ID CKN1_SCHPO Reviewed; 404 AA.
AC Q9USR0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=DNA excision repair protein ckn1;
GN Name=ckn1; ORFNames=SPBC577.09;
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 [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, DOMAIN, AND INTERACTION WITH DDB1.
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: Adapter protein for ddb1/cullin 4 ubiquitin ligases involved
CC in transcription-coupled nucleotide excision repair.
CC {ECO:0000269|PubMed:18794354}.
CC -!- SUBUNIT: Interacts with ddb1. {ECO:0000269|PubMed:18794354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The DDB-box is specifically required for ddb1-binding.
CC {ECO:0000269|PubMed:18794354}.
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DR EMBL; CU329671; CAB54817.1; -; Genomic_DNA.
DR PIR; T40553; T40553.
DR RefSeq; NP_595307.1; NM_001021214.2.
DR AlphaFoldDB; Q9USR0; -.
DR SMR; Q9USR0; -.
DR BioGRID; 277378; 2.
DR STRING; 284812.Q9USR0; -.
DR PaxDb; 4896-SPBC577-09-1; -.
DR EnsemblFungi; SPBC577.09.1; SPBC577.09.1:pep; SPBC577.09.
DR GeneID; 2540861; -.
DR KEGG; spo:SPBC577.09; -.
DR PomBase; SPBC577.09; ckn1.
DR VEuPathDB; FungiDB:SPBC577.09; -.
DR eggNOG; KOG4283; Eukaryota.
DR HOGENOM; CLU_032951_2_1_1; -.
DR InParanoid; Q9USR0; -.
DR OMA; CMTAVKA; -.
DR PhylomeDB; Q9USR0; -.
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 PRO; PR:Q9USR0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070912; C:Ddb1-Ckn1 complex; IDA:PomBase.
DR GO; GO:0000109; C:nucleotide-excision repair complex; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:PomBase.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR042238; Rad28/ERCC8/Ckn1/ATCSA-1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR46202; DNA EXCISION REPAIR PROTEIN ERCC-8; 1.
DR PANTHER; PTHR46202:SF1; DNA EXCISION REPAIR PROTEIN ERCC-8; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..404
FT /note="DNA excision repair protein ckn1"
FT /id="PRO_0000316565"
FT REPEAT 45..85
FT /note="WD 1"
FT REPEAT 101..141
FT /note="WD 2"
FT REPEAT 187..227
FT /note="WD 3"
FT REPEAT 244..283
FT /note="WD 4"
FT REPEAT 339..378
FT /note="WD 5"
FT MOTIF 1..19
FT /note="DDB-box"
SQ SEQUENCE 404 AA; 45541 MW; 799D78D76036017B CRC64;
MNSFLLAREW GQEPNSSFRR QLLQHRLQRL ALNPDVKIKR RHGAGILGSV NALSIDNTIH
QLMVSGGANS SINVWDLQNI DQKEDEDLIL DTLNAVPART SHKFGITDLH WFPFDNGIFT
SSSFDHTLKV WDVSTLQEAY TFTMEDMIYS HAWSPIASHC LIATAYRSSS IRLCDMQSGS
YTHSLSGHTG NVLAVDWCPK NEFVLASGSA DGTCRLWDIR KVSSSFACMD LHNKYLPSNQ
TNISHYGTVN GLAWTSDARY LASCGTDDRI RVWNMESGRN TLREFGPIIH NQTTSFAVHP
CMIQPSMDSD VFVLFPNDDG SLALLNLLEG SFVRRLSTHS LKRINCAAYR PDFEQCFTGD
MNGNIYMWSP KALKSPTKIS DLETRRNIIQ EVYDSLINIP VTYQ
//
