ID A0A2V5HZY0_9EURO Unreviewed; 375 AA.
AC A0A2V5HZY0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN ORFNames=BP00DRAFT_429101 {ECO:0000313|EMBL:PYI27634.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI27634.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI27634.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI27634.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC proteasomal degradation. Involved in nucleotide excision repair.
CC {ECO:0000256|RuleBase:RU367049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367049}.
CC Cytoplasm {ECO:0000256|RuleBase:RU367049}.
CC -!- SIMILARITY: Belongs to the RAD23 family.
CC {ECO:0000256|RuleBase:RU367049}.
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DR EMBL; KZ825565; PYI27634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5HZY0; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd14280; UBA1_Rad23_like; 1.
DR CDD; cd14281; UBA2_Rad23_like; 1.
DR CDD; cd01805; Ubl_Rad23; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 1.10.10.540; XPC-binding domain; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR NCBIfam; TIGR00601; rad23; 1.
DR PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR PANTHER; PTHR10621:SF0; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF101238; XPC-binding domain; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367049};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367049};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367049};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 146..186
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 327..368
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 77..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 39828 MW; 55CF180BC5B1FEF5 CRC64;
MKLTFKDLKQ QKFVIDAEPS ETVGEVKGKI SQEKGWEVAQ LKLIYSGKIL QDDKTIESYS
IEEKGFIVCM VSKPKPSASG ASTQAPSTPA RVAASTPAAP AAPAAPAPSA STASPAAPAT
PSPAASGTSQ PAGPAFNDPS ALLRGSQSDA VVAQMESMGF PRSDINRAMR AAFFNPDRAI
EYLLNGIPDN IQEEQQQQAA AASAPQTSAS PAEESAPAPV GDEHVNLFEA AAQAGGQEGG
TRGARSGAGS GEGLPSLDFL RNNPHFQQLR QLVQQQPQML EPILQQVATG NPQIAQLIGQ
NEEQFLQLLS EEDDAALPPG THQIHVTEEE RDAIERLCRL GFSRDLVIQA YFACDKNEEL
AANYLFENPD DPDDL
//
