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Database: UniProt
Entry: A0A1B8EVM9_9PEZI
LinkDB: A0A1B8EVM9_9PEZI
Original site: A0A1B8EVM9_9PEZI 
ID   A0A1B8EVM9_9PEZI        Unreviewed;       434 AA.
AC   A0A1B8EVM9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
GN   ORFNames=VF21_05679 {ECO:0000313|EMBL:OBT75414.1};
OS   Pseudogymnoascus sp. 05NY08.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT75414.1, ECO:0000313|Proteomes:UP000092096};
RN   [1] {ECO:0000313|EMBL:OBT75414.1, ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|EMBL:OBT75414.1,
RC   ECO:0000313|Proteomes:UP000092096};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
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; KV458829; OBT75414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8EVM9; -.
DR   STRING; 1622149.A0A1B8EVM9; -.
DR   OrthoDB; 1332686at2759; -.
DR   Proteomes; UP000092096; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092096}.
FT   DOMAIN          1..82
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          394..434
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          83..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  46968 MW;  2564BD88082B3BA0 CRC64;
     MRLTLNIASE EALEQDLLNL EVPTETTVGS LKGMVQAEAH IPTTSQHIYH NGQLLSDDNK
     TLEQLQVVDG DMLALHVRDI IGNTGVPQPG PAQQPARRPA ASREEQDPEV IRLQLLGNPR
     MRQEVQRAQP ELAAAVENPQ RFAQLFRQMQ DQERRERMMR QQHIADLNAD PFDIDAQTRI
     AEMIREERVQ ENLQNAIEHN PEGKVHMLYI DVEVNGHKVK AFVDSGAQAT IMSPSCAESC
     GIMRLVDKRF AGIARGVGTA NILGRVHSAQ IKIGSLFLPC SFTVMEGKDV DLLLGLDMLK
     RHQACIDLSK DKLVIQDVEV PFLGEADIPR SFEEVTEPTV EGPGGTTIGG RSGAISGPAG
     PATANTPTAP VAQAAATPQP QHPTQPPQAA TASAPSAESI DQLVALGFSR EEAVNALNAC
     DGNVEFAAGL LFQG
//
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