MPH1_SCLS1
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 03-AUG-2022, entry version 79.
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 mold)
OS (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., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., 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 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; CH476625; EDO01590.1; -; Genomic_DNA.
DR RefSeq; XP_001594258.1; XM_001594208.1.
DR AlphaFoldDB; A7EFH4; -.
DR SMR; A7EFH4; -.
DR STRING; 665079.A7EFH4; -.
DR EnsemblFungi; EDO01590; EDO01590; SS1G_04065.
DR GeneID; 5491071; -.
DR KEGG; ssl:SS1G_04065; -.
DR VEuPathDB; FungiDB:sscle_02g019780; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_1_1; -.
DR InParanoid; A7EFH4; -.
DR OMA; DSSPYRI; -.
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; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; 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; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1235
FT /note="ATP-dependent DNA helicase mph1"
FT /id="PRO_0000333380"
FT DOMAIN 272..440
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 608..784
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 20..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 388..391
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 37..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-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
