ID   J7M4U1_THEOR            Unreviewed;       879 AA.
AC   J7M4U1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Peptidase C1A papain C-terminal domain-containing protein {ECO:0000259|SMART:SM00645};
GN   ORFNames=TOT_040000993 {ECO:0000313|EMBL:BAM42525.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM42525.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM42525.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM42525.1,
RC   ECO:0000313|Proteomes:UP000003786};
RX   PubMed=22951932;
RA   Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA   Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA   Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA   Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA   Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT   "Comparative genome analysis of three eukaryotic parasites with differing
RT   abilities to transform leukocytes reveals key mediators of Theileria-
RT   induced leukocyte transformation.";
RL   MBio 3:e00204-e00212(2012).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; AP011949; BAM42525.1; -; Genomic_DNA.
DR   RefSeq; XP_009692826.1; XM_009694531.1.
DR   AlphaFoldDB; J7M4U1; -.
DR   STRING; 869250.J7M4U1; -.
DR   EnsemblProtists; BAM42525; BAM42525; TOT_040000993.
DR   GeneID; 20717013; -.
DR   KEGG; tot:TOT_040000993; -.
DR   VEuPathDB; PiroplasmaDB:TOT_040000993; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   OrthoDB; 5472948at2759; -.
DR   Proteomes; UP000003786; Chromosome 4.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411:SF741; CATHEPSIN K; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..879
FT                   /note="Peptidase C1A papain C-terminal domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003794755"
FT   DOMAIN          669..878
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
FT   REGION          165..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          501..528
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        181..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..225
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   879 AA;  100212 MW;  5A19927E6CC8D111 CRC64;
     MAEMKRPLIV LLLLCYGYKI VKSEENSSVD CTLFKVRTED TSEDCGYKDN DTSKYSYELK
     GLFKNQPLYT LNSGVKLVAL LYNDEFVWKH TSAHDLSKYP TELEIDPYNK TLWVKYGEMD
     FVTFKFENNK WKHSQDLSYG LCKSLTIPDY TDALAPVTLL PTPVEEKAEE KVEEGQFEDF
     EDREEKPAEE AKEGAVEEEK PEESPEDKVE LEVEETEELV EAGEGAQEAV EEKGVEEVAG
     PEPGEAAEEH DLPQLHAEET DERSVVGSEE VHEDEVAVDC TLFKVRTEDT SEDCGYKDND
     TSKYSYELKG LFKNQPLYTL NSGVKLVALL YNDEFVWKHT SAHDLSKYPT ELEIDPYNKT
     LWVKYGEMDF VTFKFENNKW KHSQDLSYGL CKSLTIPDYS VSPLISVIVK PREKEAEKAA
     PMVPEAPDAT PLAEGDAVIA SETVESEYAV PLAVPEAKPE DEAAPEERTD KLEPLDERYK
     MRGTMAEGEL GDEVKFDFVL DKEERREREE LKSKSEQLFE QMKEYAHNKG MAVVEGDFDK
     YITGQLKTPQ DNFVHEWKLK AVAEVLAKAE TPLEAELEFA VIQNFYVFAK KHSRVLFTLT
     QFKDSYANFR ESAKTIESHN KNPNRLYNMD YNTFADMGRD LSLMSIPTTF NVKQYVSGFQ
     THAQTLDNQE IHVDWRDQGL VSHVITQGKC AICWAIPSVD VFNSFAAKRT GDKIPYSIQQ
     VLDCVSPEYT CDSGGSFVKV LEYIKDNKMC TYEEYPYVQK KEGCQAQKCL NESKIKTVRK
     LKLNDALDFL KNNGPFVTMV NTTLEFFLYS GGIYDGPLGG YGGHSFLVVG HGYDRDKGVN
     YWIAKNSWGE SWGENGYFRM LDDSDTLTYL FLANAYGIE
//