ID   W2LRR7_PHYPR            Unreviewed;       353 AA.
AC   W2LRR7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=UBA domain-containing protein {ECO:0000259|PROSITE:PS50030};
GN   ORFNames=L917_03813 {ECO:0000313|EMBL:ETL99345.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL99345.1};
RN   [1] {ECO:0000313|EMBL:ETL99345.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL99345.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DDI1 family.
CC       {ECO:0000256|ARBA:ARBA00009136}.
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DR   EMBL; KI678376; ETL99345.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2LRR7; -.
DR   EnsemblProtists; ETL99345; ETL99345; L917_03813.
DR   VEuPathDB; FungiDB:PPTG_22315; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
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; cd14309; UBA_scDdi1_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; IPR019103; Peptidase_aspartic_DDI1-type.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
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   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF46934; UBA-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          312..352
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          265..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  38598 MW;  7E4A6D4716F21116 CRC64;
     MKLHEIPANP TPEILLDIMD KNPQLLAELQ QVNPKLATAL QTKSVSDVRM ALMQMHMEAA
     SRKFEEQQEI EALERNPFDA EAQAKIAERI RLSNVQKNME IAIEEMPEAF GHVTMLYIPC
     EVNGTQVKAF VDSGAQSTIM SSSCAERCGI MRLVDKRFAG QAVGVGTTKI IGRVHMAPLK
     IGNEFYNCSF TILDQQGVDF LFGLDMLKRH QVCYNKCFGY RALLTDLCVY PSSWFQCCID
     LSKNVLRLHE GDSFHEVSFL PEHEIPSSEN RADSAQPPAT LGGVPVPAST PGSTPTSAAA
     APQPAPAASG GQNDQEKIAQ LVGLGFPEQR AIQALQTCNG NVEMAAGLLF ESM
//