GenomeNet

Database: UniProt
Entry: Q9UT23
LinkDB: Q9UT23
Original site: Q9UT23 
ID   MPH1_SCHPO              Reviewed;         834 AA.
AC   Q9UT23;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   18-SEP-2019, entry version 128.
DE   RecName: Full=ATP-dependent DNA helicase fml1 {ECO:0000305};
DE            EC=3.6.4.12 {ECO:0000269|PubMed:22844101};
DE   AltName: Full=FANCM-like protein 1 {ECO:0000303|PubMed:18851838};
GN   Name=fml1 {ECO:0000303|PubMed:18851838};
GN   ORFNames=SPAC9.05 {ECO:0000312|PomBase:SPAC9.05};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18851838; DOI=10.1016/j.molcel.2008.08.024;
RA   Sun W., Nandi S., Osman F., Ahn J.S., Jakovleska J., Lorenz A.,
RA   Whitby M.C.;
RT   "The FANCM ortholog Fml1 promotes recombination at stalled replication
RT   forks and limits crossing over during DNA double-strand break
RT   repair.";
RL   Mol. Cell 32:118-128(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=20347428; DOI=10.1016/j.molcel.2010.01.039;
RA   Yan Z., Delannoy M., Ling C., Daee D., Osman F., Muniandy P.A.,
RA   Shen X., Oostra A.B., Du H., Steltenpool J., Lin T., Schuster B.,
RA   Decaillet C., Stasiak A., Stasiak A.Z., Stone S., Hoatlin M.E.,
RA   Schindler D., Woodcock C.L., Joenje H., Sen R., de Winter J.P., Li L.,
RA   Seidman M.M., Whitby M.C., Myung K., Constantinousend A., Wang W.;
RT   "A histone-fold complex and FANCM form a conserved DNA-remodeling
RT   complex to maintain genome stability.";
RL   Mol. Cell 37:865-878(2010).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-99 AND ASP-196.
RX   PubMed=22844101; DOI=10.1093/nar/gks715;
RA   Nandi S., Whitby M.C.;
RT   "The ATPase activity of Fml1 is essential for its roles in homologous
RT   recombination and DNA repair.";
RL   Nucleic Acids Res. 40:9584-9595(2012).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF LYS-99 AND ASP-196.
RX   PubMed=22723423; DOI=10.1126/science.1220111;
RA   Lorenz A., Osman F., Sun W., Nandi S., Steinacher R., Whitby M.C.;
RT   "The fission yeast FANCM ortholog directs non-crossover recombination
RT   during meiosis.";
RL   Science 336:1585-1588(2012).
RN   [7]
RP   FUNCTION, INTERACTION WITH MHF1-MHF2, AND MUTAGENESIS OF TYR-672;
RP   ARG-674 AND ARG-678.
RX   PubMed=24026537; DOI=10.1098/rsob.130102;
RA   Bhattacharjee S., Osman F., Feeney L., Lorenz A., Bryer C.,
RA   Whitby M.C.;
RT   "MHF1-2/CENP-S-X performs distinct roles in centromere metabolism and
RT   genetic recombination.";
RL   Open Biol. 3:130102-130102(2013).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair
CC       by homologous recombination and in genome maintenance. Capable of
CC       unwinding D-loops (PubMed:18851838, PubMed:22844101,
CC       PubMed:22723423). Plays a role in limiting crossover
CC       recombinantion during mitotic DNA double-strand break (DSB) repair
CC       (PubMed:18851838). Component of a FANCM-MHF complex which promotes
CC       gene conversion at blocked replication forks, probably by reversal
CC       of the stalled fork (PubMed:18851838, PubMed:20347428,
CC       PubMed:24026537). FANCM-MHF also promotes non-crossover
CC       recombination in meiotic cells (PubMed:22723423, PubMed:24026537).
CC       {ECO:0000269|PubMed:18851838, ECO:0000269|PubMed:20347428,
CC       ECO:0000269|PubMed:22723423, ECO:0000269|PubMed:22844101,
CC       ECO:0000269|PubMed:24026537}.
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         Evidence={ECO:0000269|PubMed:22844101};
CC   -!- SUBUNIT: Interacts with the MHF histone-fold complex composed of
CC       mhf1 and mhf2 to forms the FANCM-MHF complex.
CC       {ECO:0000269|PubMed:24026537}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitive to the alkylating agent
CC       methyl methanesulfonate (MMS) and the cross-linking agent
CC       cisplatin. {ECO:0000269|PubMed:18851838}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. FANCM sub-subfamily. {ECO:0000305}.
DR   EMBL; CU329670; CAB57423.2; -; Genomic_DNA.
DR   PIR; T39190; T39190.
DR   RefSeq; NP_593348.2; NM_001018780.3.
DR   SMR; Q9UT23; -.
DR   BioGrid; 280082; 51.
DR   STRING; 4896.SPAC9.05.1; -.
DR   iPTMnet; Q9UT23; -.
DR   SwissPalm; Q9UT23; -.
DR   MaxQB; Q9UT23; -.
