR   STRING; 6669.E9GL65; -.
DR   MEROPS; C02.029; -.
DR   EnsemblMetazoa; EFX79800; EFX79800; DAPPUDRAFT_304374.
DR   KEGG; dpx:DAPPUDRAFT_304374; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   HOGENOM; CLU_006770_2_0_1; -.
DR   InParanoid; E9GL65; -.
DR   OMA; GDYRRGC; -.
DR   PhylomeDB; E9GL65; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 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; 2.
DR   Pfam; PF00648; Peptidase_C2; 1.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT   DOMAIN          223..529
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        447
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        467
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   803 AA;  90033 MW;  BD8C8A4ED5AFDB94 CRC64;
     MTSSGTTLQQ AIELGKRAVL LDQEGKHEGA AYFYEQAAIA LEEIVATNSI VQSATLAVKA
     NQYKQRATSL RNSYLSSNVM PSLTEEQQSI LNNARNSVNK ALEVDEMGEH KKALPLYIDA
     VEVCSSAAKA TSDKNLQSKL TKLAMQALNR AEELKMKPQT NKKTSASPAA SESAQVEHLS
     VSNLKVSGAQ SYSSEEKKVL EITSMINGRE YVPFMAGDLQ ERFILLSTFS DRHGKLSLSP
     KQKKSFSRWA RAEEISADPK VIENIDCFSI KQTVVSDCSF VASLAVSAQY EKRFNKKLIT
     NIIYPQNKSG MPVYNSCGKY MIRLRINGVS RKVVIDDYLP MGRHGELLCS YSVNRNELWV
     SLLEKAYMKV MGGYDFPGSN SNIDLHALTG WIPERVALKS SGGEEFKKEE LFKKLYDRFH
     KGDVIVTVAT GEMSEAAEVR TGLVSAHAYA LLNIQEVKGI RLIMLKNPWS HVRWKGNYSE
     LDANHWTEDL KKQLNYNPES AANFDNGVFW IDYDSLCTFF DVVYLSWNPS LFTHTFSIIG
     CWNAGSGPVK DLYNIGENPQ FSLTVRSPGS AAVWILLTRH ITDIDDFREN KEYITVLVYK
     NKGKRVYYPA DPPPYIDGIR INSPHYLCKL LHTQAGIERY TLVISQYEKS NTINYSLRVY
     SSCPIELKKI TNPHRFKDEI RKDGWKGVSA GGCGNNPRTY PNNPKYQFTL EKTSDLLIDL
     KGPKEFLIGF DVTCISLCDN DSSSGTFTKK SSGAFRSGFV ILELENVPAG IYQIVPSTFH
     PGQEGSFFLT IQSPNQIKLK KIQ
//
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