ID F2S687_TRIT1 Unreviewed; 638 AA.
AC F2S687;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
GN ORFNames=TESG_06427 {ECO:0000313|EMBL:EGD99070.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGD99070.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD99070.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) 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; GG698518; EGD99070.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S687; -.
DR HOGENOM; CLU_020435_2_1_1; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000009172; 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 170..252
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 596..638
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 246..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 68260 MW; 164393F3469408F2 CRC64;
MAAKVEEKRR PCIRTQTQEA INMNQTAWMG ANCAASAVLC PPLRILSSCH TAIIAAGQPA
IHCCCWSCWN FAGVVVVVVV EKEPPASSAF GAWKAFDVNF NFNRQPQPLP ASPILFITLP
PRPRELPPGT AQHIQETKIR KIPRETVRDT LTHSLTTPST TDLVQDRVGR RITVSVVASN
VAVSSDIVTL DVGEDMTLAD LKAVIQSDVQ IPPQSQHLFH NNQPLTDDSK PLGQLGISEG
DMLGMHIRVP TPASGPGQGN PSRAGAGAAS QQGESSRGGQ PTIPDPETIR LHMLGDPRVL
AAVRQQNPQL ASAVDDPRRF REIMMSHRRA EAQAEAAKEA RIAMLNADPF NLDAQREIEE
IIRQNAVTEN LHTAMEHTPE AFGRVTMLYI PVEVNGHKVK AFVDSGAQVT IMSPACASAC
NIMRLIDRRY GGIAKGVGTA NILGRVHCAE IKIGDMFLPC SFTVMDGKHI DLLLGLDMLK
RHQACIDLKE GVLKIRDETV PFLHEADIPK HQDEFEDEPM VRGSDGAIIG GRTGAVQHPA
AAGGTAAFPR PALPTSLHRP PPTGPSPGLS PAPSAATPAA NPAANPAAAV ANAPPQRASR
WPADSIAKIT DLGFTRDEAI QALDAANGNL DGAIGYLI
//
