MPH1_MAGO7
ID MPH1_MAGO7 Reviewed; 1102 AA.
AC A4RN08; G4MZG1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; ORFNames=MGG_04429;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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}.
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DR EMBL; CM001232; EHA53716.1; -; Genomic_DNA.
DR RefSeq; XP_003713523.1; XM_003713475.1.
DR AlphaFoldDB; A4RN08; -.
DR SMR; A4RN08; -.
DR STRING; 318829.MGG_04429T0; -.
DR PRIDE; A4RN08; -.
DR EnsemblFungi; MGG_04429T0; MGG_04429T0; MGG_04429.
DR GeneID; 2678216; -.
DR KEGG; mgr:MGG_04429; -.
DR VEuPathDB; FungiDB:MGG_04429; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_1_1; -.
DR InParanoid; A4RN08; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 989616at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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..1102
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333376"
FT DOMAIN 147..315
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 490..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 19..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 263..266
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 728..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1102 AA; 122381 MW; 40988296EB250BEB CRC64;
MGSDYDSFDD DVADEVLMAL DKPATSGLHS REQEQQRDIS NATPHTSTDL ELEDFGSDAF
DYSPERERAK PIQTARNQAR TFQQTTLLGR IASQAPEPLG TQPRNSRVFR ADLPPEVPTH
HALDPEALKT WVYPTNLGPI RDYQFSIVKN GLFNNTLVAL PTGLGKTFIA ATVILNFFRW
TRNAQMVFVA PTKPLASQQV EACLNIAGIP RSQSTLLTGE TKPVLREAEW EGKRLFFMTP
QTLMNDLSKG YADPKRIVLL VVDEAHRATG DYAYVKVIEF IRRFSKSFRV LALTATPGST
VEGVQDVIDN LGVSHVEIRT EESIDIRNYV HSREIDRVVL EPSDEMLRIS ELFSQALKPL
HSKISQQKIY IGRDPMSITT FGLLKARQDW MKGPGRFANQ GLKMMLMAIF TILQSLAHAI
KLLNYHGIRP FYDNLVAFRS ETEDKGQKGS KYKRQLIGEQ SFQEMMDLAS KWLKIDGFAG
HPKLTHLCDN LLNYFMDAGE GSSTRVIVFS EYRDSAEEIT RVLNVHKPMI SASLFVGQAD
SKKSEGMKQK QQIETIAKFR DGIFNVLVAT SIGEEGLDIG QVDLIICYDA SSSPIRMLQR
MGRTGRKRAG KITLLLMKGK EEDNYAKAQD NYEKMQKLIC EGSRFNFRHD LSSRIVPRDV
KPEVDKRMVE IPIENTQDTS LPEPKARSTR GKKASKKKFN MPDGVETGFN SVASMLGISA
SKTKAKPNKS PKKAESKETD EISPVPPLEG VLLSVKELAE LNKKYRDLPF FHQDTEEICM
PSLTARPDLQ RVLRPTVHVK HGSYTKRCVR LFKKLSHSQG IETRHTKPHG DTDKSRYLDI
SVPPFAEDSG EDVVVVPSGR KRSLSPSSAA SPPPPGRKRK ANTTAAPRSK RQSVVDEYAS
ESEDDTAAAR QRKTNAAASP ESKRQSVLDE YASESDAEAV TQASEDEESV GSLADFISDG
EANGNFPKDM TGFTSDEDDD YRSGSLAKSS LSGPLSGRQV HRSSGAASKS GSTASTAAKP
FFVPASLPGT QQTDDDEDMP DIGILVGKKQ PETRVRKPAK KSNAVFLSSD DDDDDNDDED
DVQPGPAKRT VRRRVIEDSE SG
