MPH1_CANGA
ID MPH1_CANGA Reviewed; 1052 AA.
AC Q6FPQ3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=CAGL0J01980g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380956; CAG60740.1; -; Genomic_DNA.
DR RefSeq; XP_447791.1; XM_447791.1.
DR AlphaFoldDB; Q6FPQ3; -.
DR SMR; Q6FPQ3; -.
DR STRING; 5478.XP_447791.1; -.
DR PRIDE; Q6FPQ3; -.
DR EnsemblFungi; CAG60740; CAG60740; CAGL0J01980g.
DR GeneID; 2889816; -.
DR KEGG; cgr:CAGL0J01980g; -.
DR CGD; CAL0133376; CAGL0J01980g.
DR VEuPathDB; FungiDB:CAGL0J01980g; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_0_1; -.
DR InParanoid; Q6FPQ3; -.
DR OMA; IRPHIFI; -.
DR Proteomes; UP000002428; Chromosome J.
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; IEA:EnsemblFungi.
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:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR GO; GO:0007535; P:donor selection; IEA:EnsemblFungi.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR GO; GO:0060543; P:negative regulation of strand invasion; IEA:EnsemblFungi.
DR GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
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..1052
FT /note="ATP-dependent DNA helicase MPH1"
FT /id="PRO_0000333371"
FT DOMAIN 89..256
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 432..649
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 495..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 204..207
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 503..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1052 AA; 120576 MW; 9A3496875A22095A CRC64;
MEDSDFDDAE LDELYEKAIN RRVNETLIRR SLPVQRDLQN GVVPGQDTYY EEIRTEVTFG
PTHHQLNEEL LHSYIYPTNF EVRDYQFDIV RKGLLQNILC AIPTGMGKTF IASTVMLNFF
RWTKTAKIIF TAPTRPLVAQ QIKACLGITG IPHDQTAILL DKTRKNREEI WANKRVFFTT
PQVVENDLKR GVLNPKDIVC LVIDEAHRAT GSYAYANLVK FINRFNSSYR LLALTATPAT
DIEGVQEVVN NLNISKIEIR TEESMDIVKY MKKKIKDRVN IQTTVEIENI VEQLGIAILP
VLNQAVELGI YESCPPSAIN AFKAMQKSQA IIMNPSIPEG IKWRNYFILQ LLNHVGQMLK
RIKIYGIRTF FSYFQNKVKE FTTKYDLGKS TNKIAAGFYY HPMIQAITKE CEEKIKDPNF
LGHGKLEHLR DELTQFFYEN PFESRVIIFT ELRESALEIV KCIDSMENSE IRPHIFIGQA
KGKEGFDEVK FVRKHGPKGR KKSDREKRLE EERRMDEEKK QAALQEKLER TSRRTGSSEE
AQLSGMNQKQ QKEVIKKFKS GLYNVLVCTS IGEEGLDIGE VDLIICYDTT SSPIKNIQRM
GRTGRKRDGR IVLMFSSNEA SKFDQSMNDY YNLQKLISQH LVQYRKSDRI LPPENQEPEC
EKKFIEVSEE DQELNNMEDT DDVIRFATQC MLGKIPKTKK GRDKGKAKKG KTFFMPDNVI
TGIITANNLV RKRKSAQNGS GAALLDSIVN DDIDLEDEDG QVEILDVDQE VNRRLASNAV
QKTNDMALQI RNEETPEIGD TRNKAKASSS MKVKKEPTMA VDHSDDEEDL PLSRHVERAS
RETAKEVPNA TNVAEKPFPP LEFGVQRPSK RQRLQPEVQP EVQPEVQPEV QPEVQPEVQP
EVTVKPEVKI KTEEGSKLYK NIFFSDEGFL QPHEKELFLS KYNPEDATVT IEPVPRFVRA
HGRVKHSKRT EQLITLFEDM NHNRVARTIE MNKLRGIARR LHTVSQSQGQ SNSQSQAHST
SQKSQQASQK DRSSQDKDLT NSELEDLLDS DF
