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Database: UniProt
Entry: A7EFH4
LinkDB: A7EFH4
Original site: A7EFH4 
ID   MPH1_SCLS1              Reviewed;        1235 AA.
AC   A7EFH4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   18-SEP-2019, entry version 69.
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=SS1G_04065;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476625; EDO01590.1; -; Genomic_DNA.
DR   RefSeq; XP_001594258.1; XM_001594208.1.
DR   SMR; A7EFH4; -.
DR   STRING; 5180.EDO01590; -.
DR   EnsemblFungi; EDO01590; EDO01590; SS1G_04065.
DR   GeneID; 5491071; -.
DR   KEGG; ssl:SS1G_04065; -.
DR   EuPathDB; FungiDB:SS1G_04065; -.
DR   InParanoid; A7EFH4; -.
DR   KO; K14635; -.
DR   OMA; SHGYADP; -.
DR   Proteomes; UP000001312; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PS00690; DEAH_ATP_HELICASE; 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   1235       ATP-dependent DNA helicase mph1.
FT                                /FTId=PRO_0000333380.
FT   DOMAIN      272    440       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      608    784       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     285    292       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       388    391       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
SQ   SEQUENCE   1235 AA;  137407 MW;  0E947C643D968C23 CRC64;
     MSDDEYGDID AAVWDEAEAL TQASQTLPSN FPHRRKRRRI GSEELDDGFL SGRRRGSHGF
     SRSDNDEADE KKSKYRIHLG AEEVPAAVIM GATQADEMPD SSPYRIRGPI YKRPRRSPPM
     ELEQKSSPAQ PSMVESAKTQ KQNIVHSPQP TAQYDFSREL EDLPSDAFSP SPPQLRMSSI
     PITISSSPPL ESTQSVRSQR LAAPQNGLRQ TTLFGGRAPN QVPSSTQAKK VHKYLVDKVP
     EPPTHHTLDE EAIKTWIYPN NLGAERRYQY TIVHKGLFNN LLVALPTGLG KTFIAATIML
     NFFRWTTDSQ IVFMAPTKPL VSQQVKACFE IAGIPRSSTT MLTGDQSPAL RAEEWAEKRV
     FFMTPQTVEN DLKTGIADPK KIALIVVDEA HRATGNYAYT KVVQFLRRFN ESFRVLALTA
     TPGSSVEAVQ EVIDNLEIAE VEIRTEDSID IKEYVHRRDI TEILIDPSDE IIMIRELFSK
     ALQPLVNLLC SQKAYYNKDP MGLTQYGMLT ARKAWMASGA GKSAQMSIKG MMNALFTVLT
     SMGHAIKLLN FHGIGPFFSN IKDFRAEVEG NKKGGKYKNQ IVNSPEFKKM MERIQGWINK
     EDFIGHPKLT YLCDTVLNHF LDAGAGLMGD NMPPSSTRVI VFTEYRDSAE DIARVLNKHG
     PMIRASVFVG QSDSKRSEGM NQEKQLETIR KFKAGGINVI VATSIGEEGL DIGEVDLIVC
     YDSSSSPIRM LQRMGRTGRK RAGKIVLLLM RGKEEDSYKK SKDNYEQIQR MISSGSRFTF
     RHDLSARIIP RKVKPEVDKR FIEIPLENTQ DPSLPEPKRR AKPRKKLAKK FHMPDGVETG
     FRKASKLNSN AESPLTKFGI KRKPSELNDD ELAPVPLLDS VLLNAKDEAE HSRRFLKVPD
     GALEEVGMPD LTAQPITQRT LTRTAKVSHG KYTRSCVSLF NKLSRLQRPE DRDNKPYGDE
     PPSDFGSIPT MPLEAEVRAR APKAPKASDP AQVVKASRVA KTTSALKKAP ASKRVAPKKA
     KPRRGRALRN DNSDSEDSTA SMAMVSNLRS SQIPQPTPDS DEEGPGERVD RTSDMEELEA
     DDDSDLGSLV DFIDPTQTQT QIPLTGTSNF SSSPPLMETW EDERINGNAV GGRRGMLPRA
     VEMTGAKNSS FKNGTMTQES SDGGDSMDSD FPTIEDLVRS DTTTTTTRKI ADPPSSSVFS
     SGQKATPNMF TRKRDGDVRG RGLKRRVVES DDSDE
//
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