GenomeNet

Database: UniProt
Entry: A2Q8R2
LinkDB: A2Q8R2
Original site: A2Q8R2 
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   18-SEP-2019, entry version 81.
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.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   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.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair
CC       by 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
CC       a FANCM-MHF complex which promotes gene conversion at blocked
CC       replication 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
CC       FANCM-MHF complex. {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40562}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. FANCM sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK43695.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AM269966; CAK43695.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001388951.2; XM_001388914.2.
DR   SMR; A2Q8R2; -.
DR   PaxDb; A2Q8R2; -.
DR   PRIDE; A2Q8R2; -.
DR   EnsemblFungi; CAK43695; CAK43695; An01g05260.
DR   GeneID; 4978206; -.
DR   KEGG; ang:ANI_1_2526014; -.
DR   HOGENOM; HOG000076770; -.
DR   KO; K14635; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR039686; FANCM/Mph1-like.
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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1124       ATP-dependent DNA helicase mph1.
FT                                /FTId=PRO_0000333366.
FT   DOMAIN      328    496       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      666    840       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     341    348       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       444    447       DEAH box. {ECO:0000255|PROSITE-
FT                                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
//
DBGET integrated database retrieval system