MPH1_ASPOR
ID MPH1_ASPOR Reviewed; 1129 AA.
AC Q2URJ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=AO090005000804;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE55820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP007151; BAE55820.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001817822.2; XM_001817770.2.
DR AlphaFoldDB; Q2URJ5; -.
DR SMR; Q2URJ5; -.
DR STRING; 510516.Q2URJ5; -.
DR EnsemblFungi; BAE55820; BAE55820; AO090005000804.
DR GeneID; 5989767; -.
DR KEGG; aor:AO090005000804; -.
DR Proteomes; UP000006564; Chromosome 1.
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..1129
FT /note="ATP-dependent DNA helicase mph1"
FT /id="PRO_0000333367"
FT DOMAIN 331..499
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 674..843
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1129
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 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1129
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 1129 AA; 126479 MW; DD55E7B5ED0D7CEE CRC64;
MTGSDDSSVD YFREGFDDIT DDEFPDATRN AVGSSPRPAK RRRRDGTASD VRRRPSENRE
SQRYSDGGSP QTGSDSFVVD DDEGNYDELQ SPSQDSYFED AEAPSKYKVF IPKRSNIQEN
IFVTQLTQPP SPPEMIRGPR WKKPEPSIAR ASTIPTQTIG EGRAAPNAPA ASVDDYDDED
LNAAIAASLE SFENEQSRPP PSNTKAPTHQ PITRSPTVQN EGATDTSFLL EDIPDDAFDS
DISLSPPTRA QQQPATRQFG QSSNRPLGVR QTSLFDMTSR NQTDQPPIGE QVWSPPQKDE
PPTQHKLDHD ALSTWVYPTN LGKTRDYQFN IAQKGLFHNL LVALPTGLGK TFIAATIMLN
WFRWTESAQI IFVAPTKPLV AQQISACFGI AGIPRSQTTM LTGEAAPGIR AEEWQNKRVF
FMTPQTLIND LKSGIADPKR IVLLVVDEAH RATGGYAYVE VVKFLRRYNQ SFRVLALTAT
PGSTVESVQA VIDGLDIARV EIRTEQSLDI REYVHSRNTE VQTFKNSEEM VLCMDLLSKT
LQPLVDQLRT LNAYWGRDPM MLTAFGLTKS RQQWMASDAG RNAHFGLKGK VNAIFTVLAS
LAHAIDLLKY HGITPFYRHL LHFQSNTEGQ KGGKYQRQVV QDESFKKLIN HLQPWTKNPE
FIGHPKLEYL KSVVLNHFMD AGEGSNGEAS DSQSSTRIMI FVHFRDSAEE VTRVLKRYEP
MIRPHVFVGQ SSAKGSEGMG QKTQLDIVQK FKKGTYNTIV ATSIGEEGLD IGEVDLIVCY
DSSASPIRML QRMGRTGRKR AGNIVLLLME GKEEESYIKA KDNYEKMQQM IASGSRFTFH
DDISPRILPA GIRPVADKRH IDIPDENAEQ SLPEPKRRGR APKRPPKKFH MPDNVETGFT
KASSLTAGPK SKAEKSRKPR TPTPEPVEIP ALEEVVLTSA QQRELEQHYR NIGAASPQFI
RNPRNDAFPR LQLVARPTKV VKHGSLTRRM IGTLQKMNNV GPDCGDRFKK ILALESARQG
DSVIPNRSPR HERRRRLSKT KPRYNHLSTS VDKETLSTED SQLVTPEHLL SSVVKGQKQQ
PFYSSQRSKD DDSDDNFDPP DLATLLTRSA ERNNAHKTSR FVVSDDSDD
