ID   MPH1_NEUCR              Reviewed;        1168 AA.
AC   Q7SDF3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=NCU09318;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA34786.1; -; Genomic_DNA.
DR   RefSeq; XP_964022.1; XM_958929.3.
DR   AlphaFoldDB; Q7SDF3; -.
DR   SMR; Q7SDF3; -.
DR   STRING; 5141.EFNCRP00000009115; -.
DR   PRIDE; Q7SDF3; -.
DR   EnsemblFungi; EAA34786; EAA34786; NCU09318.
DR   GeneID; 3880171; -.
DR   KEGG; ncr:NCU09318; -.
DR   VEuPathDB; FungiDB:NCU09318; -.
DR   HOGENOM; CLU_002513_0_1_1; -.
DR   InParanoid; Q7SDF3; -.
DR   OMA; FMMRAIF; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000400; F:four-way junction DNA binding; IBA:GO_Central.
DR   GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR   GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR   GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
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..1168
FT                   /note="ATP-dependent DNA helicase mph1"
FT                   /id="PRO_0000333378"
FT   DOMAIN          162..330
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          506..665
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          24..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           278..281
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        24..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1038
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1168 AA;  129304 MW;  8710576BC925882B CRC64;
     MDDDDFDDIP DEDLMLAFTQ ATGNITSHHP SNSKQLASSA KPPAQAWPIS DSARRIVTPT
     VSQGQATATG RAKTASKPTT SATTSRPSLA QSSQRKNLRQ TTLWGGTLEE DAQPAPQAVS
     NRPFRADMPP EQPTHHEIDI EEMKTWVYPM NLGPIRDYQF SIVKNGLFNN TLVALPTGLG
     KTFIAATIML NYIRWTKTAK AVFVAPTKPL ASQQVQACLS IAGIPRSQAT LLTGETPPVL
     REDEWATKRL FFMTPQTLMN DLSKGYADPK SIVLLVIDEA HRATGDYAYV KVVEFLRRFS
     KSFRILALTA TPGSSLEGVQ DVIDNLGISH VEIRTEESID IRQYVHSRDI NTITFDPSDE
     MMEVRDLFSK ALKPLVTKLS SQNIYYGRDP MSLTTYGLMK ARNDWMAGPG RHVNQGTKFS
     VIATFAILQS LAHSIKLLNF HGIKPFYNNL AEFRTTEEEK GGKGSKLKRQ VLEDENFQKM
     MDMIEGWMKI DGFLGHPKLE YLCETLVNHF MDAGEGSNTR AIVFSEYRDS AEEIVRILNK
     QPLIKATVFV GQADSKRSEG MKQKQQIETI EKFKNGAHNV LVATSIGEEG LDIGQVDLIV
     CYDASASPIR MLQRMGRTGR KRAGNIVLLL MKGKEEDKFN EAKDNYATMQ RMICEGSRFT
     FRHDLSSRIV PRDIRPEVEK KVVEIPLENS QNPELPEPKR SAARMRTKPA KKKFNMPDGV
     ETGFIKASFF GQAGAKTAKP PARPPAPKET DFIAERPKLE SILLSTSQEN ELRRNYTKIP
     LGHSKVEELD IDWYRHPTSR RVVQKTIHVK HGEYTKRCVK LFRSLAKSQA PANRYTKPYG
     ETDTSSWELI PLPPLADETE GETSRKGQKK RPRLESGQEA EEAEQYAAPK KRQATAKTKS
     TGVSKQTNKP RARHTALISD CEEGGNEYDG NVDDDEQSRP RNFRSKGRGR GSGRGKKSQP
     KQGDPNVDYG DDCTRTSDME MGTDGSDDGA DLEDFIVSDG EVTSSLQHRP RGSTSPTTAP
     DAGSSSLSSK TGRKQQAPDS FASDEDDGDV FGPKFVPVTA SAAKGSLPST ARREKPKPFY
     VPVELPATQD TTDGDDDLPD IEFLSAKRKR EGTGTGMRTG SPGHVKVGDT SKGGSGGDQT
     REKPSGGAAS HARARKRTVV MDSDDDQE