ID   MPH1_NEOFI              Reviewed;        1111 AA.
AC   A1D4V5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=NFIA_021570;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW23448.1; -; Genomic_DNA.
DR   RefSeq; XP_001265345.1; XM_001265344.1.
DR   AlphaFoldDB; A1D4V5; -.
DR   SMR; A1D4V5; -.
DR   STRING; 36630.CADNFIAP00001175; -.
DR   EnsemblFungi; EAW23448; EAW23448; NFIA_021570.
DR   GeneID; 4591011; -.
DR   KEGG; nfi:NFIA_021570; -.
DR   VEuPathDB; FungiDB:NFIA_021570; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   HOGENOM; CLU_002513_0_0_1; -.
DR   OMA; FMMRAIF; -.
DR   OrthoDB; 989616at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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   InterPro; IPR003903; UIM_dom.
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..1111
FT                   /note="ATP-dependent DNA helicase mph1"
FT                   /id="PRO_0000333377"
FT   DOMAIN          306..474
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          644..818
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1092..1111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           422..425
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        33..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         319..326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1111 AA;  124531 MW;  F011C274655B1E16 CRC64;
     MSVSGDDSDD YFDHEIDDVI VPGTPDAVKS AQTDNRPAKR RRLDAGVFDE SDISIDQGDG
     EDEFQSPDRR SVNAVQSEDV ERTSKYKVFV PKRKNFQENI FVTQLTQPPS PPEMIRGPRW
     KKPGPEPLAP KPTTTTVDAS HQPDQYYDED KEIEAAIAAS LRSFEEENGG NIPSTASRST
     PALTAVAPSA ALKEAAADVP FNLDDIPDDA FDSDLSLSPP RTTSQATRGP PVQSQFRTNR
     PLGLRQSTLF DMAARNSDIP SQRGEQILSP PEKNEPPTHH KLNEEAINTW VYPTNLGKTR
     DYQFNIAQRG LFHNLLVALP TGLGKTFIAA TIMLNWYRWT KSAQIIFVAP TKPLVAQQIS
     ACFQVAGIPR SQTTMLTGEA APGIRAEEWK SKRVFFMTPQ TLVNDLKSGI ADPKRIVLLV
     VDEAHRATGG YAYVEVVKFL KRYNKSFRVL ALTATPGSTV ESVQAVIDGL GIAKVEIRTE
     QSLDIREYVH ARDTEVQTFK NSDEMVLCME LFTRTLQPLV DQLRNLNAYW GRDPMALTAF
     GLTKARQQWM GSDAGRNANL GLKGKVNAIF TVLASLAHAI DLLKYHGITP FYRHLLHFQS
     NTDGQKGGKY QRQIVQDESF KKLMNHLQPW TKNPEFIGHP KLEYLKQVVL NHFMDRGEGT
     AANGDQSQSA TRIMIFVHFR DSAEEVVRVL KRYEPLIRPH VFVGQSSAKG SEGMDQKTQL
     SIVQKFKKGT YNTIVATSIG EEGLDIGEVD LIVCYDSSAS PIRMLQRMGR TGRKRAGNIV
     LLLMQGKEEE SYIKAKDNYE KMQQMIASGT RFTFHDDTSP RILPPGVRPV AEKRQIDIPV
     ENTQADLPEP RKRARPPKRP PKKFHMPDDV ETGFAKASSL TGKVTKKAET KKAVRKPTPE
     PVEVPALEEV LLTPGEQQDL ERRYCHIGGT SPEFIRNPRV DAYPRLQSVP RPTKAIKHGS
     LTSRMIGTLQ KMSKVSVDCE RRYRKVLALE SSKEIVDSVL SREPGSPAQN SGRLGKKPHA
     FKRPSATSRP NNVHVREDEN EDNCTPELLS PEKLMSSFLE PHTERPPYSS QRSQDAFELD
     FPDVETLLNR SAERHVSRKR NRFVLDDDTE E