ID J4C354_THEOR Unreviewed; 376 AA.
AC J4C354;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=DNA-damage inducible protein {ECO:0000313|EMBL:BAM39846.1};
GN ORFNames=TOT_020001023 {ECO:0000313|EMBL:BAM39846.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39846.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39846.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39846.1,
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 DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
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DR EMBL; AP011947; BAM39846.1; -; Genomic_DNA.
DR RefSeq; XP_009690147.1; XM_009691852.1.
DR AlphaFoldDB; J4C354; -.
DR STRING; 869250.J4C354; -.
DR EnsemblProtists; BAM39846; BAM39846; TOT_020001023.
DR GeneID; 20715114; -.
DR KEGG; tot:TOT_020001023; -.
DR VEuPathDB; PiroplasmaDB:TOT_020001023; -.
DR eggNOG; KOG0012; Eukaryota.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000003786; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05479; RP_DDI; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT DOMAIN 1..52
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 189..268
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
SQ SEQUENCE 376 AA; 42171 MW; BF832CAE5E0D9450 CRC64;
MNELIKDNLN IPVENQRLYL DGNMLKGNYK SISDSGIKSG DVLLVKSERP GFDISSLLAS
DYDKVPEEAL RQRAREIMQE FKPGSTFLNT LKLHNEPMYK ALQANNEEEV YRIVKKEYEE
VKKKELDHRK KLMKAYLDPL NPESQSLIHK EIEMNRINDN LISAQNYLPE SFGKINMLYV
KVEINNVVMK ALVDTGAQST IMSKECASRC NLLRLVDERF KSVAVGVGTM KTLGKIHLAD
MKIGTVFIPV SFIVIEEASL EFILGLDVLR RYTCDINLKK NYLGINDVNV PFMSEAEVGS
FVSHTARREN PAPAAPTTPT GYANTAISAN PDSLQSSAID DKARRLSETL NITPEYAREL
LEIAGGDEQL AASYVT
//
