CYSP_THEPA
ID CYSP_THEPA Reviewed; 440 AA.
AC P22497; Q4MZ80;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cysteine proteinase;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN OrderedLocusNames=TP03_0285;
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2120221; DOI=10.1016/s0021-9258(17)44709-0;
RA Nene V., Gobright E., Musoke A.J., Lonsdale-Eccles J.D.;
RT "A single exon codes for the enzyme domain of a protozoan cysteine
RT protease.";
RL J. Biol. Chem. 265:18047-18050(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga;
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-440.
RC STRAIN=Muguga;
RX PubMed=1565135; DOI=10.1016/0166-6851(92)90196-q;
RA Nene V., Iams K.P., Gobright E., Musoke A.J.;
RT "Characterisation of the gene encoding a candidate vaccine antigen of
RT Theileria parva sporozoites.";
RL Mol. Biochem. Parasitol. 51:17-27(1992).
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; M37791; AAA30131.1; -; Genomic_DNA.
DR EMBL; AAGK01000005; EAN31020.1; -; Genomic_DNA.
DR EMBL; M67476; AAA98600.1; -; Genomic_DNA.
DR PIR; A36083; KHQBTT.
DR RefSeq; XP_763303.1; XM_758210.1.
DR AlphaFoldDB; P22497; -.
DR SMR; P22497; -.
DR STRING; 5875.XP_763303.1; -.
DR MEROPS; C01.079; -.
DR EnsemblProtists; EAN31020; EAN31020; TP03_0285.
DR GeneID; 3500253; -.
DR KEGG; tpv:TP03_0285; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_03g00285; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; P22497; -.
DR OMA; WETYKLE; -.
DR Proteomes; UP000001949; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..60
FT /evidence="ECO:0000255"
FT PROPEP 61..229
FT /note="Activation peptide"
FT /id="PRO_0000026390"
FT CHAIN 230..440
FT /note="Cysteine proteinase"
FT /id="PRO_0000026391"
FT REGION 166..182
FT /note="Involved in processing to yield active enzymes"
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /evidence="ECO:0000250"
FT ACT_SITE 382
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 250..291
FT /evidence="ECO:0000250"
FT CONFLICT 2..3
FT /note="YS -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50331 MW; 0EA1C43805649645 CRC64;
MYSSSVVSNP NERLVNNRVE NDLESSDDTL STQAKPVSRL LTRKLLLGVV VLFFLAGVSV
VSYFLFSKYK MLNKFKRELD DHLTKDFPNL ERSKRDTCFD ELTRLFGDGF LSDDPKLEYE
VYREFEEFNS KYNRRHATQQ ERLNRLVTFR SNYLEVKEQK GDEPYVKGIN RFSDLTEREF
YKLFPVMKPP KATYSNGYYL LSHMANKTYL KNLKKALNTD EDVDLAKLTG ENLDWRRSSS
VTSVKDQSNC GGCWAFSTVG SVEGYYMSHF DKSYELSVQE LLDCDSFSNG CQGGLLESAY
EYVRKYGLVS AKDLPFVDKA RRCSVPKAKK VSVPSYHVFK GKEVMTRSLT SSPCSVYLSV
SPELAKYKSG VFTGECGKSL NHAVVLVGEG YDEVTKKRYW VVQNSWGTDW GENGYMRLER
TNMGTDKCGV LDTSMSAFEL
