ID MPH1_ASPCL Reviewed; 1119 AA.
AC A1CS00;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=ACLA_031540;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW08421.1; -; Genomic_DNA.
DR RefSeq; XP_001269847.1; XM_001269846.1.
DR AlphaFoldDB; A1CS00; -.
DR SMR; A1CS00; -.
DR STRING; 344612.A1CS00; -.
DR EnsemblFungi; EAW08421; EAW08421; ACLA_031540.
DR GeneID; 4701240; -.
DR KEGG; act:ACLA_031540; -.
DR VEuPathDB; FungiDB:ACLA_031540; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_0_1; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000006701; 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 CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR Gene3D; 1.20.1320.20; hef helicase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
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; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 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; P-loop containing nucleoside triphosphate hydrolases; 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..1119
FT /note="ATP-dependent DNA helicase mph1"
FT /id="PRO_0000333363"
FT DOMAIN 313..481
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 651..825
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 112..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 429..432
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 180..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1119 AA; 125004 MW; 9E3A3707C1EE3382 CRC64;
MSDSDNGSAD SFDDEIDDFV VTTPRQSAGA WMLATRKASY DKNIVTRRLE SDSVNALGSD
SFIDRDEEDE LPSPDHALFE GIDFENVEKT SRYKVFVPKH SNYQENIFVT QLTQPPSPPE
MIRGPRWKKP DPEPPTPKPP ATMTIPASRA DQYRDDEKEI EAAIAASLRS FEEENCGPTS
AMVDKSSATR TAAVPSNAQK QHVADVPFDV DDIPDDAFDS DLSLSPPRSN SQAALRGPVQ
SQFSTNRPLG LRQSTLFGMT ARASEASIPR GEQVFSPPDK NEAPTHHKLD EEALNTWIYP
TNLGKTRDYQ FNITQRGLFH NLLVALPTGL GKTFIAATIM LNWYRWTKSS QIIFVAPTKP
LVSQQISACF GIAGIPRSQT TMLTGEAAPG IRAEEWKAKR VFFMTPQTLI NDLKSGIADP
KRIVLLVVDE AHRATGGYAY VEVVKFIKRY NKSFRVLALT ATPGSTVESV QAVIDGLDIA
KVEIRTEQSL DIREYVHARN TDVQTFQNSD EMVLCMDLFS RTLQPLVDQL CSLNAYWGKD
PMALTPFGLT KARQQWMLSD AGRNANYGLK GKVNAIFTVL ASLAHAIDLL KYHGITPFYR
HLVHFRSNTD GQKGGKYQRQ IVQDESFKKL MNHLQPWTKN PEFIGHPKLE YLKQVVLNHF
MDAGEGSGAD GNHTRSATRI MVFAHFRDSA EEIVRVLKRY EPLIRPHVFV GQSSAKGSEG
MDQKTQLSIV QKFKKGDYNT IVATSIGEEG LDIGEVDLIV CYDSSASPIR MLQRMGRTGR
KRAGNIVLLL MQGKEEESYI RAKDNYEKMQ EMIASGTRFA FHDDTSPRIL PPGIRPTADK
KQIDIPVENT QADLPEPKRR ARPPKRPPKK FHMPDDVETG FSKASSLTGN KGAKKTDKQT
TIRKPTPEPV AIPALEEVLL TPSQQNDLER RYCHIGGTSP QFIRNPRVDA YPRLQSVPRP
TRAVKHGALT SRMIGTLQKM HQVGADCESR YKDILALESS KRPEDSVLVQ ESARPRQNKK
LSVGVSRPSK AQPPQTQSTL APIREGLVDD GILEPTVPNE LASLLGHQNP KPFYSSQISQ
DDLESDFDLP DFDTLINRNA ERTTPRKRNR FVLGDDSDE
//
