ID   FFT1_SCHPO              Reviewed;         944 AA.
AC   P87114;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=ATP-dependent helicase fft1;
DE            EC=3.6.4.12;
DE   AltName: Full=Fun thirty-related protein 1;
GN   Name=fft1; ORFNames=SPAC20G8.08c;
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   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: DNA helicase that possesses intrinsic ATP-dependent
CC       nucleosome-remodeling activity and is required for heterochromatin
CC       organization. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB08602.1; -; Genomic_DNA.
DR   PIR; T38130; T38130.
DR   RefSeq; NP_593325.1; NM_001018756.2.
DR   AlphaFoldDB; P87114; -.
DR   SMR; P87114; -.
DR   BioGRID; 278468; 6.
DR   STRING; 4896.SPAC20G8.08c.1; -.
DR   MaxQB; P87114; -.
DR   PaxDb; P87114; -.
DR   EnsemblFungi; SPAC20G8.08c.1; SPAC20G8.08c.1:pep; SPAC20G8.08c.
DR   GeneID; 2541983; -.
DR   KEGG; spo:SPAC20G8.08c; -.
DR   PomBase; SPAC20G8.08c; fft1.
DR   VEuPathDB; FungiDB:SPAC20G8.08c; -.
DR   eggNOG; KOG0389; Eukaryota.
DR   HOGENOM; CLU_000315_16_3_1; -.
DR   InParanoid; P87114; -.
DR   OMA; DCSFNPF; -.
DR   PhylomeDB; P87114; -.
DR   PRO; PR:P87114; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; NAS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA: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; ISS:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:PomBase.
DR   GO; GO:0031507; P:heterochromatin assembly; ISO: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   3: Inferred from homology;
KW   ATP-binding; Chromatin regulator; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..944
FT                   /note="ATP-dependent helicase fft1"
FT                   /id="PRO_0000310747"
FT   DOMAIN          426..592
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          766..923
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          89..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           543..546
FT                   /note="DEGH box"
FT   COMPBIAS        89..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         439..446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   944 AA;  108252 MW;  23A17A57C31F5E83 CRC64;
     MKRKDNKELI CIPSSSPPST PIREENYYLL TSSPIECSPI QQLDLSGSFK NYSTTSSRAN
     GKKFGQLAMQ SRIFFDTTDH KKYVESSYAA YDPHDQPPER DVSLKESSNK INPSNFFDSE
     QITKINAVKK RFPALDSEMI IATLEKFNWR ENITIHKLTF QKLLGRGNST INKSAQKLNN
     QPIEKSSVDK ENAKRKRYVE EGTKQGQKKK PLRVIELSDE ETNEDDLLGQ SPTACTTDAN
     IDNSIPENSD KIEEVSIESS GPSEVEDEMS EYDVRVLNFL NESTLQEIVE VSGCESKVVE
     YFISKRPFPS LEKAEALCQR NAHAATGKRK KSDGRNVGRK LVNSTYEVLQ GFDAVDSLIA
     KCERYGAMIS NTMRSWHNLF DDKKMEQFLN TSTGSISYEY NSQQPSSIAS GITLKSYQIV
     GLNWLCLMYK AKLSGILADE MGLGKTCQVI SFLASLKEKG IQNRHLVVVP SSTLGNWLRE
     FEKFCPSLRV ESYSGTQSER INKRYYLMDT DFDVLVTTYQ LASGSRDDRS FLRKQRFDIS
     IFDEGHYLKN RMSERYKHLM NIPANFRLLI TGTPLQNNLK ELISLLAFML PKVFDNNMQG
     LDIIYKIKTT SDGDIERAYL SQERISRAKT IMNPFILRRR KENVLSDLPP KIQHVEYCHM
     EETQLSLYLS VLELKNLVNA NRENILMQLR KAALHQLLFR SQYNLETLSL MSKRILREDA
     YLDANPQYIF EDMEVMSDFE LHKLADQYRH LHPFALKGKP WMDSAKVKKL CSLLKKSRPN
     ERILIFSQFT QVLDILEYVL NTLDLEFLRL DGSTPVETRQ QLIDDFHTNE NYKVFLLSTK
     SGGFGINLTC ANIVILFDCS FNPFDDMQAE DRAHRVGQTR PVHVYRLITK NTIEENIRRL
     ANTKLTLESS LTTDSEKIQK EISGELMKSL QMDGRVDTMD GSVV