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Database: UniProt
Entry: Q5A1A0
LinkDB: Q5A1A0
Original site: Q5A1A0 
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   18-SEP-2019, entry version 94.
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;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., 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
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   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
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair
CC       by 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
CC       a FANCM-MHF complex which promotes gene conversion at blocked
CC       replication 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
CC       FANCM-MHF complex. {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40562}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. FANCM sub-subfamily. {ECO:0000305}.
DR   EMBL; CP017626; AOW29345.1; -; Genomic_DNA.
DR   RefSeq; XP_715573.2; XM_710480.2.
DR   STRING; 5476.C4YGM6; -.
DR   PRIDE; Q5A1A0; -.
DR   GeneID; 3642817; -.
DR   KEGG; cal:CAALFM_C406190CA; -.
DR   CGD; CAL0000186482; MPH1.
DR   EuPathDB; FungiDB:C4_06190C_A; -.
DR   InParanoid; Q5A1A0; -.
DR   KO; K14635; -.
DR   OrthoDB; 331426at2759; -.
DR   PRO; PR:Q5A1A0; -.
DR   Proteomes; UP000000559; Chromosome 4.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR039686; FANCM/Mph1-like.
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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1187       ATP-dependent DNA helicase MPH1.
FT                                /FTId=PRO_0000333370.
FT   DOMAIN      144    311       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      486    681       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     157    164       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       259    262       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS   1061   1069       Poly-Asp.
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
//
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