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
//