ID C5FFG3_ARTOC Unreviewed; 513 AA.
AC C5FFG3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
GN ORFNames=MCYG_02229 {ECO:0000313|EMBL:EEQ29410.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29410.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995702; EEQ29410.1; -; Genomic_DNA.
DR RefSeq; XP_002849295.1; XM_002849249.1.
DR AlphaFoldDB; C5FFG3; -.
DR STRING; 554155.C5FFG3; -.
DR GeneID; 9223232; -.
DR VEuPathDB; FungiDB:MCYG_02229; -.
DR eggNOG; KOG0012; Eukaryota.
DR HOGENOM; CLU_020435_2_0_1; -.
DR OMA; QIGNDHL; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000002035; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT DOMAIN 52..139
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 471..513
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 136..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 54813 MW; EB4FF6289CB88DC6 CRC64;
MDGREPLLIH GSASAAFPLL RWICPGSRPS SDLLDRKPGR VLGLLAAHIS RVILLLRAAR
LSVVASNVAV SSDIVTLDVG EDMTLADLKA VIQSDIQIPP QSQYLSHNNQ PLTDDSKPLG
QIGISEGDML GMRIQVPTPG SGPGQVNSSH SAAAGGGAGG APQHGESSRG SQAIPDPETI
RLHMLGDPRA LAAVRQQNPH LASAINDPQR FRQIMLSHRR AEAQAEAAKE ARIAMLNADP
FNLDAQREIE EIIRQNAVTE NLHTAMEHTP EAFGRVSMLY IPVEVNGHKV KAFVDSGAQV
TIMSPECASA CNIMRLIDRR YGGIAKGVGT ASILGRVHCA EIKIGDMFLP CSFTVMDGKH
IDLLLGLDML KRHQACIDLK EGVLKIRDET VPFLHEADIP KHQDEFENEP MVMGRDGAVV
GGRTGAVQQA AGGLTMPRHL PRPVPRPAPS APPRPSVAAT VPPPTSNTPP QRPSRWPADA
IAKITDLGFT RDEAIQALDA ADGNLDGAIG YLI
//
