MPH1_ASHGO
ID MPH1_ASHGO Reviewed; 1077 AA.
AC Q75AA7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=ADR011C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 8.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51931.2; -; Genomic_DNA.
DR RefSeq; NP_984107.2; NM_209460.2.
DR AlphaFoldDB; Q75AA7; -.
DR SMR; Q75AA7; -.
DR STRING; 33169.AAS51931; -.
DR EnsemblFungi; AAS51931; AAS51931; AGOS_ADR011C.
DR GeneID; 4620256; -.
DR KEGG; ago:AGOS_ADR011C; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_0_1; -.
DR InParanoid; Q75AA7; -.
DR OMA; IRPHIFI; -.
DR Proteomes; UP000000591; Chromosome IV.
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; 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:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0070336; F:flap-structured DNA binding; IEA:EnsemblFungi.
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:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR GO; GO:0007535; P:donor selection; IEA:EnsemblFungi.
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:0060543; P:negative regulation of strand invasion; IEA:EnsemblFungi.
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; 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; 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..1077
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333362"
FT DOMAIN 99..266
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 511..660
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 536..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..217
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 831..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1077 AA; 122918 MW; B51F3C1272839650 CRC64;
MLQHATITKM TDFSDLDDDD IVGLLDQDVN RCVETSVTRH KLAMQRDLTG KVLDGEKRYY
EEVVTSVTYK PTHHQLRYEN LNTYLYPTNY EVREYQFNIV HRALFENVLC AIPTGMGKTF
IASTVMLNYY RWTVGTKIIF TAPTRPLVAQ QIKACLGITG IPYNDTAILL DKSRKHREQI
WSEKRVFFAT PQVVENDLKR GALNPKDVVL LVIDEAHRAR GSYAYVELTK FIDRFNTSYR
VLALTATPAT DLEGVQEVVD NLQISKIELR TEESEDIVRY MKRRDTEEVI VPLIPEIEDI
IEQLGIAITP VLKEAVQLGL YDDCEPVNIN AFIAMQQSQK ILANSSIPEG VKWKNYFILQ
LLCHVGHMLK RLKIYGIQTF YTYFDNKYRE FTTKYGIGKS TNKTAASFYY SSILKNITKT
CQAYTANPSF LGHGKLYRVR DELSTFFASA GDDSRVIIFT ELRESALELV KCVDNMNDRF
IRPHIFIGQA KGKESFDDGE YLRKHAPKGR KKVDRIRRLE EEKRLADEKL RKKEEEKLAR
TARRTGSSEE AQISGMTQKQ QKEVISLFKK GDYNVLVCTS IGEEGLDIGE VDMIICYDTT
SSPIKNIQRM GRTGRKRDGR IVLLLSDNEP RKFEQAMEDY AQLQRLIGEE SLNYKVTDRI
IPKGINPQCQ KEFITISEKN SAVNGMEDAD SVIKYATQAM LGKLDKRKAV KKSTGKAAPK
RFFMPDDVET GIVPAMKLVK SYKYTENGEA FPVAESVKGR RPKSKDTLLD RLEYDSLESE
LSSPEKATKS QNVVEIRPKL LSDILLKDED TLHFEHSSSC PKVDSLASVT TLSSDNKSTP
DQLKRSQSDN GFGIPPKRQR LCYDTSANCS STDTHLMEAQ SKNKDNPANR KTGEPHYKLE
VSPLKREEDD RDVIPQNIAV KPEVPHLTQE CLTTGRVYKS EFSKYDGFLT VSERRYFEQN
YSPVHLVSLE PRPVFSRSRN RVAIVPHSER VQRLINIFAA MDTDDKVHII DMHRKHALAR
RTVHGGPTEN SDLLQPSSDG IIVPNDDIRL FSLRPRATDF EDMLEDDEGL SELLDSD
