ID S3D2E1_GLAL2 Unreviewed; 430 AA.
AC S3D2E1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
GN ORFNames=GLAREA_12597 {ECO:0000313|EMBL:EPE31294.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE31294.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE31294.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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; KE145362; EPE31294.1; -; Genomic_DNA.
DR RefSeq; XP_008081569.1; XM_008083378.1.
DR AlphaFoldDB; S3D2E1; -.
DR STRING; 1116229.S3D2E1; -.
DR GeneID; 19471637; -.
DR KEGG; glz:GLAREA_12597; -.
DR eggNOG; KOG0012; Eukaryota.
DR HOGENOM; CLU_020435_2_0_1; -.
DR OMA; QIGNDHL; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000016922; 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 CDD; cd01796; Ubl_Ddi1_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; IPR033882; DDI1_N.
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; 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; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF46934; UBA-like; 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:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EPE31294.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT DOMAIN 10..86
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 390..430
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 330..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 46483 MW; BBB7DD9F70023A1B CRC64;
MSECIRRITL SITAPTHDGD LLSLEILPET TVSVLKESVS AEAQIPAASQ HLYHNGQLLN
DDTKTMEQLQ IGDGEMLALH VRDMAAPRRP QPAAQAAPQQ RDGADPETLR LRLLGDPAIR
QQAANQQPEL AAAAEDPQRF AQLFRQMQDS ERQEQERRRQ HIADLNADPF DIDAQMRIAE
MIREERVQEN LQNAIEHNPE VFGRVHMLYI DVEVNGHKVK AFVDSGAQAT IMSPSCAETC
GIMRLVDKRF AGVAKGVGTA AILGRVHSAQ IKIGNLFLPC SFTVMEGKDV DLLLGLDMLK
RHQACIDLSK DKLVIQGVEV SFLGEADIPK NMEEERAEEP KVAGPGGTTI GAKSGAVDGP
SMTQPTASAS SSTPQTGPQA PTPAAPPQPE FPQQSIDTLV ALGFSREEAV NALNACGGNV
EYAAGLLFQG
//
