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Database: UniProt
Entry: Q4WKB5
LinkDB: Q4WKB5
Original site: Q4WKB5 
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   18-SEP-2019, entry version 104.
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.
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.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   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.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., 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
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}.
DR   EMBL; AAHF01000007; EAL88017.1; -; Genomic_DNA.
DR   RefSeq; XP_750055.1; XM_744962.1.
DR   SMR; Q4WKB5; -.
DR   STRING; 746128.CADAFUBP00000338; -.
DR   EnsemblFungi; EAL88017; EAL88017; AFUA_1G03050.
DR   GeneID; 3507860; -.
DR   KEGG; afm:AFUA_1G03050; -.
DR   EuPathDB; FungiDB:Afu1g03050; -.
DR   HOGENOM; HOG000076770; -.
DR   InParanoid; Q4WKB5; -.
DR   KO; K14635; -.
DR   OMA; SHGYADP; -.
DR   OrthoDB; 989616at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   Proteomes; UP000002530; 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: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   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   1101       ATP-dependent DNA helicase mph1.
FT                                /FTId=PRO_0000333364.
FT   DOMAIN      296    464       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      634    808       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     309    316       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       412    415       DEAH box. {ECO:0000255|PROSITE-
FT                                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
//
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