ID A0A0V0XVF5_TRIPS Unreviewed; 385 AA.
AC A0A0V0XVF5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protein DDI1-like protein 2 {ECO:0000313|EMBL:KRX91991.1};
GN Name=DDI2 {ECO:0000313|EMBL:KRX91991.1};
GN ORFNames=T4E_9969 {ECO:0000313|EMBL:KRX91991.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX91991.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX91991.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX91991.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX91991.1}.
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DR EMBL; JYDU01000122; KRX91991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XVF5; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
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:UniProtKB-KW.
DR CDD; cd05479; RP_DDI; 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 PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00627; UBA; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50030; UBA; 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:UP000054815}.
FT DOMAIN 3..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 208..287
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 337..376
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
SQ SEQUENCE 385 AA; 43216 MW; 4D506B2EDE146FC2 CRC64;
MCIQITLVIN QQDIVNVRGK LNWTIKEFLR ETKGFVPRLD DSLYTITIMF NGELVSDFER
TIKDYGIKDA DVLAVNVEPI AQSLGGDSLT SSAAPFDPAI AVAWLSRMMN ENPQMLQRIR
TESPAIFQAL QSGNVEEFQR LMQSFGLPNF IPSSANDLMN AETQRRIEDS IMQQNIDHTL
QHAIEHVPES FARVVMLFIK CKVNGQEVKA FVDSGAESSV MSVKFAEKCN ILRLADKRFR
GVAKGVGTCA VVGRIHMAQL QIGNDFFPIS LMVVEDDLVD MMLGLDMLKR HQCIIDLRQN
CLVIGTTGVN APFLMEHELP AGLMEMKRDL FEGTTKLPDE EDIAKVMEFG FSREEAIKAL
KMRNNVKQAV AYLVAQNVNK HFPAK
//
