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Database: UniProt
Entry: A0A077YX09_TRITR
LinkDB: A0A077YX09_TRITR
Original site: A0A077YX09_TRITR 
ID   A0A077YX09_TRITR        Unreviewed;       525 AA.
AC   A0A077YX09;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=DDI1 homolog 2 {ECO:0000313|EMBL:CDW52274.1};
GN   ORFNames=TTRE_0000053301 {ECO:0000313|EMBL:CDW52274.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW52274.1};
RN   [1] {ECO:0000313|EMBL:CDW52274.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW52274.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DDI1 family.
CC       {ECO:0000256|ARBA:ARBA00009136}.
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DR   EMBL; HG805818; CDW52274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077YX09; -.
DR   STRING; 36087.A0A077YX09; -.
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   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
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; 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; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          480..520
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
SQ   SEQUENCE   525 AA;  58764 MW;  51B9CD217F902082 CRC64;
     MPKLANQSWR SSVRPKRYGI RKSEEDMQKN QELLASQRSI TIRLAKFDMR MKARYFKRDE
     QWVRPHSSLV AKIAYISDEQ DTKIAVECDD QRGEDGSIQQ QLKTREICIR LSIHIVSVDD
     EIDCSERVVC TRFQIKMSES VSSDSVMTES TAATELQLTI VVNGEEIFPV VAQRSMTVKA
     LTDHCKQYSA TLNEHGFSVG VSFNGQFLTD HSRTLGDCGV KNGDALSFHV VPTEDLEAIN
     VVQQISNDPN AAAAIISSNP ELLEAITRRD LAKVKQLLPA AVQSARNAPG RAEKMRNPTD
     PDVQKLIEEN IRLENIDSMF VHAMEHMPET FGSVSMLFIR CKVNNFDTTA FVDSGAQATI
     ISEDFAERCG LMRLIDRRFS GVAMGVGTCK ILGRVHIAQL QIENVFLAVS CMVVEKQPMD
     ILFGLDMLKR HQCVIDLKEN CLIVGEARTP FLAEHEMPAI CRQVQDQAGP SIRLRLDGAN
     FAEEDIRKVT RCGFTVAQAI EGLKYSNGDV KKAIAWLVVR NLDKP
//
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