ID   SAK1_SCHPO              Reviewed;         766 AA.
AC   P48383; O42876;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Protein sak1;
GN   Name=sak1; ORFNames=SPAC3G9.14;
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].
RX   PubMed=7862141; DOI=10.1128/mcb.15.3.1479;
RA   Wu S.Y., McLeod M.;
RT   "The sak1+ gene of Schizosaccharomyces pombe encodes an RFX family DNA-
RT   binding protein that positively regulates cyclic AMP-dependent protein
RT   kinase-mediated exit from the mitotic cell cycle.";
RL   Mol. Cell. Biol. 15:1479-1488(1995).
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-223; SER-224 AND SER-227, 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: Positively regulates cyclic AMP-dependent protein kinase-
CC       mediated exit from the mitotic cell cycle.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00858}.
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DR   EMBL; U19978; AAA67937.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA15923.1; -; Genomic_DNA.
DR   PIR; T11650; T11650.
DR   PIR; T52535; T52535.
DR   RefSeq; NP_594086.1; NM_001019499.2.
DR   AlphaFoldDB; P48383; -.
DR   SMR; P48383; -.
DR   BioGRID; 279843; 9.
DR   STRING; 4896.SPAC3G9.14.1; -.
DR   iPTMnet; P48383; -.
DR   SwissPalm; P48383; -.
DR   MaxQB; P48383; -.
DR   PaxDb; P48383; -.
DR   PRIDE; P48383; -.
DR   EnsemblFungi; SPAC3G9.14.1; SPAC3G9.14.1:pep; SPAC3G9.14.
DR   GeneID; 2543421; -.
DR   KEGG; spo:SPAC3G9.14; -.
DR   PomBase; SPAC3G9.14; sak1.
DR   VEuPathDB; FungiDB:SPAC3G9.14; -.
DR   eggNOG; KOG3712; Eukaryota.
DR   HOGENOM; CLU_011526_1_1_1; -.
DR   InParanoid; P48383; -.
DR   OMA; ECDWMMY; -.
DR   PhylomeDB; P48383; -.
DR   PRO; PR:P48383; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR003150; DNA-bd_RFX.
DR   InterPro; IPR039779; RFX-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12619; PTHR12619; 1.
DR   Pfam; PF02257; RFX_DNA_binding; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51526; RFX_DBD; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..766
FT                   /note="Protein sak1"
FT                   /id="PRO_0000215293"
FT   DNA_BIND        101..176
FT                   /note="RFX-type winged-helix"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT   REGION          271..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        728..766
FT                   /note="QQQQQATKNSLMEAAYQNAQKQKEDDYISIVFDTNGACS -> TTTTTSH
FT                   (in Ref. 1; AAA67937)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   766 AA;  86405 MW;  1792B52FF8FA605E CRC64;
     MNPSDLPGQI PLSRSDMNVQ DQLDPVQRFD THFMLPQEEN FLNRPSITSE SAHPRGSDLE
     QETELKRLAL EHEHYSLESL AEKLRMDHVS ANSEKFRQVF GICWLKRACE EQQDAAVQRN
     QIYAHYVEIC NSLHIKPLNS ASFGKLVRLL FPSIKTRRLG MRGHSKYHYC GIKLRGQDSF
     RRLRTFSDSS LSPVSCSSFP KPIPNHFEND VSSIQNTNQR VESSPASVNA AAIVRKSAVT
     PSSDPYNSPP PSIPLLGSQT NLQLAPSFAA PQAHPLPSHL SQSNVPPQLS HSSVPSPAPP
     RSVSQPTYFS QPMPQFSSSF VPGTSSIVPT LHPASAQEDF NLQHSLFFKL KLKFLPPHKL
     PWIPSLDVSS FSLPPIDYYL NGPYDNVEAK SALMNIYSSH CITLIESVRY MHLKQFLSEI
     SNFPNSLSPS LLALLSSPYF TKWIERSDTV MYREILKLLF PMTLQVVPPP VLVLLRHLAE
     NLVNHISSIY ASHSSCLLQV KSETAAIFSN LLSRLLRVND TAHAAARFLA NPADRHLICN
     DWERFVSTRF IVHRELMCND KEAVAALDEW YSILSTCSNP SELLDPLKDK HEASDTSMNR
     VELRQIDGVL DRMADFFLEL PSRFPSCSPR MFLLCLGALQ TSVLREITVS GGEAFGALWV
     IRCWVDEYMT WVAEIGGYLD DSYDELEQHH ANFHNKAGIS QSNIPPHLQE HRQSQQHFQQ
     DIEALQSQQQ QQATKNSLME AAYQNAQKQK EDDYISIVFD TNGACS