MPH1_ASPFU
ID MPH1_ASPFU Reviewed; 1101 AA.
AC Q4WKB5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=AFUA_1G03050;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000007; EAL88017.1; -; Genomic_DNA.
DR RefSeq; XP_750055.1; XM_744962.1.
DR AlphaFoldDB; Q4WKB5; -.
DR SMR; Q4WKB5; -.
DR STRING; 746128.CADAFUBP00000338; -.
DR EnsemblFungi; EAL88017; EAL88017; AFUA_1G03050.
DR GeneID; 3507860; -.
DR KEGG; afm:AFUA_1G03050; -.
DR VEuPathDB; FungiDB:Afu1g03050; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_0_1; -.
DR InParanoid; Q4WKB5; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 989616at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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..1101
FT /note="ATP-dependent DNA helicase mph1"
FT /id="PRO_0000333364"
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
