RAD23_DICDI
ID RAD23_DICDI Reviewed; 342 AA.
AC Q54LV1; O97135;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=UV excision repair protein RAD23 homolog;
DE AltName: Full=repC-binding protein A;
GN Name=rcbA; Synonyms=rad23; ORFNames=DDB_G0286357;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX4;
RA Li G., Alexander H., Alexander S.;
RT "rcbA, the Dictyostelium discoideum homolog of yeast repair gene RAD23.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: May play a role both in proteasomal degradation of misfolded
CC proteins and DNA repair. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17913.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF103870; AAD17913.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000085; EAL64203.1; -; Genomic_DNA.
DR RefSeq; XP_637729.1; XM_632637.1.
DR AlphaFoldDB; Q54LV1; -.
DR SMR; Q54LV1; -.
DR STRING; 44689.DDB0191177; -.
DR PaxDb; Q54LV1; -.
DR EnsemblProtists; EAL64203; EAL64203; DDB_G0286357.
DR GeneID; 8625594; -.
DR KEGG; ddi:DDB_G0286357; -.
DR dictyBase; DDB_G0286357; rcbA.
DR eggNOG; KOG0011; Eukaryota.
DR HOGENOM; CLU_040364_0_0_1; -.
DR InParanoid; Q54LV1; -.
DR OMA; ANTVESY; -.
DR PhylomeDB; Q54LV1; -.
DR Reactome; R-DDI-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR PRO; PR:Q54LV1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.540; -; 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 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; SSF101238; SSF101238; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..342
FT /note="UV excision repair protein RAD23 homolog"
FT /id="PRO_0000327863"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 161..201
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 297..338
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 77..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 37044 MW; 1DF2383A34642BC5 CRC64;
MKVTIKNINK EIYVFEVNGD LTVAELKNLI SEKHNQTPSW QTLIYSGKIL EDKRTLESYN
ITDSGFIVMM IKKPREAPAT TPAPSTTPAP STTSAPTTTT TAEPTPTTSS TNNTSTTTPT
SVPTPTNNTP ATPNPTPTTS STPGSTSTTS PQQSSDFATG TELEATIKNI TDMGFARDQV
LRALRLTFNN AERAIEYLVS GNIPAANDPE DEEEMEGGGG SGDNPFEALR NHPHFNLLRE
AISKNPSIIP GILQQLAQTN PALVRQIQEN PNEFIRLFQG DGNPGGNPGQ FTLQVTQEES
EAIQRLQALT GMDKSTVIEA YFACDKNEEL TASYLFETAD DE