GenomeNet

Database: UniProt
Entry: W2SEP1_9EURO
LinkDB: W2SEP1_9EURO
Original site: W2SEP1_9EURO 
ID   W2SEP1_9EURO            Unreviewed;       450 AA.
AC   W2SEP1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
GN   ORFNames=HMPREF1541_01353 {ECO:0000313|EMBL:ETN47162.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN47162.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN47162.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN47162.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., 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 Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable aspartic protease. May be involved in the regulation
CC       of exocytosis. Acts as a linker between the 19S proteasome and
CC       polyubiquitinated proteins via UBA domain interactions with ubiquitin
CC       for their subsequent degradation. Required for S-phase checkpoint
CC       control. {ECO:0000256|ARBA:ARBA00003231}.
CC   -!- SUBUNIT: Binds ubiquitin and polyubiquitinated proteins.
CC       {ECO:0000256|ARBA:ARBA00011128}.
CC   -!- SIMILARITY: Belongs to the DDI1 family.
CC       {ECO:0000256|ARBA:ARBA00009136}.
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DR   EMBL; KB822711; ETN47162.1; -; Genomic_DNA.
DR   RefSeq; XP_008711874.1; XM_008713652.1.
DR   AlphaFoldDB; W2SEP1; -.
DR   STRING; 1220924.W2SEP1; -.
DR   MEROPS; A28.A06; -.
DR   GeneID; 19968692; -.
DR   VEuPathDB; FungiDB:HMPREF1541_01353; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; W2SEP1; -.
DR   OrthoDB; 1332686at2759; -.
DR   Proteomes; UP000030752; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05479; RP_DDI; 1.
DR   CDD; cd01796; Ubl_Ddi1_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR033882; DDI1_N.
DR   InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR015940; UBA.
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; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW   Protease {ECO:0000256|ARBA:ARBA00022750};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT   DOMAIN          6..86
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          412..450
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          85..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  49062 MW;  59AB513F57FB7770 CRC64;
     MYVLQTQISV TVIDGPNNAN ITSDFVTLDV SPDFTFGELK ALIETETNAP KASQLLSRDG
     QPITNDTKTL SEVGVTEGDL IALSIQPTRT TQQPQNRSGQ PSPEQFRQHI LSNAAVMNSV
     RQQDPELAAA AQDSTRFQNL FAARQRRLEE DRRQAEREMA RLDNDFWNPD SQAEIEKRIK
     QQQIAKNIEL AMEENPESFA RVSMLYIDVV VNNVPIKAFV DSGAQTTIMS PDAARRCNIT
     HLIDERYGGI ARGVGTAKIL GRVHHATMQL GVYQAASSFT VMEGKDVDLL LGLDMLKRHQ
     MCIDLRENCL RVQDAKIEFL PEHQIPNMMD EALDNEPKVE GPGGTTIGAE TGTVAPPPKP
     QESSQPAAAS DSSSQPAQSS NTPAPAPQQP QQPSQQTTSA QGGSFGFGQT QAITEESIAA
     VMQFGVDREM AVNLLQQAGG NPDLAISLML
//
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