FBH1_SCHPO
ID FBH1_SCHPO Reviewed; 878 AA.
AC Q9USU3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=F-box DNA helicase protein 1;
DE EC=3.6.4.12;
GN Name=fbh1;
GN Synonyms=fdh {ECO:0000312|EMBL:CAC44128.1},
GN fdh1 {ECO:0000312|EMBL:CAC44128.1}; ORFNames=SPBC336.01;
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 [GENOMIC DNA], FUNCTION, COFACTOR, AND INTERACTION WITH
RP SSB1.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9228070; DOI=10.1074/jbc.272.30.18910;
RA Park J.S., Choi E., Lee S.-H., Lee C., Seo Y.-S.;
RT "A DNA helicase from Schizosaccharomyces pombe stimulated by single-
RT stranded DNA-binding protein at low ATP concentration.";
RL J. Biol. Chem. 272:18910-18919(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16135799; DOI=10.1128/mcb.25.18.8074-8083.2005;
RA Morishita T., Furukawa F., Sakaguchi C., Toda T., Carr A.M., Iwasaki H.,
RA Shinagawa H.;
RT "Role of the Schizosaccharomyces pombe F-Box DNA helicase in processing
RT recombination intermediates.";
RL Mol. Cell. Biol. 25:8074-8083(2005).
RN [3]
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 [4]
RP INTERACTION WITH SKP1.
RX PubMed=15147268; DOI=10.1111/j.1356-9597.2004.00730.x;
RA Lehmann A., Katayama S., Harrison C., Dhut S., Kitamura K., McDonald N.,
RA Toda T.;
RT "Molecular interactions of fission yeast Skp1 and its role in the DNA
RT damage checkpoint.";
RL Genes Cells 9:367-382(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-14; PRO-15 AND
RP ASP-485.
RX PubMed=16135800; DOI=10.1128/mcb.25.18.8084-8096.2005;
RA Osman F., Dixon J., Barr A.R., Whitby M.C.;
RT "The F-Box DNA helicase Fbh1 prevents Rhp51-dependent recombination without
RT mediator proteins.";
RL Mol. Cell. Biol. 25:8084-8096(2005).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=19546232; DOI=10.1128/mcb.00471-09;
RA Lorenz A., Osman F., Folkyte V., Sofueva S., Whitby M.C.;
RT "Fbh1 limits Rad51-dependent recombination at blocked replication forks.";
RL Mol. Cell. Biol. 29:4742-4756(2009).
CC -!- FUNCTION: Involved in ATP-dependent DNA-unwinding in a 3' to 5'
CC direction, and ATP-ase activities stimulated by the single-stranded
CC DNA-binding protein ssb1. Essential for viability and normal growth of
CC stationary phase cells and in the absence of either srs2 or rqh1 DNA
CC helicase (PubMed:16135799, PubMed:9228070). Involved in DNA
CC recombination repair of strand breaks and stalled or collapsed
CC replication forks, on the rhp51-dependent pathway: promotes rhp51
CC filament dissolution from stalled forks, thereby inhibiting homologous
CC recombination and preventing excessive recombination (PubMed:16135800,
CC PubMed:19546232). Ubiquitination and DNA helicase activities are
CC essential for controlling rhp51-dependent recombination in the absence
CC of rad22. Plays a role in the processing of toxic recombination
CC intermediates. Promotes proper chromosome segregation (PubMed:16135799,
CC PubMed:16135800, PubMed:9228070, PubMed:19546232).
CC {ECO:0000269|PubMed:16135799, ECO:0000269|PubMed:16135800,
CC ECO:0000269|PubMed:19546232, ECO:0000269|PubMed:9228070}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9228070};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9228070};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the E3 ubiquitin ligase Skp1-Cullin-1-F-box (SCF)
CC complex. Interacts with skp1 and ssb1. {ECO:0000269|PubMed:15147268,
CC ECO:0000269|PubMed:9228070}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Becomes localized at
CC discrete nuclear foci together with rhp51, in response to DNA strand
CC breakage.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255}.
