ID A0A0A1UXW0_9HYPO Unreviewed; 1077 AA.
AC A0A0A1UXW0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=X797_003990 {ECO:0000313|EMBL:EXV02867.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV02867.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXV02867.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV02867.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) 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:0000256|ARBA:ARBA00003813, ECO:0000256|RuleBase:RU367027}.
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:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU367027};
CC -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC MHF complex. {ECO:0000256|ARBA:ARBA00011390,
CC ECO:0000256|RuleBase:RU367027}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU367027}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889,
CC ECO:0000256|RuleBase:RU367027}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXV02867.1}.
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DR EMBL; JELW01000004; EXV02867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1UXW0; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_1_1; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000030151; 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-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EXV02867.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 169..337
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 513..683
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 22..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..944
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 121125 MW; 47E528700E709930 CRC64;
MDDDEFGEDF VDEDFLEALD QVSSSNRARP VSQPSSNEAQ FENKTWTKSN PLAAAAQELE
DLPSDAFSSP EPEKSASVAA APTSRKASNG PRVQNGLTRT ASGNFRQTTL WGTEVREDAP
FRTQAPIQRV FRADVPHEEP SHHELDRKEM ETWVYPTNLG AIRDYQFSIV KNSLFNNTLV
ALPTGLGKTF IAATVMLNFY RWTKSAKIVF VAPTKPLAAQ QIDACYNIVG IPRSHTTLLT
GDIQPALRAE EWEKRRVFFM TPQTLLNDLS HGYAEPKSIA LLVIDEAHRA VGEYAYAKVT
KLIRRFSKSF RVLALTATPG SKIETVQEVI DNLGISHCEI RTEESIDIRQ YVHERNIEKM
VLDPSDEMNL VSELFTEALK PLVDKLGSQN IYYGRNPMAM STYGLMQVQK EWFATRGRHA
NQGVQFMMRA IFSVLTSLAH SIKLLNFHGI KPFYDNMKDF RSEQEGKGEK GSKYKRQLIE
HSSFQKMMDH ISRWLRTDGF VGHPKLAALV DCVLNHFMDQ GEGSTTRVIV FSEYRDSAED
IVCQLNKHQP LLKASVFVGQ ADGKRGEGMK QAQQIQTIEK FRKGEFNVLV ATSIGEEGLD
IGQVDLIVCY DSSASPIRML QRMGRTGRKR AGNIVLLLMR GKEEDQFAKS KDSYESMQKL
ICEGSRFNFR FDLSMRIVPR EIRPEVDKKF VEIPVENTQD PSLPEPKKRR PAAGKKKPPK
KFHMPDGVET GFQKLSYYMK SGPKPEQSKP KQNPELNDLE SIPDLSSVVL TEEELKELDR
SYRDLPFNHS VVEETDMPSM TAYPLFQRQL RPVANLKHGT CTRRFVKLLA KMGTEPESLV
RQCRSTDTSR FKDITVRAFI ASDGEPDVDD TSDSGTKKRS TRQRSVEADN EESQPPRGKR
KKISTTSIAG LSELEDDSET PGMNSRARKR TKKPKSKRKG RKTKQRTGIN SDELGDDCER
DSDLIENGGS DDGADLLDFV VADNQGTSSM VGSQVTSPTT ASAQSTPKAE SKQPFYVPTR
FSATQESDDM PDVDTLVKRK AFQKVISMDA SDSDLEDLAA KRPARGRRQV FDSDSDA
//