GenomeNet

Database: UniProt
Entry: W2XJZ7_PHYPR
LinkDB: W2XJZ7_PHYPR
Original site: W2XJZ7_PHYPR 
ID   W2XJZ7_PHYPR            Unreviewed;       353 AA.
AC   W2XJZ7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=UBA domain-containing protein {ECO:0000259|PROSITE:PS50030};
GN   ORFNames=F441_04052 {ECO:0000313|EMBL:ETP22733.1};
OS   Phytophthora parasitica CJ01A1.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP22733.1, ECO:0000313|Proteomes:UP000018958};
RN   [1] {ECO:0000313|EMBL:ETP22733.1, ECO:0000313|Proteomes:UP000018958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP22733.1,
RC   ECO:0000313|Proteomes:UP000018958};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL   Submitted (NOV-2013) 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:ETP22733.1}.
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DR   EMBL; ANIX01000921; ETP22733.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2XJZ7; -.
DR   EnsemblProtists; ETP22733; ETP22733; F441_04052.
DR   Proteomes; UP000018958; 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;  38568 MW;  6233084E7A8B7416 CRC64;
     MKLHEIPANP TPEILLDIMD KNPQLLAELQ QVNPKLATAL QTKSVSDVRM ALMQMHMEAA
     SRKFEEQQEI EALERNPFDA EAQAKIAERI RLSNVQKNME IAIEEMPEAF GHVTMLYIPC
     EVNGTQVKAF VDSGAQSTIM SSSCAERCGI MRLVDKRFAG QAVGVGTAKI IGRVHMAPLK
     IGNEFYNCSF TILDQQGVDF LFGLDMLKRH QVCYNKCFGY RALLTDLCVY PSSWFQCCID
     LSKNVLRLHE GDSFHEVSFL PEHEIPSSEN RADSAQPPAT LGGVPVPAST PGSTPTSAAA
     APQPAPAASG GQNDQEKIAQ LVGLGFPEQR AIQALQTCNG NVEMAAGLLF ESM
//
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