ID A0A178ZJ68_9EURO Unreviewed; 463 AA.
AC A0A178ZJ68;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-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=AYL99_04851 {ECO:0000313|EMBL:OAP59849.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP59849.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP59849.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP59849.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) 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}.
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:OAP59849.1}.
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DR EMBL; LVYI01000004; OAP59849.1; -; Genomic_DNA.
DR RefSeq; XP_018693216.1; XM_018836363.1.
DR AlphaFoldDB; A0A178ZJ68; -.
DR STRING; 1367422.A0A178ZJ68; -.
DR GeneID; 30009019; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000078343; 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 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:UP000078343}.
FT DOMAIN 17..97
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 425..463
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 97..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 49837 MW; 41103159D779B00F CRC64;
MAVPGNTNSQ DACIQRTSIT IISSDRELPT DLIPLDVGPD MTLNDIKAFV EAEIGVPPSA
QIFLRDGKAV TDTSMTLADF NIQEGGIIPM AIQANPPRRR AAQGATTGQP STQVDRGVND
SEALRTRILQ DPGVMADFRI RDPELVAAAQ DGQRFRDLLE ERFRQNERMQ REKEEQIALL
EADPFNVDAQ QKIEEMIRQE RVSENLQKAM DEFPEAFGKV TMLYIDVVVN GHPIKAFVDS
GAQTTIMSPS AAERCGILRL VDKRFGGIAK GVGTAQILGR VHSAEIQIGQ YDLASSFTVM
EGKDVDLLLG LDMLKRHQMC IDLKKNCLRI ENDEIPFLPE SELPKMMEEV LENEPKVAGP
GGSTVGAKTG TVMPGASTSS TQGRSGQASA STPGPSDRSG STATAIPSSV VQPHSGSSAF
GEPQPITAET IAQVTELGFT REEAIAALQQ TGGNVELAIG LLL
//
