MPH1_PICST
ID MPH1_PICST Reviewed; 1050 AA.
AC A3GH78;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 3.
DT 03-AUG-2022, entry version 83.
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=PICST_53391;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAZ63005.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAVQ01000002; EAZ63005.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001387028.2; XM_001386991.1.
DR AlphaFoldDB; A3GH78; -.
DR SMR; A3GH78; -.
DR STRING; 4924.XP_001387028.2; -.
DR EnsemblFungi; EAZ63005; EAZ63005; PICST_53391.
DR GeneID; 4851627; -.
DR KEGG; pic:PICST_53391; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_0_1; -.
DR InParanoid; A3GH78; -.
DR OrthoDB; 331426at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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; 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..1050
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333379"
FT DOMAIN 95..262
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 431..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 493..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 210..213
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 493..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1050 AA; 120120 MW; 74FCD9B067318AAF CRC64;
MPIDSDDNVF DDDDDFIELL QDSSNQTSNV TNEIATDSTN STNTRLVVPN NRLLEEIPVP
KRILLGPTHH KIDYGNLDKY VYPSNFEVRD YQFNIVQRAF YHNLLVALPT GLGKTFIAST
VMLNFLRWFP ESKMIFVAPT KPLVAQQIKA CCSITGIPSS KVAILLDKTR KNRGEIWDEK
QVFFTTPQVV ENDLASGLVD PKTIALLVID EAHRAKGNYA YNNIVKFMDR FTNSYRILAL
TATPASDVDG VQEIIDNLNI SKVEVRSEES IDIIKYMKRK RIIRRNIYQS DEIKECIDLL
CTAIAPVLKV ANGKGILEIT DPSRINFFQC MDASRKIVAN PTIPEGTKWS NFFTLQLLGV
VGQCFRRLNV YGLRSFFSYF NEKYTEFMAK HSKKKSSNKL NADFYFSEPI KQLMKRIRTM
IDDPKVFSHP KIEAMMEELD EFFTINNATD SKVIIFTEFR ESALEIVRFI EKVGKNLKPH
IFIGQAKERD KFDESNFGKK SKGKRVGKKQ QDDSKSSSEN AQINGMNQKL QKEIIKNFKQ
GTYNILVATS IGEEGLDIGE VDLIICYDST SSPIKNIQRM GRTGRKRDGK VVLLFSSNEE
SKFDKAMNGY EYIQQHIMKG QLIDLKEQNR MIPKDWEPKV EMRFIEIPEE NHELQVVDDE
DEIIRIATQY MMGGKSKKKK AAASKKGKTK EKRAKQFFMP DNVEIGFRSV TSMVRAVGSS
KSLEEEKKEE KVRDVLDRIV DSDSDEEIPL GSIPIPRSEV IAHKQSTTDE QLLERDCQSG
SNISDRTLDQ HHSASEERGI NSNFSHESNL PTPPENSPPK RKSIVLEEAR IAKKKHKKSL
GIRKPTIRPP SIIDQLKKQK SKIIRPDSAN ETICLDEDDI LLPEYTNITE KEVTVQEDRR
EIEHDDDSEI FDDGLDEQLA MIDDMNTTKS FVEPTRIDFK DEVFKNDFDE HEGFLNNDEL
MELHTSYFTA IDPMDKVFYY DPSSSVHVDG ANREYAFYGK IGHSKRSQVL IGLQKRAHEM
AAKSKQSKTA TPSEPETFQN YLDSDFIALQ
