ID   DDB1_SCHPO              Reviewed;        1072 AA.
AC   O13807;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 144.
DE   RecName: Full=DNA damage-binding protein 1;
DE   AltName: Full=Damage-specific DNA-binding protein 1;
GN   Name=ddb1; ORFNames=SPAC17H9.10c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12181326; DOI=10.1074/jbc.m207890200;
RA   Zolezzi F., Fuss J., Uzawa S., Linn S.;
RT   "Characterization of a Schizosaccharomyces pombe strain deleted for a
RT   sequence homologue of the human damaged DNA binding 1 (DDB1) gene.";
RL   J. Biol. Chem. 277:41183-41191(2002).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CSN2.
RX   PubMed=12695334; DOI=10.1101/gad.1090803;
RA   Liu C., Powell K.A., Mundt K., Wu L., Carr A.M., Caspari T.;
RT   "Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by
RT   both checkpoint-dependent and -independent mechanisms.";
RL   Genes Dev. 17:1130-1140(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=12857752; DOI=10.1074/jbc.m303003200;
RA   Bondar T., Mirkin E.V., Ucker D.S., Walden W.E., Mirkin S.M.,
RA   Raychaudhuri P.;
RT   "Schizosaccharomyces pombe Ddb1 is functionally linked to the replication
RT   checkpoint pathway.";
RL   J. Biol. Chem. 278:37006-37014(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=14701809; DOI=10.1074/jbc.m312570200;
RA   Bondar T., Ponomarev A., Raychaudhuri P.;
RT   "Ddb1 is required for the proteolysis of the Schizosaccharomyces pombe
RT   replication inhibitor Spd1 during S phase and after DNA damage.";
RL   J. Biol. Chem. 279:9937-9943(2004).
RN   [6]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CSN1
RP   AND CDT2.
RX   PubMed=16252005; DOI=10.1038/sj.emboj.7600854;
RA   Liu C., Poitelea M., Watson A., Yoshida S.H., Shimoda C., Holmberg C.,
RA   Nielsen O., Carr A.M.;
RT   "Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-
RT   CSN ubiquitin ligase.";
RL   EMBO J. 24:3940-3951(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=15805471; DOI=10.1101/gad.329905;
RA   Holmberg C., Fleck O., Hansen H.A., Liu C., Slaaby R., Carr A.M.,
RA   Nielsen O.;
RT   "Ddb1 controls genome stability and meiosis in fission yeast.";
RL   Genes Dev. 19:853-862(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=17039252; DOI=10.1038/sj.embor.7400827;
RA   Ralph E., Boye E., Kearsey S.E.;
RT   "DNA damage induces Cdt1 proteolysis in fission yeast through a pathway
RT   dependent on Cdt2 and Ddb1.";
RL   EMBO Rep. 7:1134-1139(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=16407242; DOI=10.1074/jbc.c500464200;
RA   Hu J., Xiong Y.;
RT   "An evolutionarily conserved function of proliferating cell nuclear antigen
RT   for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA
RT   damage.";
RL   J. Biol. Chem. 281:3753-3756(2006).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH CKN1; IQW1 AND WDR21.
RX   PubMed=18794354; DOI=10.1128/mcb.00757-08;
RA   Fukumoto Y., Dohmae N., Hanaoka F.;
RT   "Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor
RT   proteins through a novel protein motif, the DDB-box.";
RL   Mol. Cell. Biol. 28:6746-6756(2008).
CC   -!- FUNCTION: Component of an E3 ubiquitin-protein ligase that includes
CC       cul4 (By similarity). Required for ubiquitination and the subsequent
CC       degradation of the DNA replication licensing factor cdt1 and of the
CC       ribonucleotide reductase inhibitor spd1. Also required for
CC       transcription-coupled nucleotide excision repair. {ECO:0000250,
CC       ECO:0000269|PubMed:12857752, ECO:0000269|PubMed:14701809,
CC       ECO:0000269|PubMed:15805471, ECO:0000269|PubMed:16252005,
CC       ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:17039252,
CC       ECO:0000269|PubMed:18794354}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with csn1, csn2, cdt2, ckn1, iqw1 and wdr21.
CC       {ECO:0000269|PubMed:12695334, ECO:0000269|PubMed:16252005,
CC       ECO:0000269|PubMed:18794354}.
