MPH1_ASPTN
ID MPH1_ASPTN Reviewed; 1100 AA.
AC Q0CWI2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=ATEG_01952;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU36914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476596; EAU36914.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001211130.1; XM_001211130.1.
DR AlphaFoldDB; Q0CWI2; -.
DR SMR; Q0CWI2; -.
DR STRING; 341663.Q0CWI2; -.
DR GeneID; 4316557; -.
DR eggNOG; KOG0354; Eukaryota.
DR OrthoDB; 989616at2759; -.
DR Proteomes; UP000007963; 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 InterPro; IPR003903; UIM_dom.
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..1100
FT /note="ATP-dependent DNA helicase mph1"
FT /id="PRO_0000333368"
FT DOMAIN 317..485
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 655..829
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 433..436
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..59
FT /note="Polar 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 121..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1100 AA; 122805 MW; D4C60033FB2FBA3A CRC64;
MSDSDDYLQD DPDDQAFDDF ADVASSPPPP KRRRLQARNQ TRNTTSRRNE DNSVASDSDS
FVVDDDDASK TDELPSPSQA SYHFADHPEN EASSKYKIFV PKRNNPQENI FVTQLTQPPS
PPEMIRGPRW KKPDPPPPPP PAPTKPTPKT TRGPGHEDYG DDEDLDAAIA ASLASFEEEN
SRLSFSTAQN SPPAPVASDN APTNTAQTES FDFLDDIPDD AFDSDLSLTP PPPAPPSNSS
RPSSFMQSSN RPLGVRQTTL FNMATRNQAP QPPQGEQVFA PPEKVEAPTQ HKLNQEAIST
WVYPTNLGKT RDYQFNITQK GLFHNLLVAL PTGLGKTFIA ATIMLNWFRW TRDAQIVFVA
PTKPLVAQQV SACFGVAGIP RSQTTMLTGE AAPGIRAQEW QDKRVFFMTP QTLINDLKSG
IADPKRIVLL VVDEAHRATG GYAYVEVVKF LRRYNQSFRV LALTATPGST VESVQAVIDG
LEISKVEIRT EQSLDIREYV HARNTEVQTF KNSEEMVLCM DLLSKTLQPL VDQLRTLNAY
WGRDPMALTA YGLTKSRQQW MLSDAGRNSS FGLKGKVNAI FTVLASLAHG IDLLKYHGIT
PFYRHLLHFQ GNTDGQKGGK YQRQIVQDEH FKKLMNHLSP WTKNPEFIGH PKLEYLKQVV
LNHFMDAGEG SAGAEGASQS TTRVMIFVHF RDSAEEVARV LKRYEPMIRP QVFVGQASAK
GSDGMNQKTQ LGVVQKFKQG TYNTIVATSI GEEGLDIGEV DLIVCYDSSA SPIRMLQRMG
RTGRKRAGNI VLLLMEGKEE ESYIKAKDNY EKMQQMIASG TRFTFHDDKS PRILPPGVKP
IVDKRHIDIP EENEEQALPE PKRRGRVPKK PPKKFHMPDN VITGFTKASS LAGGSKRTAQ
DKRKARTPTP EPVDIPALED VILTAEQQRE LEHRYCTIGD TSPEVIRTPR TDAFPRLQLV
SRPTKVVKHG SLTRRMIDAL QKMDKTSSDC EGRFKEVLAL ESRRPAEESL IHQSISRPGN
KKRLRKGRSG QPEPRLPPSR VHEEKDEDLD GSQPISPEQL LSSFTDRQGP KPFSSSPRSE
NLELDADFEA PDLDTLLGRR
