ID D4DJL4_TRIVH Unreviewed; 773 AA.
AC D4DJL4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
GN ORFNames=TRV_07382 {ECO:0000313|EMBL:EFE37977.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE37977.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE37977.1}.
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DR EMBL; ACYE01000438; EFE37977.1; -; Genomic_DNA.
DR RefSeq; XP_003018622.1; XM_003018576.1.
DR AlphaFoldDB; D4DJL4; -.
DR GeneID; 9580773; -.
DR KEGG; tve:TRV_07382; -.
DR HOGENOM; CLU_020435_2_1_1; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000008383; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 297..379
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 731..773
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 82776 MW; 9CBBBCD0E8F0C168 CRC64;
MQHLGPPAAR KGQSKGEKKE RSRAGRENRL FTIPGWGWNG MTGRTVATAC SAANPHPPPF
VSEDGSKSRG EKAALHSHAD AGGNQYESDC MDGRELLLIH GLLSASLPFP LLLRLLSAGA
ASAVLCPPPH HILRYLPASS SARRTQLRIA SLQAPAQAAA QAAVVVAAAA AVVACCWSFA
ESWCRCRRGK RAACVICLWR LEESLQRQRQ RQLQHPTSAS LFITLHPLRP LQPRPRELPP
GTAQHIQETK IRKIPRTDTP DTHSLTHSYS VYRDLVQDVS GFQPGKGFPH TNQRVDRRIT
VSVVASNVAV SSDIVTLDVG EDMTLADLKA VIQSEIQIPP QSQHLFHNNR PLADESKPLG
QLGISEGDML GMHIRVPTPA SGPGQGNPSG AGAGAASQQG DSSRGGQPTI PDPETIRLHM
LGDPRVLAAV RQQNPQLASA VDDPRRFREI MMSHRRAEAR VEAAKEARIA MLNADPFNLD
AQREIEEIIR QNAVTENLHT AMEHTPEAFG RVTMLYIPVE VNGHKVKAFV DSGAQVTIMS
PACASACNIM RLIDRRYGGI AKGVGTADIL GRVHCAEIKI GDMFLPCSFT VMDGKHIDLL
LGLDMLKRHQ ACIDLKEGVL KIRDETVPFL HEADIPKHQD EFEDEPMVRG SDGAIIGGRT
GAVQHPAAAG GTAAFPRPAL PTSLHRPPPT GPSPGLSPAP RPGPAATPAA TPAATPAAAT
PAAATANAPQ QRASRWPADS IAKITDLGFT RDEAIQALDA ANGNLDGAIG YLI
//
