ID   DDB1_DICDI              Reviewed;        1181 AA.
AC   B0M0P5; Q23865;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=DNA damage-binding protein 1;
DE   AltName: Full=DNA repair protein E;
DE   AltName: Full=UV-damaged DNA-binding protein 1;
GN   Name=repE; Synonyms=ddb1; ORFNames=DDB_G0286013;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=AX3;
RX   PubMed=8710499; DOI=10.1093/nar/24.12.2295;
RA   Alexander H., Lee S.-K., Yu S.-L., Alexander S.;
RT   "repE--the Dictyostelium homolog of the human xeroderma pigmentosum group E
RT   gene is developmentally regulated and contains a leucine zipper motif.";
RL   Nucleic Acids Res. 24:2295-2301(1996).
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   DEVELOPMENTAL STAGE.
RC   STRAIN=AX4;
RX   PubMed=9171087; DOI=10.1093/nar/25.12.2365;
RA   Lee S.-K., Yu S.-L., Garcia M.X.U., Alexander H., Alexander S.;
RT   "Differential developmental expression of the rep B and rep D xeroderma
RT   pigmentosum related DNA helicase genes from Dictyostelium discoideum.";
RL   Nucleic Acids Res. 25:2365-2374(1997).
RN   [4]
RP   INDUCTION BY UV.
RX   PubMed=9765592; DOI=10.1016/s0167-4781(98)00103-1;
RA   Lee S.-K., Yu S.-L., Alexander H., Alexander S.;
RT   "A mutation in repB, the dictyostelium homolog of the human xeroderma
RT   pigmentosum B gene, has increased sensitivity to UV-light but normal
RT   morphogenesis.";
RL   Biochim. Biophys. Acta 1399:161-172(1998).
RN   [5]
RP   INDUCTION BY UV AND CISPLATIN.
RX   PubMed=9649625; DOI=10.1093/nar/26.14.3397;
RA   Yu S.-L., Lee S.-K., Alexander H., Alexander S.;
RT   "Rapid changes of nucleotide excision repair gene expression following UV-
RT   irradiation and cisplatin treatment of Dictyostelium discoideum.";
RL   Nucleic Acids Res. 26:3397-3403(1998).
RN   [6]
RP   INDUCTION BY UV, AND DEVELOPMENTAL STAGE.
RX   PubMed=11004503; DOI=10.1016/s0167-4781(00)00063-4;
RA   Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S.,
RA   Alexander H.;
RT   "Differential developmental expression and cell type specificity of
RT   Dictyostelium catalases and their response to oxidative stress and UV-
RT   light.";
RL   Biochim. Biophys. Acta 1492:295-310(2000).
CC   -!- FUNCTION: Plays a role in DNA repair. May be a component of an E3
CC       ubiquitin-protein ligase which promotes histone ubiquitination in
CC       response to UV irradiation. Histone ubiquitination may be important for
CC       subsequent DNA repair (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Levels accumulate after the removal of the food
CC       source and increase with the onset of development (accumulation at 1-3
CC       hours) peaking at 5-7 hours of development and declining abruptly. Not
CC       expressed by mitotically dividing cells. Not measurable during
CC       vegetative growth on bacteria. {ECO:0000269|PubMed:11004503,
CC       ECO:0000269|PubMed:8710499, ECO:0000269|PubMed:9171087}.
CC   -!- INDUCTION: Down-regulated in response to UV-damage followed by an
CC       increase in transcription back to basal level. Shows slight increase in
CC       transcription following cisplatin treatment.
CC       {ECO:0000269|PubMed:11004503, ECO:0000269|PubMed:9649625,
CC       ECO:0000269|PubMed:9765592}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC47162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U50042; AAC47162.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AAFI02000085; EAL64385.2; -; Genomic_DNA.
DR   PIR; S71092; S71092.
DR   RefSeq; XP_637896.2; XM_632804.2.
DR   AlphaFoldDB; B0M0P5; -.
