RTF_SCHPO
ID RTF_SCHPO Reviewed; 466 AA.
AC Q9UUI6; Q5NJL6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Replication termination factor 1;
GN Name=rtf1; ORFNames=SPAC22F8.07c;
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], FUNCTION, DNA-BINDING, AND MUTAGENESIS OF
RP LEU-129; PRO-136; SER-154; LEU-162; GLY-183; ARG-293; SER-340 AND MET-343.
RX PubMed=18723894; DOI=10.1534/genetics.108.089243;
RA Eydmann T., Sommariva E., Inagawa T., Mian S., Klar A.J.S., Dalgaard J.Z.;
RT "Rtf1-mediated eukaryotic site-specific replication termination.";
RL Genetics 180:27-39(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 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).
CC -!- FUNCTION: Mediates site-specific replication termination at the polar
CC replication barrier RTS1, a barrier which ensures that replication of
CC the mat1 locus in S.pombe occurs in the centromere-proximal direction.
CC {ECO:0000269|PubMed:18723894}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: DNA-binding domain 1 interacts with the repeated motifs encoded
CC by the RTS1 element as well as the elements enhancer region. DNA-
CC binding domain 2 has only a weak DNA binding activity.
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DR EMBL; AJ627891; CAF31329.1; -; mRNA.
DR EMBL; CU329670; CAB52717.2; -; Genomic_DNA.
DR PIR; T38197; T38197.
DR RefSeq; NP_594730.2; NM_001020158.3.
DR AlphaFoldDB; Q9UUI6; -.
DR SMR; Q9UUI6; -.
DR BioGRID; 278045; 36.
DR STRING; 4896.SPAC22F8.07c.1; -.
DR PaxDb; Q9UUI6; -.
DR EnsemblFungi; SPAC22F8.07c.1; SPAC22F8.07c.1:pep; SPAC22F8.07c.
DR GeneID; 2541545; -.
DR KEGG; spo:SPAC22F8.07c; -.
DR PomBase; SPAC22F8.07c; rtf1.
DR VEuPathDB; FungiDB:SPAC22F8.07c; -.
DR eggNOG; KOG0051; Eukaryota.
DR HOGENOM; CLU_598729_0_0_1; -.
DR InParanoid; Q9UUI6; -.
DR OMA; HWRDYIQ; -.
DR PhylomeDB; Q9UUI6; -.
DR PRO; PR:Q9UUI6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990943; F:mating type region replication fork barrier binding; IDA:PomBase.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0071171; P:site-specific DNA replication termination at RTS1 barrier; IMP:PomBase.
DR CDD; cd00167; SANT; 1.
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; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA replication inhibitor; DNA-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..466
FT /note="Replication termination factor 1"
FT /id="PRO_0000372310"
FT DOMAIN 251..304
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 305..363
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 278..300
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 336..359
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 94..249
FT /note="DNA-binding domain 1"
FT REGION 250..421
FT /note="DNA-binding domain 2"
FT MUTAGEN 129
FT /note="L->F: Abolishes barrier activity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 136
FT /note="P->L: Abolishes wild-type barrier activity and
FT induces a faint new barrier signal of inversed polarity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 154
FT /note="S->L: Abolishes wild-type barrier activity and
FT induces a new barrier signal of inversed polarity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 162
FT /note="L->Y: Abolishes wild-type barrier activity and
FT partially induces a new barrier signal of inversed
FT polarity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 183
FT /note="G->E: Abolishes barrier activity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 293
FT /note="R->K: Strongly reduces barrier activity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 340
FT /note="S->F: Strongly reduces barrier activity."
FT /evidence="ECO:0000269|PubMed:18723894"
FT MUTAGEN 343
FT /note="M->R: Strongly reduces barrier activity."
FT /evidence="ECO:0000269|PubMed:18723894"
SQ SEQUENCE 466 AA; 55219 MW; F3B923077788CAB3 CRC64;
MQGKNNLSCR PDTEDNEELF VDDQLLSPIG DSKNTSSFIY LGNPISFHEY NYDETMVSPE
NVKTAIAGSA KDHETCRGFK KTGTTSYKDF VFSRDYTNWT PTFWVLLSQL IDEFLKESEL
NFVAARDLLI KTKRLPKPFN NLLIQFQIQV PNVSRRTVYR HLKGYFNIPG YERFQYVKKA
SSGSWGANDI ITLEKEIAMF KKKKNWSDEQ FLQYVWSDNH RDEMKTLYNC LYELIDRDKK
SIYNYLRRKY NPFKKKCKWT IEDEAELKKL VEKHGTSWSL IGKLSNRLPM HCRDHWRDYI
QPGEINRSPW TIQEKEKLIK TVNQYLQSNP SSPIQWSLIS KNMRNRHRHH CRWKYYTLIS
RDIHNSSPFK LGDSIWLIER MMDLNVAEER MIDWKCLSEY ANHLWTADAC KSHFERIKKT
LFIDGLSTFS DTLIHLHKML NSSPEETYIS NLHDSYTAFS NADDLC
