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Database: UniProt
Entry: A0A0A1UXW0_9HYPO
LinkDB: A0A0A1UXW0_9HYPO
Original site: A0A0A1UXW0_9HYPO 
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
//
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