FFT2_SCHPO
ID FFT2_SCHPO Reviewed; 1284 AA.
AC O74842;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ATP-dependent helicase fft2;
DE EC=3.6.4.12;
DE AltName: Full=Fun thirty-related protein 2;
GN Name=fft2; ORFNames=SPCC1235.05c;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-383, 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).
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: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21109.1; -; Genomic_DNA.
DR PIR; T40879; T40879.
DR RefSeq; NP_587731.1; NM_001022726.2.
DR AlphaFoldDB; O74842; -.
DR SMR; O74842; -.
DR BioGRID; 275618; 31.
DR STRING; 4896.SPCC1235.05c.1; -.
DR iPTMnet; O74842; -.
DR MaxQB; O74842; -.
DR PaxDb; O74842; -.
DR PRIDE; O74842; -.
DR EnsemblFungi; SPCC1235.05c.1; SPCC1235.05c.1:pep; SPCC1235.05c.
DR GeneID; 2539045; -.
DR KEGG; spo:SPCC1235.05c; -.
DR PomBase; SPCC1235.05c; fft2.
DR VEuPathDB; FungiDB:SPCC1235.05c; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_5_1; -.
DR InParanoid; O74842; -.
DR OMA; CMETMEG; -.
DR PhylomeDB; O74842; -.
DR PRO; PR:O74842; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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: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 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Cytoplasm; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1284
FT /note="ATP-dependent helicase fft2"
FT /id="PRO_0000310748"
FT DOMAIN 562..730
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 928..1079
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 681..684
FT /note="DEGH box"
FT COMPBIAS 22..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 575..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1284 AA; 143667 MW; 018E16C67B4C3759 CRC64;
MLPYNSNYLS DNGKRKFSDE NPQSEVYGSS QTGLPSSYGN PQSYGTPPVQ QSSAMYGVNN
SMGGGMYNTS ENTQFMNTDY SQTSSYASTP MSNAYSRDAP AAINNNFGYS YVGQSSQPVP
SYNPLPSYNT ASLPNAGIPA AMPGMPSGYP GTVPIPQGGY NAHYSSPYNN GYPIGAVNPT
SAIPAQPPAQ PVNNVLPSYV RSNSRSSARS TARSAPRSTQ RSRSSSANPV TTPPVNNTLL
TPPAPPVELP PVTTTSPNAI IRSVQWIRSF VPQAPIHQVI NTLAQTKWDE TAALSILSQK
YLSCDLGIPI QEHKRFKQSP VASNMPTYGS SNRTVQSQKR SIRDKYIQMP NDSTQASLMP
SYTRKTSNAS KKLTTEEDEF YDSEEEPEAI VHRDTSALER TVLNFINSST AKELSDTASC
PLSHSKLLLE HRPFQTLAEA CIIKHPDDVP SKPGRRGRRR EKNPMGQKIV NACMETMEGY
YAIDNLIAKC EFLGNRISKG MASWGIKLEM SNGELNIVDM ESVPTEAADN SDFPKFVTEQ
PKTLASDVQL KSYQLVGVNW LHLLYQQKLS GILADEMGLG KTCQVVAFFA LLLEQGHHGP
HLVVVPSSTL ENWLRELARF CPSLRVEPYY GSQQERANIR EAIEENEIKY DILVTTYQLA
TNNKEDRSFL KHQNFDVCVY DEGHYLKNRM SERYKHLMNL NANFRLLLTG TPLQNNLKEL
VSLLAFILPN MFDSDMDDLD VIFKAKPTAD ADIEQALLSK QRISRAKTMM TPFVLRRRKN
QVLNDLPKKT QIIEHCKLSE NQLEIYNRYA ALQKNQQLRR DDKRNKRSKN DEESDGKSLS
AGHVLMQLRK AANHALLFRK FYDDEKLKQM AKDIMQEEQY KNANEQYIYE DMEVMSDFEL
HRLCRSFPTL QSYTLKDDPW MDSGKIRVLK ELLPKMKEEG SRILLFSQFT QMLDILEQVL
DTLKISYVRL DGSTQVEVRQ DIIDQFHKEE DVTVFLLSTK AGGFGINLAC ANVVILYDCS
YNPFDDLQAE DRAHRVGQVR EVTVIRLITD NTIEEYIQKL ANTKLALDMS LSSDGKDREE
IGERLVQDML DEENNGNNTK PEITGNESDG EFKVSSSNNS KQTDAEETNT GVPLEGSQPN
SVEKTDLADG DEKANIKTEM KSETVEGDNK ELRETMKGEN VQTDSNAAVP SSKSSTEEPN
ESVLSGHLDL DTEASPVVST IEKTTKGDVS VTEEQQSANI DGQLEKPEIE ESKKPDVLNQ
VSLSIEEEKP KNKESEVDNN AAKD
