MPH1_VANPO
ID MPH1_VANPO Reviewed; 1012 AA.
AC A7TSV4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Kpol_328p1;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480526; EDO14649.1; -; Genomic_DNA.
DR RefSeq; XP_001642507.1; XM_001642457.1.
DR AlphaFoldDB; A7TSV4; -.
DR SMR; A7TSV4; -.
DR STRING; 436907.A7TSV4; -.
DR PRIDE; A7TSV4; -.
DR EnsemblFungi; EDO14649; EDO14649; Kpol_328p1.
DR GeneID; 5542673; -.
DR KEGG; vpo:Kpol_328p1; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_0_1; -.
DR InParanoid; A7TSV4; -.
DR OMA; IRPHIFI; -.
DR OrthoDB; 989616at2759; -.
DR PhylomeDB; A7TSV4; -.
DR Proteomes; UP000000267; 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; Reference proteome.
FT CHAIN 1..1012
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333381"
FT DOMAIN 94..261
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 430..654
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 493..555
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 COMPBIAS 509..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1012 AA; 115737 MW; 5279583251B831A8 CRC64;
MQAGNNGGAK LKNDEFDNLY QKNINRRETE TVIRRSIPVQ RDLTGKILPN QVAYYEEIER
EVTFGATHHI LDKDNFDSYI YPTNFEVREY QFNIVQKSLY QNTLCAIPTG MGKTFIASTV
MLNFFRWSKN GKIIFTAPTR PLVAQQIKAC LGITGIPHDQ AAILLDKSRK NREDIWTQKR
VFFTTPQVIE NDLKRGVLNP KDIICLVFDE AHRATGSYAY TNVVKFIDRF NSSYRILALT
ATPGTDIASV QEVVNNLNIS NIEIRTEESM DIIRYMKKRY KEKIEIGLTT EIEMIIEQLG
IAVKPVLQQA VELGIYDECH PSQINSFVAM QKSQQIIANP TIAEGIKWRN FFILQLLNHV
GQMLKRIKIY GIRSFYGYFR NKFSEFTTKY NMGKSTNKIA ASFYYHPILK ILMKNCDVYT
SNSSFIGHDK LQKIINELSD FFLNSRLDSR VIIFTELRES ALEIVKTIDN MGSSSIRPHI
FIGQARGKEN FDDEGFIRKN KPKGRKKADR LKRLEEDKQK QLSKAKQKEQ EKVERSSRRT
GSSEEAQISG MNQKQQKEVI SKFKNGDYNV LVCTSIGEEG LDIGEVDMII CFDTTGSPIK
NIQRMGRTGR KRDGKILLLF SGNESRKFEK AMEDYYDLQR LIGQNFVEYK KSDRILPSNI
TPECRKEFIH ISAENNELNN MEDSDEVIRY ATQCMLGKVP KSKKSKAKAA KEPKGKSKTF
FMPDNVETGI VSAIALVNKK KSNSNESETV IKTECFPNLD DIEKDMLASL SSPVKPEVDD
YKDGTFQKTD RFEEKITGSN LKDMLMSFSK RDEESKVTSF SSDGNYVNEP FGNISLGEKL
DINDDFASTP IVKADMNIGQ YDRSLIENNS RGGVLFKNAF EKEEGLLKKS EKVYFRDHYS
IDNTVVIEPI PNFKRYNKSC LINHNPQVEN ILNLFKGINE NKTQITIEMN RSRCIARGIE
KGSIQLTGSD FSLANVMVAQ KNNEADIVWD TSKTNKNSHE NLNELLDSDS DF
