MPH1_DEBHA
ID MPH1_DEBHA Reviewed; 1105 AA.
AC Q6BRF0; B5RTJ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=DEHA2D16896g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382136; CAR65680.1; -; Genomic_DNA.
DR RefSeq; XP_002770326.1; XM_002770280.1.
DR AlphaFoldDB; Q6BRF0; -.
DR SMR; Q6BRF0; -.
DR STRING; 4959.XP_002770326.1; -.
DR PRIDE; Q6BRF0; -.
DR EnsemblFungi; CAR65680; CAR65680; DEHA2D16896g.
DR GeneID; 8998603; -.
DR KEGG; dha:DEHA2D16896g; -.
DR VEuPathDB; FungiDB:DEHA2D16896g; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_0_1; -.
DR InParanoid; Q6BRF0; -.
DR OMA; EGLKWQN; -.
DR OrthoDB; 331426at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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..1105
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333374"
FT DOMAIN 94..261
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 468..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 493..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 209..212
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 516..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1105 AA; 125395 MW; C20D240391FCB918 CRC64;
MNSDDDSVFN DDLNDSEITN LIHNIPSSSS SCSSSKNKLQ RNLYGEIIPE QYVEIDSSKG
YTELPPTHHA LNYENLSSYI YPTNFEVRDY QFNIVQRAFY DNLLVALPTG LGKTFIASTV
MLNFTRWFPR GKIIFMAPTK PLVAQQIKAC CGITGIPTSE VAILLDKSRR NRADIWDSKT
VFFTTPQVVE NDLTAGIIDP KEVVLLVIDE AHKSKGNYAY NNVVKFITRF NISFRILALT
ATPASDVEGV QEIIDNLSIS KVEVRTEQSI DITKYMKQKK IERVTVSPSV EICELVDMLC
TAIQPVLSMA NERRIYDMSD PSKINAFQVI DASQRLLKNP TIPEGLKWQN YFILQILNVV
GQALRRLNIY GIKSFYNYFD QKHKEFTIKF KNKKSNNQTA ARFYFHDNIK LILDKCKELI
ADDNFLGHPK LEILINELDE FFKENEANDS RVIIFTEFRE SALDIVSSIE RIGSNLRPHI
FIGQSKEKEK FDEEAYLSKG KKGRTKGKAT KGKQNSETPE RSTSRTSSED AQIKGMNQKL
QKDLIKKFKK GEYNILVATS IGEEGLDIGE VDLIVCYDST SSPIKNIQRM GRTGRKRDGK
VLLLFAGNEE SKFDKAMAGY EFIQQHIMNG RLITLAQSNR IIPKSYKPIV EKKFIEIPEE
NTEIKAEEDE DEIIRIATSY MNNKGKKVTK SKSKSKSNSK SKKIEKRFFM PDNVTTGFQN
VTSMVRKADS DKSVADKRRE KDLLDKLLDS DTEDELLIQS KKSPVKENQS KRPNSEHICE
EDSRQETENN SNESNGSFEN ENDQNKESGV SYPLSYRQTP PKLGIRRLSP QVSMNINLDA
PVATEEAAPL VTGKSTSPPE NVAEKRNSPI LNSSNRECAP KQKTLGLKRR KANSITDQLK
RHYSRVIKPN TAYRTITVSD DEKSVEDSIN NQQLHKNKNL GSTSDDDDAF DEGDVFDDGM
DDELALIAND KLSSFERSLS PNLPAQNNAS DEVYKHEFSP GEGVLNQEQM LELYTSYFSL
LDPADRVDFY DPLNFNQKPN TSINHRGRIG HSQVSRRLLQ SSKFIGSVST TTAKNIVKRY
AQTYNTTNHQ HNMHIVQEIT NSSSK
