REB1_SCHPO
ID REB1_SCHPO Reviewed; 504 AA.
AC Q9P6H9; O94422;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=DNA-binding protein reb1;
GN Name=reb1; ORFNames=SPBC1198.11c, SPBC660.01c;
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 FUNCTION.
RX PubMed=9016645; DOI=10.1093/nar/25.4.904;
RA Zhao A., Guo A., Liu Z., Pape L.;
RT "Molecular cloning and analysis of Schizosaccharomyces pombe Reb1p:
RT sequence-specific recognition of two sites in the far upstream rDNA
RT intergenic spacer.";
RL Nucleic Acids Res. 25:904-910(1997).
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).
CC -!- FUNCTION: DNA-binding protein that recognizes sites within both the
CC enhancer and the promoter of rRNA transcription, as well as upstream of
CC many genes transcribed by RNA polymerase II. Has a role in the
CC termination of RNA polymerase I catalyzed transcription.
CC {ECO:0000269|PubMed:9016645}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
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DR EMBL; U33010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329671; CAB91186.1; -; Genomic_DNA.
DR PIR; T40613; T40613.
DR RefSeq; NP_595080.1; NM_001020986.2.
DR PDB; 5EYB; X-ray; 2.70 A; A/B=146-504.
DR PDBsum; 5EYB; -.
DR AlphaFoldDB; Q9P6H9; -.
DR SMR; Q9P6H9; -.
DR BioGRID; 276474; 222.
DR IntAct; Q9P6H9; 1.
DR STRING; 4896.SPBC1198.11c.1; -.
DR iPTMnet; Q9P6H9; -.
DR MaxQB; Q9P6H9; -.
DR PaxDb; Q9P6H9; -.
DR PRIDE; Q9P6H9; -.
DR EnsemblFungi; SPBC1198.11c.1; SPBC1198.11c.1:pep; SPBC1198.11c.
DR PomBase; SPBC1198.11c; reb1.
DR VEuPathDB; FungiDB:SPBC1198.11c; -.
DR eggNOG; KOG0051; Eukaryota.
DR HOGENOM; CLU_538797_0_0_1; -.
DR InParanoid; Q9P6H9; -.
DR OMA; MARMPND; -.
DR PhylomeDB; Q9P6H9; -.
DR PRO; PR:Q9P6H9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0033553; C:rDNA heterochromatin; EXP:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0043110; F:rDNA spacer replication fork barrier binding; IMP:PomBase.
DR GO; GO:0110035; F:rDNA spacer replication fork barrier binding, bending; IDA:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0071946; P:cis-acting DNA replication termination; IDA:PomBase.
DR GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IMP:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0043111; P:replication fork arrest; IMP:PomBase.
DR GO; GO:0031582; P:replication fork arrest at rDNA repeats; IMP:PomBase.
DR GO; GO:0071807; P:replication fork arrest involved in DNA replication termination; IMP:PomBase.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:PomBase.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..504
FT /note="DNA-binding protein reb1"
FT /id="PRO_0000197088"
FT DOMAIN 308..361
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 362..422
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 335..357
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 395..418
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 30..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 158..174
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:5EYB"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5EYB"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:5EYB"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:5EYB"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 426..441
FT /evidence="ECO:0007829|PDB:5EYB"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:5EYB"
FT HELIX 484..498
FT /evidence="ECO:0007829|PDB:5EYB"
SQ SEQUENCE 504 AA; 58448 MW; 667C45F453E4F916 CRC64;
MDTSVLNPEL QIHGFIGVDS LQSSRKRKND FDDFPLNKGL KTNNNDYSGS IEPKFSPALS
IKEDGKNDRN FEALMSLQAQ DSNLSEQNTS IHLDALASSS IALGNDNVDS SAFLSKVNKG
VNAMRNSTSN QTNDSILISP SEITNMDPFL KGSARWTAEH WDYLERRMQN FCQTYSLDHT
QVADSLHEKR LHGPLSSLVK LLVQEMPSFT RRTILRHLRA LYNIPGYEKY SRKNSSGRGD
FGVQETAIIS QEVHNFIMDQ GWSEYQFCNQ IWAGKCPKTI RMFYSNLYKK LSHRDAKSIY
HHVRRAYNPF EDRCVWSKEE DEELRKNVVE HGKCWTKIGR KMARMPNDCR DRWRDVVRFG
DKLKRNAWSL EEETQLLQIV AELRNREDLS SDINWTLVAQ MLGTRTRLQC RYKFQQLTKA
ASKFELQENV WLLERIYDSL LNNGGKIHWE NIVKEANGRW TRDQMLFQFI NLKKMIPSYD
NLPLLEATKS AIDDFKVVLS GFSN
