ID   CYSP_THEAN              Reviewed;         441 AA.
AC   P25781; Q4UCF3;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Cysteine proteinase;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=TACP; ORFNames=TA03740;
OS   Theileria annulata.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1518523; DOI=10.1016/0166-6851(92)90100-x;
RA   Baylis H.A., Megson A., Mottram J.C., Hall R.;
RT   "Characterisation of a gene for a cysteine protease from Theileria
RT   annulata.";
RL   Mol. Biochem. Parasitol. 54:105-107(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara;
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA   Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA   Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA   McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA   Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA   Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA   Shiels B., Tait A., Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata compared
RT   with T. parva.";
RL   Science 309:131-133(2005).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; M86659; AAA30135.1; -; mRNA.
DR   EMBL; CR940352; CAI75498.1; -; Genomic_DNA.
DR   PIR; A45565; A45565.
DR   RefSeq; XP_954974.1; XM_949881.1.
DR   AlphaFoldDB; P25781; -.
DR   SMR; P25781; -.
DR   STRING; 5874.XP_954974.1; -.
DR   GeneID; 3864605; -.
DR   KEGG; tan:TA03740; -.
DR   VEuPathDB; PiroplasmaDB:TA03740; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   InParanoid; P25781; -.
DR   OMA; DNHWNLW; -.
DR   OrthoDB; 1275401at2759; -.
DR   Proteomes; UP000001950; Chromosome 3.
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; 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; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..227
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026388"
FT   CHAIN           228..441
FT                   /note="Cysteine proteinase"
FT                   /id="PRO_0000026389"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        249..290
FT                   /evidence="ECO:0000250"
FT   CONFLICT        242
FT                   /note="I -> T (in Ref. 1; AAA30135)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  49665 MW;  B7489C05844BE31E CRC64;
     MTVLDDHFPQ GDDETVVPTS SSIPILSQMR QIVIKKRLLI SFLLTFFILA LSSASILTYF
     FFRSKSITNF KSLAIEHIES HYPSMDPSKR AGFVEEIVKI RQTGKITSDA ESELDMLIEF
     DAFVEKYKKV HRSFDQRVQR FLTFRKNYHI VKTHKPTEPY SLDLNKFSDL SDEEFKALYP
     VITPPKTYTS LSKHLEFKKM SHKNPIYISK LKKAKGIEEI KDLSLITGEN LNWARTDAVS
     PIKDQGDHCG SCWAFSSIAS VESLYRLYKN KSYFLSEQEL VNCDKSSMGC AGGLPITALE
     YIHSKGVSFE SEVPYTGIVS PCKPSIKNKV FIDSISILKG NDVVNKSLVI SPTVVGIAVT
     KELKLYSGGI FTGKCGGELN HAVLLVGEGV DHETGMRYWI IKNSWGEDWG ENGFLRLQRT
     KKGLDKCGIL TFGLNPILYS S