ID   RES2_SCHPO              Reviewed;         657 AA.
AC   P41412; Q02300;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 165.
DE   RecName: Full=Cell division cycle-related protein res2/pct1;
GN   Name=res2; Synonyms=pct1; ORFNames=SPAC22F3.09c;
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].
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=8168485; DOI=10.1002/j.1460-2075.1994.tb06456.x;
RA   Miyamoto M., Tanaka K., Okayama H.;
RT   "res2+, a new member of the cdc10+/SWI4 family, controls the 'start' of
RT   mitotic and meiotic cycles in fission yeast.";
RL   EMBO J. 13:1873-1880(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7926774; DOI=10.1101/gad.8.8.885;
RA   Zhu Y., Takeda T., Nasmyth K., Jones N.;
RT   "pct1+, which encodes a new DNA-binding partner of p85cdc10, is required
RT   for meiosis in the fission yeast Schizosaccharomyces pombe.";
RL   Genes Dev. 8:885-898(1994).
RN   [3]
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   [4]
RP   INTERACTION WITH CDK9.
RX   PubMed=12475973; DOI=10.1074/jbc.m211713200;
RA   Pei Y., Schwer B., Shuman S.;
RT   "Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA
RT   capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality
RT   control.";
RL   J. Biol. Chem. 278:7180-7188(2003).
CC   -!- FUNCTION: Required for the initiation of mitotic and premeiotic DNA
CC       synthesis. Has an additional role in meiotic division.
CC   -!- SUBUNIT: Interacts with cdc10 and cdk9. {ECO:0000269|PubMed:12475973}.
CC   -!- INTERACTION:
CC       P41412; P01129: cdc10; NbExp=3; IntAct=EBI-1149177, EBI-1009350;
CC       P41412; P36630: cig2; NbExp=3; IntAct=EBI-1149177, EBI-1149212;
CC       P41412; O42913: nrm1; NbExp=2; IntAct=EBI-1149177, EBI-15720278;
CC       P41412; P33520: res1; NbExp=2; IntAct=EBI-1149177, EBI-1149288;
CC   -!- INDUCTION: During conjugation and nitrogen starvation.
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DR   EMBL; D17761; BAA04608.1; -; Genomic_DNA.
DR   EMBL; Z32838; CAA83678.1; -; mRNA.
DR   EMBL; S73870; AAB32253.1; -; mRNA.
DR   EMBL; CU329670; CAA91074.1; -; Genomic_DNA.
DR   PIR; A54278; A54278.
DR   RefSeq; NP_593032.1; NM_001018431.2.
DR   AlphaFoldDB; P41412; -.
DR   SMR; P41412; -.
DR   BioGRID; 278361; 200.
DR   DIP; DIP-35569N; -.
DR   IntAct; P41412; 4.
DR   MINT; P41412; -.
DR   STRING; 4896.SPAC22F3.09c.1; -.
DR   MaxQB; P41412; -.
DR   PaxDb; P41412; -.
DR   EnsemblFungi; SPAC22F3.09c.1; SPAC22F3.09c.1:pep; SPAC22F3.09c.
DR   GeneID; 2541871; -.
DR   KEGG; spo:SPAC22F3.09c; -.
DR   PomBase; SPAC22F3.09c; res2.
DR   VEuPathDB; FungiDB:SPAC22F3.09c; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   HOGENOM; CLU_009666_3_1_1; -.
DR   InParanoid; P41412; -.
DR   OMA; MGHIEMI; -.
DR   PhylomeDB; P41412; -.
DR   PRO; PR:P41412; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0030907; C:MBF transcription complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0033309; C:SBF transcription complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; EXP:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:PomBase.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.10.260.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA_N/APSES_HTH.
DR   InterPro; IPR029793; Mbp1/Res1/Res2.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR43828:SF1; PTHR43828:SF1; 2.
DR   Pfam; PF13637; Ank_4; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF54616; SSF54616; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell cycle; DNA-binding; Meiosis; Reference proteome; Repeat.
FT   CHAIN           1..657
FT                   /note="Cell division cycle-related protein res2/pct1"
FT                   /id="PRO_0000067073"
FT   DOMAIN          8..115
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REPEAT          247..276
FT                   /note="ANK 1"
FT   REPEAT          368..397
FT                   /note="ANK 2"
FT   DNA_BIND        39..60
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REGION          113..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..131
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        482
FT                   /note="A -> R (in Ref. 2; CAA83678/AAB32253)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        639..641
FT                   /note="Missing (in Ref. 2; AAB32253)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        657
FT                   /note="K -> DLEK (in Ref. 2; AAB32253)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   657 AA;  73702 MW;  1159312B63E475E4 CRC64;
     MAPRSSAVHV AVYSGVEVYE CFIKGVSVMR RRRDSWLNAT QILKVADFDK PQRTRVLERQ
     VQIGAHEKVQ GGYGKYQGTW VPFQRGVDLA TKYKVDGIMS PILSLDIDEG KAIAPKKKQT
     KQKKPSVRGR RGRKPSSLSS STLHSVNEKQ PNSSISPTIE SSMNKVNLPG AEEQVSATPL
     PASPNALLSP NDNTIKPVEE LGMLEAPLDK YEESLLDFFL HPEEGRIPSF LYSPPPDFQV
     NSVIDDDGHT SLHWACSMGH IEMIKLLLRA NADIGVCNRL SQTPLMRSVI FTNNYDCQTF
     GQVLELLQST IYAVDTNGQS IFHHIVQSTS TPSKVAAAKY YLDCILEKLI SIQPFENVVR
     LVNLQDSNGD TSLLIAARNG AMDCVNSLLS YNANPSIPNR QRRTASEYLL EADKKPHSLL
     QSNSNASHSA FSFSGISPAI ISPSCSSHAF VKAIPSISSK FSQLAEEYES QLREKEEDLI
     RANRLKQDTL NEISRTYQEL TFLQKNNPTY SQSMENLIRE AQETYQQLSK RLLIWLEARQ
     IFDLERSLKP HTSLSISFPS DFLKKEDGLS LNNDFKKPAC NNVTNSDEYE QLINKLTSLQ
     ASRKKDTLYI RKLYEELGID DTVNSYRRLI AMSCGINPED LSLEILDAVE EALTREK