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Database: UniProt
Entry: A0A3R7MIX0_PENVA
LinkDB: A0A3R7MIX0_PENVA
Original site: A0A3R7MIX0_PENVA 
ID   A0A3R7MIX0_PENVA        Unreviewed;       641 AA.
AC   A0A3R7MIX0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROT82910.1};
GN   ORFNames=C7M84_023895 {ECO:0000313|EMBL:ROT82910.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT82910.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT82910.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT82910.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT82910.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT82910.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) 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:ROT82910.1}.
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DR   EMBL; QCYY01000759; ROT82910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7MIX0; -.
DR   STRING; 6689.A0A3R7MIX0; -.
DR   EnsemblMetazoa; XM_027350971.1; XP_027206772.1; LOC113800237.
DR   Proteomes; UP000283509; 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:InterPro.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
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; PTHR47901; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 18; 1.
DR   PANTHER; PTHR47901:SF8; CASPASE-3; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509}.
FT   DOMAIN          423..540
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          558..631
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
FT   REGION          114..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  73984 MW;  31E13B66CE80986E CRC64;
     MTSRTSDKQQ VLQDGTFSLQ PNGKYLCVCG TQLLKASIKR HLASIKHLEK VSGQVVRGSS
     RTGKDSNTRH LENTRNMAHS VINSKNEVAQ ALQPNGKYLC VCGTQLLKAS IKRHLASDKH
     KRMTAPHMRS RTGREQSTGS EGRLTSNEEK GAVRKSQKQA NFRLGFAPRT NGTTATVREG
     ERRRREHQKY DDNKPSLERK TRESTEESDS DSTDDSEEEE SLGEEEEEES LGEEEEEEEE
     SLGEEEEEEE SLGEEEEEEE SLGEEEEEES LGEEEEEENQ EEKEEERGQK YENNEQNQEE
     EEQSQEEEEE NQEEKEEEQS QEEKEEERGQ EYEKNEQSQE ESEEEFHLQQ PWTEHSKREE
     GELSEEELNL TQLYEQEDTE EEEAFGLRQL YDSELSKGES QSKEEDNTST ESYRMASHPR
     GNVYVFNYKF TGKHNQRDGA DYDSESIQKT FTDMGYRVFV KEDLSRRATL MELKLIRDGE
     SIRNVDSLVM FFLSHGKGVR DFLTEDGQSL CLSRIHRMFT DGQCPALRGK PKIFFANFCR
     RGAFETCPAF EVSDSPRDMV TVHAAGEGSG ALRNASFGTY FIRNLCQVLQ EHAGGKSLRE
     IYLELDRSAA ERGGTQPMWE DYVFRNFYFS PTKRRDEEIE I
//
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