ID F0XI67_GROCL Unreviewed; 1329 AA.
AC F0XI67;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=CMQ_2506 {ECO:0000313|EMBL:EFX02577.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX02577.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL629769; EFX02577.1; -; Genomic_DNA.
DR RefSeq; XP_014172059.1; XM_014316584.1.
DR STRING; 655863.F0XI67; -.
DR GeneID; 25975503; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_2_0_1; -.
DR InParanoid; F0XI67; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000007796; 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:EFX02577.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 196..364
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 534..700
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 45..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1329 AA; 148748 MW; 26280860FD220099 CRC64;
MTDDDEFGDD IADEDLMLAY EAASAPTLSA LPVVSRPSNA AAVINQPQPV SSRQISSVGR
QMGAPRPPAK SNNSLKNIIA QVEESRTGFT DAAAELDGLP SDAFDSSQTN VGQSQRSLLA
SCRQPLRLSG QTSLRQTTLF GDRLQTEPTQ PPPSNRLYRG DFPPETPTHH KLDQEQLKTW
VYPTNLGPIR DYQFNIVKNG LFHNTLVALP TGLGKTFIAA TVILNFYRWT KDAKMVFVAP
TKPLVSQQVE ACFTIAGIPR SETTLLTGDT APALRAAEWA SKRLFFMTPQ TLQNDLSKGY
ADPKSIVLLV IDEAHRATGD YAYVKVIGFI RRFTKSFRVL ALTATPGSTV EGVQDVINNL
GVSHVEIRTE ESLDIRQYVH GRDVERFVLD PSVEIKFVQE HLSKALKPFC EKLDQQKIWY
GRDPMSLTMF GLMKARQEWM AGPARHLNQG TKYMTMAVFA VLQSVAHAIK LLNFHGIKPF
HDSMAELRST TEKDEKGPKY RKQLVGDPDF QEMMLTVERW LQEDSFESHP KIGFLKERLN
THFQDNLGSN TRAIVFSEYR DSAEEIVRTL NRCSPNIKAA IFVGQADSKR SSGMKQKQQI
EAIEKFKAGA FNVLVATSIG EEGLDIGQVD LIICYDASSS PIRMLQRMGR TGRKRAGHVI
LLLMRGKEEE KFTDAQNNYT HMQKLISDGS QFEFRFDMSE RILPRDVKPE VERRFIDIPV
ENTQDLSLPE PKKKNAARTK KAPKKIFHMP DNVETGFVKA SAVLGGPKKR NQPTLDRGPV
ETDFLADTSD LKAIMATCSA FKAFPIKNGF ENGTVFNLGH LEEVDVGTAQ FEFLQNLRPT
KYLGHGQYTR RNVRLMGRMA EQAYSQPTKN ARKYMRIPVP AFAANSDAPE ESGPDEVVSQ
TMTVEPLPKR RRVIAPATKA TQRQRVVTYG TLDEEAEKDI GEEESERRPR KFKPAVKGLT
KQRSSQFVTY ATLDKKFDED AEEEEENERW PRKSFKPAIK GLTKQRSSQF VAYATLDKDV
DKDIGAEEES ERQPKKSFRP AVKGLTKQRS SQWQSYALSG SNNRPPPISR PKQETRDKLK
APEMEEEMEE EELDEEMEII QILPTRTRRD RGGARGGGGR GGRGGRGGRG RGAAQVSYGR
LEDKGDDCMR TSDMYESDGS DSGGDLVDFI ADDDEVEMAT SSSMARVDDD DDFDESRSKG
PKKRRTGPFI SPSMPSSPPM QTINEFDSED EAPGRTTKKP KFYEPMHLSQ TLENDGIDED
GAAPVFGEKT RPLGREKQPA AAARRGRTGT LHNIEGGDDD DDDERGIFAR RPLGAQRSRR
LMNDSDSDD
//