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
//