CDB4_SCHPO
ID CDB4_SCHPO Reviewed; 381 AA.
AC Q09184;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Curved DNA-binding protein;
DE AltName: Full=42 kDa protein;
GN Name=cdb4; ORFNames=SPAC23H4.09;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 5-31.
RC STRAIN=972 / ATCC 24843;
RX PubMed=7985416; DOI=10.1002/yea.320100704;
RA Yamada H., Mori H., Momoi H., Nakagawa Y., Ueguchi C., Mizuno T.;
RT "A fission yeast gene encoding a protein that preferentially associates
RT with curved DNA.";
RL Yeast 10:883-894(1994).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND THR-362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: A non-essential protein that preferentially binds curved DNA.
CC Binds non-curved DNA with a much lower affinity.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
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DR EMBL; D14907; BAA03607.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11663.1; -; Genomic_DNA.
DR PIR; S46583; S46583.
DR RefSeq; NP_593397.1; NM_001018829.2.
DR AlphaFoldDB; Q09184; -.
DR SMR; Q09184; -.
DR BioGRID; 278308; 6.
DR STRING; 4896.SPAC23H4.09.1; -.
DR iPTMnet; Q09184; -.
DR MaxQB; Q09184; -.
DR PaxDb; Q09184; -.
DR PRIDE; Q09184; -.
DR EnsemblFungi; SPAC23H4.09.1; SPAC23H4.09.1:pep; SPAC23H4.09.
DR GeneID; 2541817; -.
DR KEGG; spo:SPAC23H4.09; -.
DR PomBase; SPAC23H4.09; cdb4.
DR VEuPathDB; FungiDB:SPAC23H4.09; -.
DR eggNOG; KOG2776; Eukaryota.
DR HOGENOM; CLU_041451_2_1_1; -.
DR InParanoid; Q09184; -.
DR OMA; HTVLLMP; -.
DR PhylomeDB; Q09184; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:Q09184; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0004518; F:nuclease activity; TAS:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR004545; PA2G4.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00495; crvDNA_42K; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..381
FT /note="Curved DNA-binding protein"
FT /id="PRO_0000148991"
FT MOTIF 368..375
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 381 AA; 41598 MW; A87AE1346597CF49 CRC64;
MSTKEATSET AVDYSLSNPE TVNKYKIAGE VSQNVIKKVV ELCQPGAKIY DICVRGDELL
NEAIKKVYRT KDAYKGIAFP TAVSPNDMAA HLSPLKSDPE ANLALKSGDV VKILLGAHID
GFASLVATTT VVSEEPVTGP AADVIAAASA ALKAAQRTIK PGNTNWQVTD IVDKIATSYG
CKPVAGMLSH QQEREVIDGK KQVILNPSDS QRSEMDTFTF EEGEVYGVDI LVSTSPSGKV
KRSDIATRIY KKTDTTYMLK LQASRKVYSE IQTKFGPFPF STRNISFDSR TNMGLNECTS
HKLLFPYEVL LDKDGGIVAE FYSTIALTKK GTIILSDSEP KEDFIKSDKK VEDPEIVALL
ETPIKVTKNK KKSKKPSKAN E
