FFT3_SCHPO
ID FFT3_SCHPO Reviewed; 922 AA.
AC O42861; Q9US92;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ATP-dependent helicase fft3;
DE EC=3.6.4.12;
DE AltName: Full=Fun thirty-related protein 3;
GN Name=fft3; Synonyms=snf2SR; ORFNames=SPAC25A8.01c;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 51-226, 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 [3]
RP FUNCTION.
RX PubMed=15317843; DOI=10.1091/mbc.e04-01-0067;
RA Kusano A., Yoshioka T., Nishijima H., Nishitani H., Nishimoto T.;
RT "Schizosaccharomyces pombe RanGAP homolog, SpRna1, is required for
RT centromeric silencing and chromosome segregation.";
RL Mol. Biol. Cell 15:4960-4970(2004).
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, FUNCTION, AND INTERACTION WITH SPI1.
RX PubMed=18422602; DOI=10.1111/j.1365-2443.2008.01190.x;
RA Ohba T., Nishijima H., Nishitani H., Nishimoto T.;
RT "Schizosaccharomyces pombe Snf2SR, a novel SNF2 family protein, interacts
RT with Ran GTPase and modulates both RanGEF and RanGAP activities.";
RL Genes Cells 13:571-582(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-219 AND SER-617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [7]
RP FUNCTION.
RX PubMed=21437270; DOI=10.1371/journal.pgen.1001334;
RA Stralfors A., Walfridsson J., Bhuiyan H., Ekwall K.;
RT "The FUN30 chromatin remodeler, Fft3, protects centromeric and subtelomeric
RT domains from euchromatin formation.";
RL PLoS Genet. 7:E1001334-E1001334(2011).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is required for heterochromatin
CC organization. Required for maintaining a heterochromatin chromatin
CC structure at centromeres and subtelomeres by protecting these regions
CC from euchromatin assembly. Enhances the nucleotide exchange activity of
CC the pim1 guanine nucleotide exchange factor and abolishes histone-H3-
CC mediated RanGAP inhibition. Involved in the construction of the
CC centromeres. {ECO:0000269|PubMed:15317843, ECO:0000269|PubMed:18422602,
CC ECO:0000269|PubMed:21437270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: interacts with the GDP-bound form of spi1.
CC {ECO:0000269|PubMed:18422602}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; CU329670; CAA16951.1; -; Genomic_DNA.
DR EMBL; AB027947; BAA87251.1; -; Genomic_DNA.
DR PIR; T38371; T38371.
DR RefSeq; NP_593617.1; NM_001019048.2.
DR AlphaFoldDB; O42861; -.
DR SMR; O42861; -.
DR BioGRID; 278031; 1191.
DR STRING; 4896.SPAC25A8.01c.1; -.
DR iPTMnet; O42861; -.
DR MaxQB; O42861; -.
DR PaxDb; O42861; -.
DR PRIDE; O42861; -.
DR EnsemblFungi; SPAC25A8.01c.1; SPAC25A8.01c.1:pep; SPAC25A8.01c.
DR GeneID; 2541531; -.
DR KEGG; spo:SPAC25A8.01c; -.
DR PomBase; SPAC25A8.01c; fft3.
DR VEuPathDB; FungiDB:SPAC25A8.01c; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; O42861; -.
DR OMA; LDILCVC; -.
DR PhylomeDB; O42861; -.
DR PRO; PR:O42861; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; EXP:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0140698; P:attachment of telomeric heterochromatin to nuclear envelope; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IMP:PomBase.
DR GO; GO:0106253; P:positive regulation of DNA strand resection involved in replication fork processing; EXP:PomBase.
DR GO; GO:1905099; P:positive regulation of guanyl-nucleotide exchange factor activity; IDA:PomBase.
DR GO; GO:0031297; P:replication fork processing; EXP:PomBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..922
FT /note="ATP-dependent helicase fft3"
FT /id="PRO_0000074383"
FT DOMAIN 399..567
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 765..922
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 139..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 518..521
FT /note="DEGH box"
FT COMPBIAS 154..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 412..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 922 AA; 104504 MW; 9C268E6FD220CA5A CRC64;
MDGKRKIEHT ADGTHYDATS NVKRKPIFPP FIADSLSEAT EKANVMGGGM NSRLQILSEM
SKRVQATAPI SSLEHFKQLS DISPSFTSSA NSINQPYNYS GSLENLVPTP SAGTPSQFMD
AQNPYGAVYN ALSQFSETEP KMPSYMDDEE ASDSLPLSLS SQSLSSQVTN QKPAPHRLTM
RERYAANNLT NGLQFTLPLS SRKTYEPEAD DDSNDDMYSD DDSNADRWAS RIDTAALKEE
VLKYMNRCST QDLADMTGCT LAEAEFMVAK RPFPDLESAL VVKQPRPVIP KGRRGRREKT
PLGPRLVGIC MEIMRGYFVV DALIRQCEQL GGKIQRGIEA WGLSNTATSD EGETSLVNFD
QMKSFGTPAN SSFITTPPAS FSPDIKLQDY QIIGINWLYL LYELKLAGIL ADEMGLGKTC
QTIAFFSLLM DKNINGPHLV IAPASTMENW LREFAKFCPK LKIELYYGSQ VEREEIRERI
NSNKDSYNVM LTTYRLAATS KADRLFLRNQ KFNVCVYDEG HYLKNRASER YRHLMSIPAD
FRVLLTGTPL QNNLKELISL LAFILPHVFD YGLKSLDVIF TMKKSPESDF ERALLSEQRV
SRAKMMMAPF VLRRKKSQVL DALPKKTRII EFCEFSEEER RRYDDFASKQ SVNSLLDENV
MKTNLDTNAN LAKKKSTAGF VLVQLRKLAD HPMLFRIHYK DDILRQMAKA IMNEPQYKKA
NELYIFEDMQ YMSDIELHNL CCKFPSINSF QLKDEPWMDA TKVRKLKKLL TNAVENGDRV
VLFSQFTQVL DILQLVMKSL NLKFLRFDGS TQVDFRQDLI DQFYADESIN VFLLSTKAGG
FGINLACANM VILYDVSFNP FDDLQAEDRA HRVGQKKEVT VYKFVVKDTI EEHIQRLANA
KIALDATLSG NAETVEAEDD DD
