MPH1_YEAS7
ID MPH1_YEAS7 Reviewed; 993 AA.
AC A6ZVS0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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};
DE AltName: Full=Mutator phenotype protein 1 {ECO:0000250|UniProtKB:P40562};
GN Name=MPH1 {ECO:0000250|UniProtKB:P40562}; ORFNames=SCY_2786;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000124; EDN61495.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZVS0; -.
DR SMR; A6ZVS0; -.
DR PRIDE; A6ZVS0; -.
DR EnsemblFungi; EDN61495; EDN61495; SCY_2786.
DR HOGENOM; CLU_002513_1_0_1; -.
DR Proteomes; UP000007060; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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.
FT CHAIN 1..993
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333382"
FT DOMAIN 94..261
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 507..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 530..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 209..212
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 993 AA; 114205 MW; 64FB1E68352ECB90 CRC64;
MASADDYFSD FEDDELDKLY EKAINKSVKE TITRRAVPVQ KDLHDNVLPG QKTVYEEIQR
DVSFGPTHHE LDYDALSFYV YPTNYEVRDY QYTIVHKSLF QNTLCAIPTG MGKTFIASTV
MLNYFRWTKK AKIIFTAPTR PLVAQQIKAC LGITGIPSDQ TAILLDKSRK NREEIWANKR
VFFATPQVVE NDLKRGVLDP KDIVCLVIDE AHRATGSYAY TNVVKFIDRF NSSYRLLALT
ATPASDLEGV QEVVNNLDIS KIEIRTEESM DIVKYMKKRK KEKIEVPLLL EIEDIIEQLG
IAVKPVLQQA IELGIYEECD PSQINAFKAM QQSQKIIANP TIPEGIKWRN FFILQLLNNV
GQMLKRLKIY GIRTFFNYFQ NKCTEFTTKY NLKKSTNKIA AEFYYHPILK NIKNQCENYL
SDPKFVGHGK LQCVRDELME FFQKRGSDSR VIIFTELRES ALEIVKFIDS VANDQIRPHI
FIGQARAKEG FDEVKYTRKH APKGRKKVER LHRQEQEKFL EAERTKRAAN DKLERSARRT
GSSEEAQISG MNQKMQKEVI HNFKKGEYNV LVCTSIGEEG LDIGEVDLII CYDTTSSPIK
NIQRMGRTGR KRDGKIVLLF SSNESYKFER AMEDYSTLQA LISKQCIDYK KSDRIIPEDI
IPECHETLIT INDENEIINE MEDVDEVIRY ATQCMMGKKV KPKKAITKKK RVQENKKPKK
FFMPDNVETS IVSASTLINK FLVNESGGKQ LVTSNENPSK KRKIFKALDN LENDSTEEAS
SSLETEDEEF SDDNNVFIAE GQNGCQKDLE TAIIRTGESL TTLKPLHNFE RPNMALFVND
CGLPTKIEKN VKDIRGNQHN LEKEKNCTVD KNNMVLSLDD WNFFRDRYIP EGVSFDVEPN
FVQYTKGVKV PHCHKVSKII TLFNDESNDN KKRTIDMNYT KCLARGMLRD EKKFVKVNDK
SQVDNNSVNH DSSQSFTLSN AELDDILGSD SDF
