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Database: UniProt
Entry: F0XI67_GROCL
LinkDB: F0XI67_GROCL
Original site: F0XI67_GROCL 
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}.
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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
//
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