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DR EMBL; AF380117; AAK58077.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC44128.1; -; Genomic_DNA.
DR RefSeq; NP_596121.3; NM_001022039.3.
DR AlphaFoldDB; Q9USU3; -.
DR BioGRID; 276776; 63.
DR IntAct; Q9USU3; 1.
DR STRING; 4896.SPBC336.01.1; -.
DR MaxQB; Q9USU3; -.
DR PaxDb; Q9USU3; -.
DR PRIDE; Q9USU3; -.
DR EnsemblFungi; SPBC336.01.1; SPBC336.01.1:pep; SPBC336.01.
DR GeneID; 2540244; -.
DR KEGG; spo:SPBC336.01; -.
DR PomBase; SPBC336.01; fbh1.
DR VEuPathDB; FungiDB:SPBC336.01; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_329036_0_0_1; -.
DR InParanoid; Q9USU3; -.
DR OMA; LVASHIM; -.
DR PhylomeDB; Q9USU3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9USU3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; IDA:PomBase.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:PomBase.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; IDA:PomBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0006310; P:DNA recombination; IGI:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR GO; GO:0060542; P:regulation of strand invasion; IDA:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:PomBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Magnesium; Manganese; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..878
FT /note="F-box DNA helicase protein 1"
FT /id="PRO_0000271430"
FT DOMAIN 8..56
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT MUTAGEN 14
FT /note="L->A: Modest reduction in DNA helicase activity;
FT when in combination with A-15."
FT /evidence="ECO:0000269|PubMed:16135800"
FT MUTAGEN 15
FT /note="P->A: Modest reduction in DNA helicase activity;
FT when in combination with A-14."
FT /evidence="ECO:0000269|PubMed:16135800"
FT MUTAGEN 485
FT /note="D->N: Prevents DNA helicase activity."
FT /evidence="ECO:0000269|PubMed:16135800"
SQ SEQUENCE 878 AA; 99705 MW; E051D904F8293C15 CRC64;
MSAQHLHSCK FYRLPLEIIP LICRFLSVQD IQSFIRVFPS FQTILDSSND LFWKKKNYEL
RIRRNRLLRG SYAAGVSSSA MNGFVNGTQI SSTPAEREYY SKSDEIKNIC GLPPGPMKVE
QIGHAIDHLV SETHTVDHLG SSIKASFFHI DDVPLEWISS ICMQVQSFFS PAAREAISSL
KSRTTTSNLL LSLFVGILFE DDLWYFFNTL YMLSSTSAIE FAYFLDSIFT VVRTDYEHYR
DPLSQTLITS CTRIHNIVAV IESPYDEPNT KGLTSEQKMI VECQLNPGEV LKVKAFAGTG
KTKALLEFAK SRPKDKILYV AFNKAAKEDA ELRFPFNVKC STMHGLAYGA ILAQADLPQA
KLERQLSNST IASLLSLQVA FPKANRKNNP GTPSASLVAS HIMFTLNRFM HSTDWQLGFR
HISKRSLEVT KLSKEKLLAY TKKLWSLIVN FEYTHAPLIP DAYMKLLHLY EFPNIFSKYD
YILFDEAQDF TPCMVDLIYR QKHARIVIVG DAHQCIYGFR GANACAFNEN LYPSTKQLCL
TKSFRFGNSV AKYANFLLSL KGENVKLKGV QNDHAYWSSA SNPNNVSGAF RFFPHTIIFR
TNKELILQSI RLSVSLPKEI PIAILGSMRK KAFQLLRSGS ELAHGQRPSH PKLKDFSSWG
EFEVHVKNSA EEDAELALVY DMADELFSES FLSRLDNCEK RLMDSKDDGD NGIILATAHQ
SKGLEWDNVQ LGNDFRPKFD SVSFSRIGSS RYLQEEINIL YVALTRAKKR LILNDTITKL
YALECGLVRF AGGILTEDQL QPGKVALFVD WQIDKFSFFY ETPAEGYNLL VEANEKSVWD
IFFGVLSGAW QNYIANTSER LKRSMLFIEN QLFAVHDQ
