MPH1_CANAL
ID MPH1_CANAL Reviewed; 1187 AA.
AC Q5A1A0; A0A1D8PMI6; Q5A1F9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=CAALFM_C406190CA; ORFNames=CaO19.10436, CaO19.2919;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017626; AOW29345.1; -; Genomic_DNA.
DR RefSeq; XP_715573.2; XM_710480.2.
DR AlphaFoldDB; Q5A1A0; -.
DR SMR; Q5A1A0; -.
DR STRING; 237561.Q5A1A0; -.
DR PRIDE; Q5A1A0; -.
DR GeneID; 3642817; -.
DR KEGG; cal:CAALFM_C406190CA; -.
DR CGD; CAL0000186482; MPH1.
DR VEuPathDB; FungiDB:C4_06190C_A; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_1_1; -.
DR InParanoid; Q5A1A0; -.
DR OrthoDB; 331426at2759; -.
DR PRO; PR:Q5A1A0; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0070336; F:flap-structured DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR GO; GO:0007535; P:donor selection; IEA:EnsemblFungi.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0060543; P:negative regulation of strand invasion; IEA:EnsemblFungi.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
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..1187
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333370"
FT DOMAIN 144..311
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 486..681
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 542..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 259..262
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 781..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1187 AA; 135038 MW; 97451D4A927549A3 CRC64;
MIIFATPKVC KGKTRILYFY LSKLFFYVYF FFLIYYSIQK HSYINSTMPI IPLEDDKDDD
WILEDEDDPE FQAILQGNSS KGPAQRTLEG SVAAVSTRPQ NDKYETIPVP VKINTPTHHA
MDFENLKTYI YPTNFEIRDY QYNIVERAFY DNLLVALPTG LGKTFIASTV MLNFLRWFPI
SKIIFMAPTR PLVAQQIKAC CSIAGIPSSK VAILLDKTRR NRAEIWNSRQ VFFTTPQVVE
NDLASGVVNP KSIALLVIDE AHRAKGNYSY NNVVKFINRF SDSYRILALT ATPASDVEGV
QQIIDNLNIS KVEVRTEQSI DIVRHMKRKT VERKTCYPSS EITECIELLA EGITPVLNTA
KERGLLDLTD PTRINFLQCM EISRKIVANP TIPEGLKWSN YFILQLLGMV GQCYRRLNIY
GIRSFQSYFN EKFLEFKTKW NAKKSTNKLN ADFYFSDPIT TLMDRVEELS KTLTYGHPKI
EALMEELDDF FKNHETAGSR VIIFTEFRES ALEIVQCIEK ANDNRKPHIF IGQSKEKEKF
DVENFGKKKQ KGQTKKKKDE RPSTRSSSEN AQMTGMSQKL QKEIIKKFKK GVFNILVATS
IGEEGLDIGE VDLIICYDST SSPIKNIQRM GRTGRKRDGK VLMLFSSNEE SKFDKAMGGY
EYIQQHIMKG DFIQLRPQHR MIPDEYKPEA VKQLIQIPEE NIELKAEDDE DEIIRIATSY
MLGGKGKKGK KANNNSTKKP AKTFFMPDNV ETGFKSAATM VRKVGDNKSL AERNKEKTFL
DKLVDSDSES EVDKENENVI QEVDKSKNQE QNDHIITELD NTEQSVAGNT KSTTNGTSYS
EPENNNQVNQ ESVTANLDSV ARVPEPEVIE NSESEEEQIS KITHNTPATS VDLSNGPEET
SYKIDSVLID LIDDDFTFSS DTEGDKVEVI DAVSPEVCKL PEKPATPPIR KSLGVKRKVN
KTPDPESNSI SIPSSTTKKS HNEVTRKVVQ DPSTTNKKSL GVKRPRPVSI IDQLKRQKIR
SQVIVSRETQ SIIEHESRTQ SSLPSPRNMS DEISEIDVII DLDDDDDDDN KVNGHDKSQT
TISKVQPIYE FSNKEDEGFL SSSQTRELYK NYYIAIDSSD DIPFYDPVQG FSKIKDTDKF
TMGRTGPITH SLRTQRLFQA CNAEFDSQLA AQTKDNDKQD YTFILKK
