MPH1_COCIM
ID MPH1_COCIM Reviewed; 1110 AA.
AC Q1DY43; J3KEQ3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=CIMG_04770;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704914; EAS33746.3; -; Genomic_DNA.
DR RefSeq; XP_001245329.1; XM_001245328.1.
DR AlphaFoldDB; Q1DY43; -.
DR SMR; Q1DY43; -.
DR STRING; 246410.Q1DY43; -.
DR PRIDE; Q1DY43; -.
DR EnsemblFungi; EAS33746; EAS33746; CIMG_04770.
DR GeneID; 4564165; -.
DR KEGG; cim:CIMG_04770; -.
DR VEuPathDB; FungiDB:CIMG_04770; -.
DR InParanoid; Q1DY43; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 989616at2759; -.
DR Proteomes; UP000001261; 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..1110
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333373"
FT DOMAIN 331..499
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 675..846
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 24..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 447..450
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 32..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1110 AA; 124193 MW; 35B2E7C073FAA468 CRC64;
MADDGCSGLS DFITDDELFN EVTLNEVSDS QTGRPTKRRR LNSHEINTDS TGRREIEEAG
TDSDTFDPSL PPNSKTTGRG RKSNDDNPAA RKPKTYTPKY HVDQKPLFVT QTQPSSSPSR
IRGPRWKAPE RNKPSTVSKA KQKSPLPAIW GRKPSTIGSH GTNGKDIDAA IAASLRSFEE
EQSARGDAEM LDDSIEEPGD TQVHATPGPV TNAEKETIFD FEDIPDDAFD FEPEFTETAD
KEPILISSQP RPSQNTTRRP TASQSTSFRQ TTLLGGFASS SSKRSSQPAT QTWPSSSRNE
PPTHHELNKD ALRTWIFPKN LGSRREYQFN IAHRALFHNL LVALPTGLGK TFIAATVMLN
WFHWTKDAQI VFVAPTKPLV SQQVDACFHI AGIPRSQTTL LTGNTPPGVR AEEWRSKRVF
FMTPQTIMND LKTGIADPKR IVLLVVDEAH RATGAYAYVE IVKFLQRFNN SFRVLALTAT
PGATVEAVQE VIDGLSISRI EIRTEKSLDI RGFVHQRNVE TITFENSRDM ITSMELFAKA
LQPVVDRLRN QNAYWGRDPM ALTPFGLTKA RQEWNSSPAG RAASWPVKGT INSMFTVLAS
LAHAIDLLKY HGIGPFYRNL VSFEDSVLKE KKGGKCASQI VADGNFKVLM SKLRSWTNTE
EFIGHPKLEY LRRAILNHFL DAGGKNGGDS EGSDSNTRVM IFSHFRDSAE EIVRVLRKHQ
PFVRPHVFVG QANAKGSEGM DQKTQLEVVG KFKTGTYNTI VATSIGEEGL DIGEVDLIIC
YDGHSSPIRM LQRMGRTGRK RAGNIILLLS KGKEEESYSK AKDSYEKMQQ LIASGSRFTF
HTDKSSRIVP QDIQPEAEEK MIEIPIENSQ LGLPEPAKRS RAPKRPPKKF HMPDGVEKGF
TKASRLGRTN TDSNGRSKRK RVVRTPSPEL EEFPDLGDLC ANQSQELADD PDFQEIAGKQ
IPRLRMDVYP EHQRSLRPTG FIEHGKYTRR VVKTFRKISK LGFDCEAQYR AIVGDPDDDG
EGLEGLSTDR EDDPQSVTAH QSREQPPRVE KRCGTEELSS LDIEAFFPNL AWPARPEAPR
PESDGTDNRD QKPSQRKKRY MISDDSDVFE
