ID G0U9Y4_TRYVY Unreviewed; 888 AA.
AC G0U9Y4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative calpain {ECO:0000313|EMBL:CCC52615.1};
DE Flags: Fragment;
GN ORFNames=TVY486_1101000 {ECO:0000313|EMBL:CCC52615.1};
OS Trypanosoma vivax (strain Y486).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCC52615.1};
RN [1] {ECO:0000313|EMBL:CCC52615.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y486 {ECO:0000313|EMBL:CCC52615.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR EMBL; HE573027; CCC52615.1; -; Genomic_DNA.
DR AlphaFoldDB; G0U9Y4; -.
DR VEuPathDB; TriTrypDB:TvY486_1101000; -.
DR OrthoDB; 151434at2759; -.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF427; PUTATIVE-RELATED; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 3: Inferred from homology;
FT DOMAIN 273..547
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 844..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCC52615.1"
SQ SEQUENCE 888 AA; 99887 MW; 7184B64139540184 CRC64;
DVPVDLLMLK NDSTLVSFAR ELRSLRDASS LPNSGAVEQV TKNITDRVEH LILQYKAVER
EFLKSAVGVS LSDVPLDDDP IFCELEKQLR KFMCNPDANA EVIEDQKYAM TLRAVELADG
VLCQDRSFLN NAPLGLPLSE LTLDDPLFHE MELKRRRLKE LDPVRYASKI KELEQKLNDH
VNDLAFHALS EQRSFLDPNP CGIPLSELPL DVDDTMRSLE CEYRKILRES PRNLKLLRDI
RAKISEHVRK LALDVLNCQD VEFHKANQHA AEKWPRIGEL YPEGAREPVV PEVTSPSDVS
SAPRELGYLA PFIAALSRHP QLIHRLIDSK AHPVNAPYSF IFFDPHSNPV RVDIDDRVPV
NANFEPKFTR VPRRSWYPLL LEKAYAKFVG GYDKLDHCTP HETLRDLTGR PVTHIPFEEK
RADGIKMGDF RSTKFWREVR ANLDQGDVMT CISNPDCVDG IHPQCSYAVL GVVETVSESN
DPSDVVIKLH NCYPDEPVYS GPLRRNDRRW TEELKRVCRY HPDEDVLYLP LPVFLRNFSS
MQRCHVNCGD RLTSVGEWNE VTGGGNPRYT SFRNNPIYLV ENKSSRPVTI LAELRHHAPV
FFDADGAKHF HQSGLALLQQ HQHVGPLSWL LTNSTHRFLQ KGIMLDTREV CSQMELPPKS
MCYLVPYAMK RGGCGEFSLS VYPGAANVSL TPLRPLLTKH MVLNADVILK PGSRDSKCVD
FVIGNACDVH VLLCQSKVTE PLSVKRGNVI AEDSVTMSLF DENKTRLAST GDPTSAREHS
ISVNLPVAGR YRITMCCPNR GSTGDCPCVV SLYVPRTSGA KIVSIPSNGM QALLPALQRS
PMREGSWTLP TERGNKATSS RSAPKIEPRA TQGAAFQLPR IGLRSQRK
//
