MPH1_ASPNC
ID MPH1_ASPNC Reviewed; 1124 AA.
AC A2Q8R2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
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=An01g05260;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAK43695.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM269966; CAK43695.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001388951.2; XM_001388914.2.
DR AlphaFoldDB; A2Q8R2; -.
DR SMR; A2Q8R2; -.
DR PaxDb; A2Q8R2; -.
DR PRIDE; A2Q8R2; -.
DR EnsemblFungi; CAK43695; CAK43695; An01g05260.
DR GeneID; 4978206; -.
DR KEGG; ang:ANI_1_2526014; -.
DR VEuPathDB; FungiDB:An01g05260; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0070336; F:flap-structured DNA binding; IEA:EnsemblFungi.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR GO; GO:0007535; P:donor selection; IEA:EnsemblFungi.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR GO; GO:0060543; P:negative regulation of strand invasion; IEA:EnsemblFungi.
DR GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
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..1124
FT /note="ATP-dependent DNA helicase mph1"
FT /id="PRO_0000333366"
FT DOMAIN 328..496
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 666..840
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 444..447
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1124 AA; 125664 MW; 9A8C124AC5E41D94 CRC64;
MFTLDGDSSD YFDDDLGDLG VDRPSDATDP DTPPPAKRRR LRAGKDASNA DLQSHQKPRA
ERGDGARTAL SSDSFIDYDD DEVPSPERES PYFQDDSERE ARSKYKVFAP KNANIQENIF
VTQLTQPPSP PEMLRGPRWK KPDPGLPTRT VATPLPETTQ SRESAAGDRD DEYDDDEEMK
AAIEASLQSF EEETSRPAPS VPLQKPPSST PIIGQQSTTI EASNDLLDDI PDDAFDSDLS
MSPPPAPQPR PAARSFTQST NRPLGVRQTT LFGMVARNPE NQPPRGEQVY SPPEKSEPPT
QHKLNQEALG TWVYPTNLGK TRDYQFNIAQ KGLFHNLLVA LPTGLGKTFI AATIMLNWFR
WTKDAQIVFV APTKPLVAQQ ISACFEVAGI PRSQTTMLTG EAAPGIRAEE WKAKRVFFMT
PQTLINDLKT GIADPKRIVL VVVDEAHRAT GGYAYVEVVK FLRRYNQSFR VLALTATPGS
TVESVQAVID GLDISRVEIR TEQSLDIREY VHSKDTDVQT FQNSEEMVLC MDLMSKALQP
LLDQLRSTNA YWGRDPMGLT AYGLTKARQQ WMLSDSGRNA HFGVKAKMNA IFTVLASLAH
GIDLLKYHGI TPFYRHLLHF QSNTEGQKGG KYQRQVVQDE SYKKLMNHLQ PWTKNPEFIG
HPKLEYLKQV VLNHFMDAGE GSGADENKDQ PATRVMIFVH FRDSAEEVTR VLKRYEPMIR
PHVFVGQSSA KGSEGMGQKT QLDIVQKFKK GTYNTIVATS IGEEGLDIGE VDLIVCYDSS
ASPIRMLQRM GRTGRKRSGK ITLLLMQGKE EESYIKAKDN YEKMQQMIAS GTRFTFHDDM
SPRILPPGVR PVADKRAIDI PEENTVRDLP EPKRRGRAPK RPPKKFHMPD NVETGFTTAS
HLAGTSKRRV PNKSKARTPT PEPVELPALE DVLLTPAQQK ELELHYSNAG PSEELLVSYP
RSDAFPRLQL APRPTKAVRH GSLTRRMIET LQKMDQITPD CGDRYKGILA REKASMPKAS
IVAPKPNGRG EAQSRTKARH TSKVVSSKSR NQEEQDVTEV QRTPPGKHSV SATNAEVEPF
YCSQRTQDGD TDDDFDLPDV STLLNRSVER PSTRGRFVLD DSDD
