ID A0A2J7R3A3_9NEOP Unreviewed; 368 AA.
AC A0A2J7R3A3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Caspase family p20 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B7P43_G04803 {ECO:0000313|EMBL:PNF35300.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF35300.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF35300.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF35300.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNF35300.1}.
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DR EMBL; NEVH01007822; PNF35300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7R3A3; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR22576:SF41; CASPASE 23-RELATED; 1.
DR PANTHER; PTHR22576; MUCOSA ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1/PARACASPASE; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000235965};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 1..71
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 95..182
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 342..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41591 MW; DE4C149E3B10B395 CRC64;
MSMLTVSKDD HKNEDCIVVA VLTHGKGKGK LYAYDDFYRA DTLWSSFTGD VCPSLGGKPK
LFIVQACRGE EASEGMSFKS SIQIDSHNMN TEASHRYSIP VEADLLVAFS TYEGRAALRH
VEGGTWFIQE LCKELEDNGE TLDLLSLFTN VNRRVAVHKE YKKLKQMPVI QSTLTRKVFF
GSMTARSRIT ITSDVFSLQG RTLEKLDVVI GMLENTIVSI PVPRTGTAKK LSSSLNWDSL
QSSKQTVVGP LPEMQDVYRI AEALKVFLED EADKLKPVVK EGGEFILNFI SCWDNLTKEL
RCYGYKKLVV FLNENARNWR VYKLLHIPDI CSLNTENSHR RWSQSDVTDS DSTSSRRSTI
PRRIAPKK
//
