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 27-MAR-2024, entry version 173.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 284812.P41412; -.
DR MaxQB; P41412; -.
DR PaxDb; 4896-SPAC22F3-09c-1; -.
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; IHHAAIM; -.
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: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; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR43828; ASPARAGINASE; 1.
DR PANTHER; PTHR43828:SF17; CELL DIVISION CYCLE-RELATED PROTEIN RES2_PCT1; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 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
//
