ID A0A2C9JDH0_BIOGL Unreviewed; 936 AA.
AC A0A2C9JDH0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=106057304 {ECO:0000313|EnsemblMetazoa:BGLB001014-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB001014-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB001014-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB001014-PB};
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 RefSeq; XP_013069901.1; XM_013214447.1.
DR AlphaFoldDB; A0A2C9JDH0; -.
DR STRING; 6526.A0A2C9JDH0; -.
DR EnsemblMetazoa; BGLB001014-RB; BGLB001014-PB; BGLB001014.
DR GeneID; 106057304; -.
DR KEGG; bgt:106057304; -.
DR VEuPathDB; VectorBase:BGLB001014; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000076420; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 2.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF382; CALPAIN-15; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00547; ZnF_RBZ; 4.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 3.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 50..79
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 218..247
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 347..663
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 112..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 584
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 604
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 936 AA; 105031 MW; 65B972B1876D7B40 CRC64;
MFIQASTRVY EHKIKMSRPT AIATGEEKTN TLSTDEIYGR IAGQAIIATS AAEWSCKRCT
LINQPTVSSC SVCRAPRHSR LPTLSDVDTC VENSSVIGTT DKQIIDLTLS DDNKNATSES
DKIELPSKSL NTKPKGSTSS DDSAHLINVD EEWKCKHCTF NCNPDWEKSC QICKKPKTSP
PNSQRSSISP PSPIAIVNGN VSYTHRPNDQ SPIQHPPSQS TWNCSKCTFT NTAEKSVCSM
CLNPRSLSDL TAWTCDYCTV INNPVHNNCT VCCMPRHLGY KSQVANVSPS SPSNNHLKQA
SSPADRAPFE LLRQESSLVE DIRIVEEKEA SELRQKIIQH CKSTGDTFVD DSFPLAPKSL
FLDQKKQYFV QETQSPNTKL SVSNIQWLRP QNIVVPDGLR IPWVVYRTPM PEDISQGILG
NCWFFSALAV LAERCHLVEH IVISKEMCKE GVYQVRLCKD GLWKTILIDD YLPCNSKNLI
FAQARRRQLW VPFIEKAMAK LYGSYEALVA GKCIEGLATL TGAPCESIPL QAEGTRGEEI
CADLIWAKLM SCRDLNFLMG ASCGGGNMNA KEEDFAQVGL RSKHSYSILD IQDLEGNKLV
RLRNPWGRYS WKGAWSDGSP KWKDISEASR NKLLSFGEEH GVFWMEFSDL MRYFDSIDVC
KIRPGWEERR IQGAFPINGT SPLKLIKLSI FHTTEVELGL FQESSRGTNG NKFLLDLCIE
VLKETQNAQL VSVGKLVVHS SRQLRGFVGC HHMFSPGEYI LVPLAFNQWR KVPDLSKVSH
PSYVLTVHSS KKLMVTENIC DRPNLLCDAL IQLAVTKGSR EELRPGVTAY SLMKGWAGCI
FVVENCLESK FIHLTTDCTN SMNIVSTRET LTTMDIIPPF HRQVILILSH LERTLPYHLS
RKLIHRPISS HERPQRLNDL ELSPESASLH IARPYV
//
