ID   MPH1_ASPFC              Reviewed;        1101 AA.
AC   B0XMV6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=AFUB_003450;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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}.
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; DS499594; EDP55648.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XMV6; -.
DR   SMR; B0XMV6; -.
DR   EnsemblFungi; EDP55648; EDP55648; AFUB_003450.
DR   VEuPathDB; FungiDB:AFUB_003450; -.
DR   HOGENOM; CLU_002513_0_0_1; -.
DR   PhylomeDB; B0XMV6; -.
DR   Proteomes; UP000001699; 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   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.
FT   CHAIN           1..1101
FT                   /note="ATP-dependent DNA helicase mph1"
FT                   /id="PRO_0000333365"
FT   DOMAIN          296..464
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          634..808
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          22..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           412..415
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        25..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..120
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         309..316
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1101 AA;  123391 MW;  8B8CF03928335BA3 CRC64;
     MSVSGDDFDD YFDDEIDDVI VPGTSDTVES VQTNNRPAKQ SDISISQGNE EDEFQSPDRL
     SGNAVQFEDV ERTSKYNVFI PKCKNVQENI FVTQLTQPPS PPEMIRGPRW KKPGPEPLAP
     EPATTRVGAN HQSDQYHDED KEMEAAIAAS LRSFEEENGG DVPSTASGST PARTAAAPCA
     APKGTAADVP FDLDDIPDDA FDSDLSLSPP RSTSQATRGP PVQSQFRTNR PLGLRQSTLF
     DMAARNPDIS SQRGEQIFSP PEKSEPPTHH KLNEEALNTW VYPTNLGKTR DYQFNIAQRG
     LFHNLLVALP TGLGKTFIAA TIMLNWYRWT KSAQIIFVAP TKPLVAQQIS ACFQVAGIPR
     SETTMLTGEA APGIRAEEWK SKRVFFMTPQ TLVNDLKSGI ADPKRIVLLV VDEAHRATGG
     YAYVEVVKFL KRYNKSFRVL ALTATPGSTV ESVQAIIDDL GIAKVEIRTE QSLDIREYVH
     ARDTEVQTFQ NSDEMVLCME LFTRTLQPLV DQLRNLNAYW GRDPMALTAF GLTKARQQWM
     GSDAGRNANL ALKGKVNAIF TVLASLAHAI DLLKYHGITP FYRHLLHFQS NTDGQKGGKY
     QRQIVQDESF KKLMNHLQPW TKNPDFIGHP KLEYLKQVVL NHFMDRGEGT AANGDQSQSA
     TRIMIFVHFR DSAEEVVRVL KRHEPLIRPH VFVGQSSAKG SEGMDQKTQL SIVQKFKKGT
     YNTIVATSIG EEGLDIGEVD LIVCYDSSAS PIRMLQRMGR TGRKRAGNIV LLLMQGKEEE
     SYIKAKDNYE KMQQMIASGT RFTFHDDKSP RILPPGVRPV AEKRQIDIPV ENTQADLPEP
     RRRARPPKRP PKKFHMPDDV ETGFAKASSL TGKVTKKAET KRAVRKPTPE PVEVPALEEV
     LLTPRQQQDL ERRYCHIAGT SPEFIRNPRV DAYPRLQSVP RPTKAVKHGS LTSRMIGTLQ
     KMGKVSVDCE SRYRKVLALD SSKEIVDSVL SRDPWPPAKN SGRLGEKTHA FKRPSATPRP
     NNVHVREDEN EDNCTPELVS PEKLMSSFLE PHTERPPYSS QRSQDAFELD FPDVETLLNR
     SAERHVSRKR NRFVLDDDSD E