DR   PaxDb; Q9UT23; -.
DR   PRIDE; Q9UT23; -.
DR   EnsemblFungi; SPAC9.05.1; SPAC9.05.1:pep; SPAC9.05.
DR   GeneID; 2543668; -.
DR   KEGG; spo:SPAC9.05; -.
DR   EuPathDB; FungiDB:SPAC9.05; -.
DR   PomBase; SPAC9.05; fml1.
DR   HOGENOM; HOG000076770; -.
DR   InParanoid; Q9UT23; -.
DR   KO; K14635; -.
DR   OMA; HRAVGNY; -.
DR   PhylomeDB; Q9UT23; -.
DR   PRO; PR:Q9UT23; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0071821; C:FANCM-MHF complex; ISS:PomBase.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000400; F:four-way junction DNA binding; IDA:PomBase.
DR   GO; GO:0009378; F:four-way junction helicase activity; IDA:PomBase.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:PomBase.
DR   GO; GO:0036297; P:interstrand cross-link repair; IMP:PomBase.
DR   GO; GO:1902346; P:meiotic strand displacement involved in double-strand break repair via SDSA; IDA:PomBase.
DR   GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:PomBase.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; ISO:PomBase.
DR   GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR   GO; GO:0071932; P:replication fork reversal; IDA:PomBase.
DR   GO; GO:0000732; P:strand displacement; IDA:PomBase.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR039686; FANCM/Mph1-like.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR14025:SF20; PTHR14025:SF20; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN         1    834       ATP-dependent DNA helicase fml1.
FT                                /FTId=PRO_0000310751.
FT   DOMAIN       80    248       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      416    582       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      93    100       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      650    690       Interaction with MHF complex.
FT                                {ECO:0000269|PubMed:24026537}.
FT   MOTIF       196    199       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MUTAGEN      99     99       K->R: Retains DNA-binding activity but is
FT                                unable to unwind D loops or dissociate
FT                                synthetic HJs.
FT                                {ECO:0000269|PubMed:22723423,
FT                                ECO:0000269|PubMed:22844101}.
FT   MUTAGEN     196    196       D->N: Retains DNA-binding activity but is
FT                                unable to unwind D loops or dissociate
FT                                synthetic HJs.
FT                                {ECO:0000269|PubMed:22723423,
FT                                ECO:0000269|PubMed:22844101}.
FT   MUTAGEN     672    672       Y->A: Abolishes interaction with MHF
FT                                complex; when associated with A-674 and
FT                                A-678. {ECO:0000269|PubMed:24026537}.
FT   MUTAGEN     674    674       R->A: Abolishes interaction with MHF
FT                                complex; when associated with A-672 and
FT                                A-678. {ECO:0000269|PubMed:24026537}.
FT   MUTAGEN     678    678       R->A: Abolishes interaction with MHF
FT                                complex; when associated with A-672 and
FT                                A-674. {ECO:0000269|PubMed:24026537}.
SQ   SEQUENCE   834 AA;  96555 MW;  987AD715109C8215 CRC64;
     MSDDSFSSDE DWDELDTQVV DKIENEYHNN TIGLNGYSVD EYFDANDSNR YRLQHELDES
     AAQQWVYPIN VSFRDYQFNI VQKALFENVL VALPTGLGKT FIAAVVMMNY LRWFPKSYIV
     FMAPTKPLVT QQMEACYKIT GIPKSQTAEL SGHVPVTTRN QYYQSRNVFF VTPQTILNDI
     KHGICDRTRI SCLVIDEAHR STGNYAYVEV VHLLSLSNKN FRILALSATP GNKLEAIQNV
     IDSLHISRIE IRTENSIDIS QYVQKKEVDF FPVDLSAEIT DIRDRFSSIL EPMLQKLNKG
     NYYRIQNAKD ITSFTVVQAK QAFLAMSGQN FPANQKWDIL NTFDALATFA YPLNLLLNHG
     IRPFYQKLRE VEEECFVGRS GYKKRIINHE NYRPLMDDIE ILLRDQSFVG HPKLEHLERI
     VTEYFEKEQT KDTRIMIFVE IRSSAEEILR FLGKFYPNVR PAIFIGQSAV RKAAGMSQKL
     QNETVKQFQK GEVNTLIATS IGEEGLDIGE VDMIICYDAS ASPIRMLQRM GRTGRKRKGY
     IYMLLTRGKE EAKWERAKDA YRTLQDNIVS GRGLSLSEKS YRILPEKFRP VCDKRVIEIP
     KENEEVVVAP KKVQLRTKIK KKFFMPENAL NGFITASALG KPKRALAKSE ESPFEICPVT
     YSIEQEKKLE KYKRVCLRGL DIHRNRRLSQ LSVTGRIPHS LATKSIHSFL KHLNTIDSQK
     AQEWRREINN QFQVSNINST DRDTKQPKMH DFRQPLHPNP MTTLKRKGQH NSFSYDKSTL
     FYDNNNNLEE DLPDVNISIS SRNEEASKTK PFDDRQQRLQ QLVEKRKRMK GMLI
//
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