ID   MPH1_KLULA              Reviewed;        1002 AA.
AC   Q6CQX2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ATP-dependent DNA helicase MPH1 {ECO:0000250|UniProtKB:P40562};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P40562, ECO:0000250|UniProtKB:Q9UT23};
DE   AltName: Full=FANCM-like protein 1 {ECO:0000250|UniProtKB:Q9UT23};
GN   Name=MPH1 {ECO:0000250|UniProtKB:P40562}; OrderedLocusNames=KLLA0D13552g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by
CC       homologous recombination and in genome maintenance. Capable of
CC       unwinding D-loops. Plays a role in limiting crossover recombinants
CC       during mitotic DNA double-strand break (DSB) repair. Component of a
CC       FANCM-MHF complex which promotes gene conversion at blocked replication
CC       forks, probably by reversal of the stalled fork.
CC       {ECO:0000250|UniProtKB:Q9UT23}.
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:0000250|UniProtKB:Q9UT23};
CC   -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC       MHF complex. {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40562}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       FANCM sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH00763.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR382124; CAH00763.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_453667.2; XM_453667.2.
DR   AlphaFoldDB; Q6CQX2; -.
DR   SMR; Q6CQX2; -.
DR   STRING; 28985.XP_453667.2; -.
DR   EnsemblFungi; CAH00763; CAH00763; KLLA0_D13552g.
DR   GeneID; 2893426; -.
DR   KEGG; kla:KLLA0_D13552g; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   HOGENOM; CLU_002513_1_0_1; -.
DR   InParanoid; Q6CQX2; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0070336; F:flap-structured DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR   GO; GO:0007535; P:donor selection; IEA:EnsemblFungi.
DR   GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR   GO; GO:0060543; P:negative regulation of strand invasion; IEA:EnsemblFungi.
DR   GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
DR   CDD; cd18033; DEXDc_FANCM; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR039686; FANCM/Mph1-like.
DR   InterPro; IPR044749; FANCM_DEXDc.
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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1002
FT                   /note="ATP-dependent DNA helicase MPH1"
FT                   /id="PRO_0000333375"
FT   DOMAIN          108..275
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          506..669
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          531..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           223..226
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        531..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         121..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1002 AA;  114976 MW;  4BFB9FA962E9065B CRC64;
     MFCKQKHKTR KKPAVNALMA DLSDLSDDDL ESLLENNVNR SVNQTVTRHR IPVQRDLFMN
     VLPNQQTFYE ETHTDVSYGP THHQLNEENL DEYIYPTNYE VRQYQYDIVR CALFENVLCA
     IPTGTGKTFI ASTVMLNYYR WTKSSKIIFT APTRPLVAQQ IKACLGITGI PYSDTAILLD
     KSRKNREEIW QQKRVFFTTP QVVENDLKRG VLNPKDVVLL VIDEAHRARG NYAYVELTKF
     IDRFNTSYRL LALTATPAAD LEGVQEVVNN LHISKIELRT EDSLDVARYM MRRDREMIEI
     GLIPEIEEVV EQIGIAIAPV LQEAIQLGIY ESCEPHQINA FVAMQQSQKI ILNPSIPEGL
     KWKNFFILQL LSQVGHMYRR LRIYGLRAFY NYFQNKYTEF TTKYSMKKST NKTAANFFYS
     PILKTVIDKC KRRLEEPEFY SHEKLEYLNN ELADFFTMAP SDSRAIIFTE LRESALEIVK
     SIDILNDGAL RPHIFIGQAK GKEHFDEETY IRKNKPKGRT KAARLRRIEE ENRVEEEKKR
     QKEQAKLERT GRRTGSSEEA QLSGMNQKQQ KKVISDFKKG IYNVLVCTSI GEEGLDIGEV
     DLIICFDSTS SPIKNIQRMG RTGRKRDGRI VLLFSGNEKF KFEQAMNDYE NLQTAITHNA
     LEYTKSDRIL PPNVQPKCEE KFIIISNEND EVNKLEDSDE VIKYATQAML GKLKTKKKEP
     KPKKTTAKAK KSSDKTFFMP DNVKEGFTSA SSLLNKYTIN EFGEKISLTP SVSKKAIKPK
     KEWNMLDEIE YDSVEISPAK SQVEQPSQPH KPTTTQGILT PDETTNHIPS ASQGSSVQTD
     SHTVQEPVLK KLKLAHQIED PSTSIEYYSG YELVPQYGAT DSAQMLTMQE QRHFLKKYVP
     DTVHWSIAPD LAKSKTRKIR HVPKIEEILN TCQDMHTNTR EKIIGMNRTN ALARSIGYNR
     SVGMELEVML PSIVVPNETI TNAKNMTDLL EDEDGLSDFL SD