DR   SMR; B0M0P5; -.
DR   STRING; 44689.DDB0191144; -.
DR   PaxDb; B0M0P5; -.
DR   EnsemblProtists; EAL64385; EAL64385; DDB_G0286013.
DR   GeneID; 8625406; -.
DR   KEGG; ddi:DDB_G0286013; -.
DR   dictyBase; DDB_G0286013; repE.
DR   eggNOG; KOG1897; Eukaryota.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; B0M0P5; -.
DR   OMA; CTEMEHE; -.
DR   PhylomeDB; B0M0P5; -.
DR   Reactome; R-DDI-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-DDI-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR   Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:B0M0P5; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:dictyBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   SUPFAM; SSF50998; SSF50998; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1181
FT                   /note="DNA damage-binding protein 1"
FT                   /id="PRO_0000376007"
FT   REGION          150..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          882..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1181 AA;  132254 MW;  B05F8B5B66FB77B8 CRC64;
     MYNFVSTVQK PTSVTHSVTG NFTGPNDKNL IISKCTKIEI FLMDQDGLKP MFDVNIYGRI
     SVLKLFSVAG SKQDYLFIST ESFKFCILAY DYEKKEIITK ASGNAEDTIG RPTEAGQLGI
     IDPDGRIVAL HLYEGLLKLI TLDNNNTPNK INNNNNNNNN NNNNNNNNNN NNINNNNFNI
     NNNNNNSPIQ KNVNNVRLEE LQVLDMTFLY GCKVPTIAVL FKDTKDEKHI STYEISSKDT
     ELVVGPWSQS NVGVYSSLLV PVPLGGVLVV ADNGITYLNG KVTRSVAVSY TKFLAFTRVD
     KDGSRFLFGD HFGRLSVLVL IHQQQKVMEL KFEQLGRISI PSSISYLDSG VVYIGSSSGD
     SQLIRLNTEK DQTTDSYVTY LEAFTNIGPV VDFCVVDAEK QGQAQIVTCS GTYRDGSLRI
     IRNGIGIAEQ ASIELEGIKG IFPINNNNNN NNNNNNNNNN NNNNNSNGIT DSKDRYLITS
     FIECTKVLSF QGEEIEETEF EGLESNCSTL YCGTIDKLNL LIQITNVSIN LIDSNTFKRV
     SQWNVEPSRR INLVSTNQDQ IVLSIDKSLL YFQINSSNKS IQLVKEIELP HEISCIDISP
     FDSFMDTKSQ LVSVGLWNDI TLRIFKLPTL EEIWKEPLGG EILPRSILMI SFDSIDYIFC
     SLGDGHLFKF QFDFSSFKLF DKRKLTLGTQ PIILKKFKLK NTINIFAISD RPTVIYSHNK
     KLFYSVVNLK DVTNVTSFNS DGFPNSMAIA TTNSLTIGTI DEIQKLHIKT IPLNEEMGRR
     IVHLEDHSCY AVITVKNNEG LLGGAQDLCE EDEEVSYIRI YNDQTFELIS SYKLDPYEMG
     WSITPCKFAG DDVNTYLAVG TSINTPIKSS GRVLLFSLSS SSSSNDKDSL DNNNNNNNNS
     GANGKLTLLE EIKFRSSVYF LLSFNGRLIA AVHKRLFSIR YTHSKEKNCK VISSESVHKG
     HTMILKLASR GHFILVGDMM KSMSLLVEQS DGSLEQIARN PQPIWIRSVA MINDDYFIGA
     EASNNFIVVK KNNDSTNELE RELLDSVGHY HIGESINSMR HGSLVRLPDS DQPIIPTILY
     ASVNGSIGVV ASISEEDFIF FSKLQKGLNQ VVRGVGGFSH ETWRAFSNDH HTIDSKNFID
     GDLIETFLDL KYESQLKAVA DLGITPDDAF RRIESLMQYI R