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Database: UniProt
Entry: C9ZZG8_TRYB9
LinkDB: C9ZZG8_TRYB9
Original site: C9ZZG8_TRYB9 
ID   C9ZZG8_TRYB9            Unreviewed;       492 AA.
AC   C9ZZG8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Metacaspase 5, putative {ECO:0000313|EMBL:CBH14817.1};
GN   ORFNames=TbgDal_IX8930 {ECO:0000313|EMBL:CBH14817.1};
OS   Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH14817.1, ECO:0000313|Proteomes:UP000002316};
RN   [1] {ECO:0000313|Proteomes:UP000002316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX   PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA   Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA   Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA   Barry J.D., Berriman M., Hertz-Fowler C.;
RT   "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT   chronic human african trypanosomiasis.";
RL   PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC   -!- SIMILARITY: Belongs to the peptidase C14B family.
CC       {ECO:0000256|ARBA:ARBA00009005}.
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DR   EMBL; FN554972; CBH14817.1; -; Genomic_DNA.
DR   RefSeq; XP_011777083.1; XM_011778781.1.
DR   AlphaFoldDB; C9ZZG8; -.
DR   MEROPS; C14.043; -.
DR   GeneID; 23860956; -.
DR   KEGG; tbg:TbgDal_IX8930; -.
DR   VEuPathDB; TriTrypDB:Tbg972.9.8930; -.
DR   OrthoDB; 1077459at2759; -.
DR   Proteomes; UP000002316; Chromosome 9.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.12660; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   PANTHER; PTHR48104:SF30; METACASPASE-1; 1.
DR   PANTHER; PTHR48104; METACASPASE-4; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..492
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003005529"
FT   DOMAIN          62..317
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          358..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..471
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  54467 MW;  5B13D4020252DE72 CRC64;
     MDAALALLFG QVATAVLPYV VNSIGRVPRP KRVDVKKAMG EAHQCRPVVP YRAPRPYTEG
     RVKALFIGIN YTGSSAQLGG CVNDVMHMLQ TLQRIEFPIS ECCILVDDRR FPNFTAMPTR
     ENIIKYMAWL VYDVRPGDVL FFHFSGHGAE TKGGRDSNEK MDQCLVPLDY DKAGAILDDD
     LFELMIKGLP AGVRMTAVFD CCHSASLLDL PFAFVAGRNV SSNQRHEMRM VRKDNYSRGD
     VVMFSGCEDS GTSADVTNTS SFGNGTVAAG GAATQAFTWA LLNTTGYSYI DIFMKTREVL
     RQKGYKQVPQ LSSSKPVDLY KQFSLFGPLT MNASLVQHLP QEYVQPWAPH PAYQQPHEAT
     LPASVSQPHS QPVMGIPVAS TSNGKSNPGV SDGGRASGEV YPPTQYPSSH PAPQQQAYYQ
     PPQQAYYQPP QQAYYQPPQQ AYYQPPQQAY YQPEPHHQPA PPPPPKKENK PARPGYPMSY
     CMKFSQGKPG RK
//
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