ID A0A1X0P3Q1_9TRYP Unreviewed; 411 AA.
AC A0A1X0P3Q1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=DNA-damage inducible protein DDI1-like protein {ECO:0000313|EMBL:ORC91189.1};
GN ORFNames=TM35_000061940 {ECO:0000313|EMBL:ORC91189.1};
OS Trypanosoma theileri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC91189.1, ECO:0000313|Proteomes:UP000192257};
RN [1] {ECO:0000313|EMBL:ORC91189.1, ECO:0000313|Proteomes:UP000192257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC91189.1};
RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA Matthews J., Matthews K., Carrington M.;
RT "An alternative strategy for trypanosome survival in the mammalian
RT bloodstream revealed through genome and transcriptome analysis of the
RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORC91189.1}.
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DR EMBL; NBCO01000006; ORC91189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0P3Q1; -.
DR STRING; 67003.A0A1X0P3Q1; -.
DR VEuPathDB; TriTrypDB:TM35_000061940; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000192257; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05479; RP_DDI; 1.
DR CDD; cd14348; UBA_p47; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_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 Pfam; PF14555; UBA_4; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF46934; UBA-like; 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 Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000192257}.
FT DOMAIN 1..71
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 189..228
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT REGION 74..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 45119 MW; 8793D5D3D0312996 CRC64;
MVKIQCIDEK GNICTVDVDV NSLVDDMKAV LEVELGIPMD EQELRTASGM MLCSNETFSA
QGIVSDTQLT VRRQPLQESQ QPPPKPQPPK PQQQPQPQRS QQHPQQEERL SLDEARARIE
QLFNARMAQG QGGWPMMNEN DPNLQQRIYD HIQARNVDEN LENALEHAPE LFIPVTMLYV
NCEINKHKVK AFIDSGAQKS IISARLAEEC GLTRLINTKW KSLLRGVGAK QAIGHIHMTV
VNLGGLFIPC SFCVLEDDNI DLIIGLDQLK RHRMIIDLKE FCLRIDDTAI PFLPDHEVPM
GKIPDEEELQ KLKGDANKSS ESSSYPSTGV TSAGTAQTPG VAATAGAPTR TTGGTTGVSS
HTSGSRQGGA INENAVANFM SLTGIDRERA ILLLEAAGWD VNIAMSLLLD D
//
