MPH1_CHAGB
ID MPH1_CHAGB Reviewed; 1134 AA.
AC Q2HG76;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, 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=CHGG_00778;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ92543.1; -; Genomic_DNA.
DR RefSeq; XP_001219999.1; XM_001219998.1.
DR AlphaFoldDB; Q2HG76; -.
DR SMR; Q2HG76; -.
DR STRING; 38033.XP_001219999.1; -.
DR EnsemblFungi; EAQ92543; EAQ92543; CHGG_00778.
DR GeneID; 4386877; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_1_1; -.
DR InParanoid; Q2HG76; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 989616at2759; -.
DR Proteomes; UP000001056; 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..1134
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333372"
FT DOMAIN 194..362
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 538..699
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..313
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..956
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1134 AA; 126419 MW; AEFA753206D362C9 CRC64;
MDDDEFDDEF GDIADEDMIL ALTQATDSAA ASSNEQANQP RSFGSGPRPP LPRPSTQFSN
SVKAPPLQPP SHRQPIARAP GSFSRNPAPG NTRHGSLNTS PANAFDTSPK RPNPPRPSAQ
TQAQIQAQNL RQTTLWGTTI QEDRVAGSQA PNSRPFRADL PPETPTHHEL QHDELSTWVY
PLNLGAIRDY QFSIVKNGLF HNTLVALPTG LGKTFIAATI MLNYFRWTKR SKIVFVAPTK
PLASQQVQAC LGIAGIPRSQ ATLLTGETPP VLRQGEWESK RLFFMTPQTL MNDLSKGYAD
PKSIVLLVVD EAHRATGDYA YVKVVEFIRR FSKSIRILAL TATPGSTVEG VQDIIDNLGI
SHVEIRTEES IDIRQYVHSR NIDTVTFDPS DEMHEVRGLF SKALKPLVDK LSAQNIYYGR
DPMNLTTFGL LKSRQEWLAG PGGHANQGVK FMMMAVFSIL QSLAHLIKLL NFHGIKPFYN
GLAEFRSSEE GKPGQGSKLK RQLLADESFQ RMMALIERWM RMEEFNGHPK LTYLCETLVN
HFIDAGENSN TRAIVFSEYR DSAEEIVRLL NNQPLIRATV FVGQADSKRS EGMKQKQQIE
TIEKFKNGGF NVLVATSIGE EGLDIGQVDL IVCYDASASP IRMLQRMGRT GRKRAGNIVL
LLMKGKEEEK FLEAKDNYQK MQQLICNGDG FTFRHDLSTR IVPRDIRPEV DKRHVDIPIE
NSQNTSLPEP KKTAAGLRKK VAKKKFNMPD DVETGFVNLK ASFFGQPAER AANIPKPPAE
TDFLVEVPPL EKVLLSKSQT ERFERLYKTL PKTPFDKVQE LGFDDINLGA HPASQRVLRR
TVSLKHGQYT RKCVKLFRTL GESQDPLERY TQPYGEIDTM SWKQLPVPAI RRRGSGQPAK
QGPGYSSVST NSVQAASCQR LERQIASLTR KRISESNYFS ECEEAEEDED EAEETATEGT
TPQGRGGRGR GAAKRGRGGF KRAHDHIEDF GDDCTRTSDM EETDGSDSGA DLDDFIVGDD
VFSSSNWQGS NDPTTPSSSR LSLRHRRTEQ VTAEEKPFYE PPEFGSTQDS DDEMPDLAEL
VAKSAKKPAG PSKPRVAPPA DEDGEDDLPQ LSPRRPQAKR RRQVLSDSDD DDTP
