ID A0A182P1T4_9DIPT Unreviewed; 726 AA.
AC A0A182P1T4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI000868-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI000868-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI000868-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR AlphaFoldDB; A0A182P1T4; -.
DR STRING; 199890.A0A182P1T4; -.
DR EnsemblMetazoa; AEPI000868-RA; AEPI000868-PA; AEPI000868.
DR VEuPathDB; VectorBase:AEPI000868; -.
DR OrthoDB; 230045at2759; -.
DR Proteomes; UP000075885; 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; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
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; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
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 157..453
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 391
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 726 AA; 82277 MW; 0E659F0D1DE3B01C CRC64;
MSSEGEIRSL LGRALDADEA GKKEEAIELY GRAVEQILRL EDKERREKLN KFAKQALDRA
EELKGIRYQA GQQSAPQASR HPPTVLQPVR SSTAPASPSR PAGPVLEISG SRHAYTSEEK
KVLEHTSHVN AKVYVPFMDI DLLEKFHFPM PFTDRDGYLE LAPKQKRDFV SWVRVSELSE
HPQLIVGDHP DFYSIRQTVV SDCSFVASLA VASQFEKKFK RRILTSIIYP RNSKDEPIYN
PSGKYSIRMH VNGVPRKVVI DDYLPLGRYN QLLCSYSSNK NEFWVSLLEK AYMKLMGGYD
FPGSNSNIDL HALTGWIPER ALVKSTEPDF NADAVFNRLQ EGLSLGRCLV TVATGELTDA
EAERTGLVST HAYAVLDMRE VDGVKLLQLK NPWSHLRWRG NYSELDAVHW TPELQRTLGY
DPKMAATYDN GVFWIDFRSI MNFFDVFYLN WDPALFQYTY CIHQSWSAGV GPTKDAYNVG
DNPQFSLTVP AGRGSVWILL TRHITSIEDF RENHEYITVL VYNSNGKRVY YPTDPPPYID
GVRINSPHCL CKIRLDPAAK RRYTLVVSQY EKTATIYYTL RAYSRTKFEL EQLGPRYTTV
ENLSGEWKGR TAGGCLNHPA TYKNNPLYRL HIGPADTSDL VIELRGPKVY QVGLELTVVS
LADDTVTAPF VSQKTGVYRS GFCVLDLEGI PAGVYQVRPS TFLPDQESPF FLKVKSTTNV
VIEKLN
//
