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Database: UniProt
Entry: A0A1E4S6K8_CYBJN
LinkDB: A0A1E4S6K8_CYBJN
Original site: A0A1E4S6K8_CYBJN 
ID   A0A1E4S6K8_CYBJN        Unreviewed;       408 AA.
AC   A0A1E4S6K8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN   ORFNames=CYBJADRAFT_176460 {ECO:0000313|EMBL:ODV75110.1};
OS   Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS   / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV75110.1, ECO:0000313|Proteomes:UP000094389};
RN   [1] {ECO:0000313|EMBL:ODV75110.1, ECO:0000313|Proteomes:UP000094389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC   NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV453926; ODV75110.1; -; Genomic_DNA.
DR   RefSeq; XP_020072149.1; XM_020216788.1.
DR   AlphaFoldDB; A0A1E4S6K8; -.
DR   STRING; 983966.A0A1E4S6K8; -.
DR   GeneID; 30991184; -.
DR   OMA; PHMLEPI; -.
DR   OrthoDB; 158575at2759; -.
DR   Proteomes; UP000094389; 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; 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; 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|RuleBase:RU367049};
KW   DNA repair {ECO:0000256|RuleBase:RU367049};
KW   Nucleus {ECO:0000256|RuleBase:RU367049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094389}.
FT   DOMAIN          1..73
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          154..194
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          366..406
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          78..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  42838 MW;  C0532F8F37884D69 CRC64;
     MQVIFKDFKK EKIPVEVAPE ETVLDAKKKL AEIKGVEASQ LKFVYSGKVL QDDKTIQETK
     IKADDQVIFM ISKAVKKATP STPAQPTTTQ TPTAPRAQAP VAQVPAQEPA PAAAAAAAAA
     LPEQQTPSNS AAVDASSASA EPQSFDASTF AVGSAREQAI ANIMEMGYER SQVEAALRAA
     FNNPDRAVEY LLTGIPESAQ VPVQGQQQAQ QSGDQQGQEA EQGASDAPTA IEEIVEEDVV
     VGDADADEDD DDQHGDLFAA AAAASAGGAI GGADASSPGG ANAAGNIDLG SAEGLRRLAQ
     ESPEALEGLL TMLAQQNPQL SSLIQQHPEE FIRMLLQGPE GLEDVEGGEL AQPQLGEGEE
     LPQITPDDEN AINRLMELGF DRGTVVQVYF ACDKNEELAA NILFNDHA
//
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