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Database: UniProt
Entry: A0A068SEZ4_9FUNG
LinkDB: A0A068SEZ4_9FUNG
Original site: A0A068SEZ4_9FUNG 
ID   A0A068SEZ4_9FUNG        Unreviewed;       391 AA.
AC   A0A068SEZ4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN   ORFNames=LCOR_11705.1 {ECO:0000313|EMBL:CDH60928.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH60928.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH60928.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) 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:CDH60928.1}.
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DR   EMBL; CBTN010000116; CDH60928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068SEZ4; -.
DR   STRING; 1263082.A0A068SEZ4; -.
DR   VEuPathDB; FungiDB:LCOR_11705.1; -.
DR   OrthoDB; 158575at2759; -.
DR   Proteomes; UP000027586; 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   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:UP000027586};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          151..191
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          344..385
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          74..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  42656 MW;  323AC8C6529CD705 CRC64;
     MQLTVKTLQQ KQFKLDVEGS DTILSVKQKI EESQGHAVSQ QKLIFSGKIL ADDKKVEEYN
     ISEKDFLVVM VSKPKTTSSA AGSSTSASTP TEKKQETPKQ QEEKPAPAST TTQSQPAPAA
     AAAATTTTPS TQAPTQENTQ VSSDSSLVTG SQYESVVQNM MEMGFERDQV KRALRASFNN
     PDRAVEYLFN GIPEDLLAEE QAEQAHSQEQ QQQQQDGAPN TTETPAAAAT SPNSTQTRGN
     DASQNLFLAA QQAAQQQQQQ QQQSGTGNVD FSQLRNTPHF QQLRQLVQSN PSLLQPLLQQ
     LGQSNPELLR MINSDPQGFF QLLMEGGDEE GGAVPPGSHV IQVTQEEKEA IDRLEGLGFD
     RAQAIEAYFA CDKNEELAAN YLFDNGADDF E
//
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