ID A0A2R6S504_9APHY Unreviewed; 730 AA.
AC A0A2R6S504;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
DE Flags: Fragment;
GN ORFNames=PHLCEN_2v776 {ECO:0000313|EMBL:PSS37374.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSS37374.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSS37374.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSS37374.1,
RC ECO:0000313|Proteomes:UP000186601};
RA Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA Riley R.;
RT "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT centrifuga.";
RL Submitted (FEB-2018) 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|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|RuleBase:RU367027};
CC -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC MHF complex. {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:PSS37374.1}.
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DR EMBL; MLYV02000051; PSS37374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6S504; -.
DR STRING; 98765.A0A2R6S504; -.
DR Proteomes; UP000186601; 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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186601}.
FT DOMAIN 28..196
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 378..559
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 566..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 730
FT /evidence="ECO:0000313|EMBL:PSS37374.1"
SQ SEQUENCE 730 AA; 82309 MW; 40BC6FA08E68D0E9 CRC64;
MKLHPNLLAA QRWLYPLNQQ RRDYQFNIVK RCLFENTLVA LPTGLGKTFI AGVVMLNFYT
WFPEGKVVFV APTKPLVAQQ IEACHKTCGI PGSHAAELTG QNSRAVRSRT WQEKRVVYMT
PQTLMNDLKT DNCDPQDIVL LVIDEAHKGT GDYAYAQVIR YMMAKNPHFR VLALTATPGG
KPDTVQAIVD ALHISHIEIR DEGSLDLKPY LHKKHIKQHI IEMSDDVRKV RDILSEAMAP
HIKKLVSAKI LHSHPSPVML HPFSCNMAMQ GLHAGRNGAA WAFSALQKLS GLARAMGYLL
ESTTNQCYIC LTALVTGDNG TTKQGKQKQN LFKSDPQVQA VIKELEAQKS RLGGFSTHPK
MDRVKTLLVE HFAQKRYDKE DADANGGSEE LTGDSHVMIF VSFRQCVDEI VEFLNLESPL
IRAIPFIGQG ADKAGKRGYA QKEQLEVIQK FKSGQFNVLV STSIGEEGLD IGEIDMIICY
DAQKTPIRML QRVGRTGRKR DGYVHVLLSE VREERNWDKA HVNYEDVQRF IIRAEQLELY
EDVERLLPEN MKPECIEMEM EIEEYTREEP KAKKGPLPKR PPAKRQPRND DAMRKVPTGA
SSAFVSVKDL TLKGTKKRKK KGSALIEFDP HAGEDDSDDE EIEAGIFGPR RTQSMPESSK
QPRQKKLRQS TTMATKEQEK SQATKISHKK KAASIEDLTN NQLEHDGTDD IDDREIEMGL
SSAHLELLSK
//