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Database: UniProt
Entry: A0A1Q8S5S4_9PEZI
LinkDB: A0A1Q8S5S4_9PEZI
Original site: A0A1Q8S5S4_9PEZI 
ID   A0A1Q8S5S4_9PEZI        Unreviewed;       389 AA.
AC   A0A1Q8S5S4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN   ORFNames=CCHL11_02267 {ECO:0000313|EMBL:OLN96808.1};
OS   Colletotrichum chlorophyti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN96808.1, ECO:0000313|Proteomes:UP000186583};
RN   [1] {ECO:0000313|EMBL:OLN96808.1, ECO:0000313|Proteomes:UP000186583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTL11 {ECO:0000313|EMBL:OLN96808.1,
RC   ECO:0000313|Proteomes:UP000186583};
RA   Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT   "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT   herbaceous plants.";
RL   Submitted (NOV-2016) 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}.
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:OLN96808.1}.
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DR   EMBL; MPGH01000014; OLN96808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8S5S4; -.
DR   STRING; 708187.A0A1Q8S5S4; -.
DR   OrthoDB; 158575at2759; -.
DR   Proteomes; UP000186583; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000186583};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          144..184
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          339..380
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          77..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  40592 MW;  688424A0A3B5E8DB CRC64;
     MKVTFKDLKQ QKFTLDVEPT DLISSVKEKI AGEKGWDAKD QKLIYSGKIL KDEDTVESYK
     IEEKGFVVCM VNKPKKVNKP AESSSAPAVP ATPAQPVAAT PAAPPAPAAQ AAAPAAAPQT
     PTPAARTAGG DAAAPADPSM AMGAQRQEVI ANMEAMGFER AQIDAAMRAA FYNPDRAVEY
     LLNGIPDNVQ QEQQQRQAAA AAPAGQPAAG APVDDDGNVN LFDLAAQRGG SGGGGGGRGA
     GGNTAAAAAG AAAAAGAAAA QGGFGNLDFL RNNAQFQQLR QVVQQQPQML EPILQQLGAG
     NPQLAQLIAN NPDQFLQLLG EEVDDDVPLP PGAQAIQVTE EERDAIERLC RLGFDRDAAI
     QAYFACDKNE ELAANFLFDQ PDDDDPPQN
//
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