TRF1_SCHPO
ID TRF1_SCHPO Reviewed; 485 AA.
AC Q6E434; O42961; Q9US79;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Telomeric DNA-binding factor trf1;
GN Name=trf1; ORFNames=SPBC19G7.13;
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 [MRNA], PROTEIN SEQUENCE OF 76-83 AND 407-414, SUBUNIT,
RP AND DNA-BINDING.
RX PubMed=17977837; DOI=10.1074/jbc.m708784200;
RA Pitt C.W., Valente L.P., Rhodes D., Simonsson T.;
RT "Identification and characterization of an essential telomeric repeat
RT binding factor in fission yeast.";
RL J. Biol. Chem. 283:2693-2701(2008).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 190-384, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19074598; DOI=10.1128/ec.00174-08;
RA Cockell M.M., Lo Presti L., Cerutti L., Cano Del Rosario E., Hauser P.M.,
RA Simanis V.;
RT "Functional differentiation of tbf1 orthologues in fission and budding
RT yeasts.";
RL Eukaryot. Cell 8:207-216(2009).
CC -!- FUNCTION: Binds the telomeric double-stranded TTACAGG repeat and
CC regulates telomere length.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17977837}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:19074598}. Note=Enriched throughout the euchromatic
CC hemisphere.
CC -!- DISRUPTION PHENOTYPE: Cells arrest in interphase and have an aberrant
CC chromatin structure. {ECO:0000269|PubMed:19074598}.
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DR EMBL; AY584065; AAT51726.1; -; mRNA.
DR EMBL; CU329671; CAA17067.1; -; Genomic_DNA.
DR EMBL; AB027990; BAA87294.1; -; Genomic_DNA.
DR PIR; T39844; T39844.
DR RefSeq; NP_595979.1; NM_001021886.2.
DR PDB; 6K5S; X-ray; 1.90 A; A/B/C/D=98-319.
DR PDB; 6K5U; X-ray; 2.08 A; A/B=407-485.
DR PDBsum; 6K5S; -.
DR PDBsum; 6K5U; -.
DR AlphaFoldDB; Q6E434; -.
DR SMR; Q6E434; -.
DR BioGRID; 277255; 18.
DR STRING; 4896.SPBC19G7.13.1; -.
DR MaxQB; Q6E434; -.
DR PaxDb; Q6E434; -.
DR EnsemblFungi; SPBC19G7.13.1; SPBC19G7.13.1:pep; SPBC19G7.13.
DR GeneID; 2540732; -.
DR KEGG; spo:SPBC19G7.13; -.
DR PomBase; SPBC19G7.13; -.
DR VEuPathDB; FungiDB:SPBC19G7.13; -.
DR eggNOG; ENOG502QRT9; Eukaryota.
DR HOGENOM; CLU_008791_4_0_1; -.
DR InParanoid; Q6E434; -.
DR OMA; EIACYIH; -.
DR PhylomeDB; Q6E434; -.
DR PRO; PR:Q6E434; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:PomBase.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IBA:GO_Central.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF08558; TRF; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..485
FT /note="Telomeric DNA-binding factor trf1"
FT /id="PRO_0000290649"
FT DOMAIN 400..457
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 428..453
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 133..152
FT /evidence="ECO:0007829|PDB:6K5S"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 168..186
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 214..233
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:6K5S"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:6K5U"
FT HELIX 428..435
FT /evidence="ECO:0007829|PDB:6K5U"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:6K5U"
FT HELIX 450..466
FT /evidence="ECO:0007829|PDB:6K5U"
FT HELIX 473..477
FT /evidence="ECO:0007829|PDB:6K5U"
SQ SEQUENCE 485 AA; 54604 MW; DF3DA46B4BB2C4A5 CRC64;
MSKRSLDPSD DFKGQKRLAI DPESTALEQD RQMLQQLSEQ NSELEPQNVA PNAEIPLGFD
LSGIQFNMTP DFYLRMNQGM DYAFNQPNPI ATPQQLLRTS LIPTLGNLSN IILSILGKPV
QEASAIVTNP ASEMGMAFTK VMNMFRMVKD IYTEESFIYS SAIGMRTPSQ RSTTRRANLA
IFLAAVYGAL QIGFFHLNEN FLEVFAPDES NILTNQGTLY MELKTQAYIS AMAQAERPKG
DILNDLFPSD MAHRFLIRRN AKLDDKLTYV EKQIIEKCTA RKERLANFSP QEALNEVYPW
GKFLSEIACY IHNNYSSISA IPIPANSFKR RSKKNGLRFK AGEAESSPSE SGSDLTDSLA
FGIPSSTFDG SSETQNVSSV VLYDQVRHMT NNNLNNKRTR RVANRRSWTK EEEEALLDGL
DLVKGPRWSQ ILELYGPGGK KSEVLKYRNQ VQLKDKARNM KLFFLKSGQV VPAALQCVTG
DLRRD