CC   -!- INTERACTION:
CC       O13807; Q10990: cdt2; NbExp=4; IntAct=EBI-3647902, EBI-3505190;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12181326}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11219.1; -; Genomic_DNA.
DR   PIR; T37876; T37876.
DR   RefSeq; NP_593580.1; NM_001019012.2.
DR   AlphaFoldDB; O13807; -.
DR   SMR; O13807; -.
DR   BioGRID; 278682; 278.
DR   IntAct; O13807; 2.
DR   STRING; 4896.SPAC17H9.10c.1; -.
DR   MaxQB; O13807; -.
DR   PaxDb; O13807; -.
DR   EnsemblFungi; SPAC17H9.10c.1; SPAC17H9.10c.1:pep; SPAC17H9.10c.
DR   GeneID; 2542207; -.
DR   KEGG; spo:SPAC17H9.10c; -.
DR   PomBase; SPAC17H9.10c; ddb1.
DR   VEuPathDB; FungiDB:SPAC17H9.10c; -.
DR   eggNOG; KOG1897; Eukaryota.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; O13807; -.
DR   OMA; CTEMEHE; -.
DR   PhylomeDB; O13807; -.
DR   Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR   Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O13807; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; EXP:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0070912; C:Ddb1-Ckn1 complex; IDA:PomBase.
DR   GO; GO:0070913; C:Ddb1-Wdr21 complex; IDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IGI:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:PomBase.
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; IPR031297; DDB1.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..1072
FT                   /note="DNA damage-binding protein 1"
FT                   /id="PRO_0000079843"
SQ   SEQUENCE   1072 AA;  120655 MW;  70AB463DE14351F3 CRC64;
     MTYVTYLHKP SSIRNAVFCK FVNASSWNVI VAKVNCLEVY SYENNRLCLI TSANIFAKIV
     NVKAFKPVSS PTDHIIVATD SFRYFTLFWD ANDNTVSNGI KIQDCSERSL RESQSGPLLL
     VDPFQRVICL HVYQGLLTII PIFKSKKRFM TSHNNPSLHD NFSVRIQELN VVDIAMLYNS
     SRPSLAVLYK DSKSIVHLST YKINVREQEI DEDDVVCHDI EEGKLIPSEN GGVFVFGEMY
     VYYISKDIQV SKLLLTYPIT AFSPSISNDP ETGLDSSIYI VADESGMLYK FKALFTDETV
     SMELEKLGES SIASCLIALP DNHLFVGSHF NNSVLLQLPS ITKNNHKLEI LQNFVNIAPI
     SDFIIDDDQT GSSIITCSGA YKDGTLRIIR NSINIENVAL IEMEGIKDFF SVSFRANYDN
     YIFLSLICET RAIIVSPEGV FSANHDLSCE ESTIFVSTIY GNSQILQITT KEIRLFDGKK
     LHSWISPMSI TCGSSFADNV CVAVAGGLIL FFEGITEVGR YQCDTEVSSL CFTEENVVYV
     GLWSADIIML TYCQDGISLT HSLKLTDIPR SIVYSQKYGD DGGTLYVSTN NGYVLMFNFQ
     NGQVIEHSLR RNQLGVAPII LKHFDSKEKN AIFALGEKPQ LMYYESDKLV ITPLSCTEML
     NISSYVNPSL GVNMLYCTNS YISLAKMSEI RSLNVQTVSV KGFPRRICSN SLFYFVLCMQ
     LEESIGTQEQ RLLSFLRVYE KNTLSEIAHH KFNEYEMVES IILMNDDKRV VVGTGFNFPD
     QDAPDSGRLM VFEMTSDNNI EMQAEHKVQG SVNTLVLYKH LIVAGINASV CIFEYEHGTM
     HVRNSIRTPT YTIDISVNQD EIIAADLMKS ITVLQFIDDQ LIEVARDYHP LWATSVEILS
     ERKYFVTEAD GNAVILLRDN VSPQLSDRKK LRWYKKFYLG ELINKTRHCT FIEPQDKSLV
     TPQLLCATVD GSLMIVGDAG MSNTPLLLQL QDNIRKVIPS FGGLSHKEWK EYRGENETSP
     SDLIDGSLIE SILGLREPIL NEIVNGGHEG TKLDISVQDL KSIIENLEKL HP