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Database: UniProt
Entry: F4NSE6_BATDJ
LinkDB: F4NSE6_BATDJ
Original site: F4NSE6_BATDJ 
ID   F4NSE6_BATDJ            Unreviewed;       581 AA.
AC   F4NSE6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN   ORFNames=BATDEDRAFT_9192 {ECO:0000313|EMBL:EGF84245.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF84245.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF84245.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) 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|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; GL882879; EGF84245.1; -; Genomic_DNA.
DR   RefSeq; XP_006675092.1; XM_006675029.1.
DR   AlphaFoldDB; F4NSE6; -.
DR   STRING; 684364.F4NSE6; -.
DR   GeneID; 18244432; -.
DR   HOGENOM; CLU_002513_3_2_1; -.
DR   InParanoid; F4NSE6; -.
DR   OMA; HRAVGNY; -.
DR   OrthoDB; 12149at2759; -.
DR   Proteomes; UP000007241; 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   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   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007241}.
FT   DOMAIN          44..212
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          401..563
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGF84245.1"
SQ   SEQUENCE   581 AA;  65595 MW;  356D7B130061EAD1 CRC64;
     MANQIQQGDP SAVSSLNTHV IDEKELETWI YPINYPLRDY QFNIISRALF ANTLVALPTG
     LGKTFLAAVV MYNYYRWFPE GKIIFMAPTK PLVAQQIEAC FKITGIHQDM TYELTGTTKS
     ETRIGIWKQK RVFFLTPQVM QNDLRSAACS ADKVVLLVVD EAHRATGNYA YCEVIRELSK
     ASSPFRVLAL SATPGSDMKA VQHVVNNLLI QHIEIRTEDS FDIRPFIFSR QIEEIIVSLT
     PQITRIVDAF AKVVSIFLVR LCNHGVFYEK DPRAVSRYAL LDARKRWIDN HKDANRAQIS
     SIMNDSGICM AMCAALQQLQ TYGIRSFYDT VSSFLAEAPS EKNSRSRSEL VENSDLKALM
     IHVNEITKSP DFSSHPKLDR LVAVVLEHFS KELPDNGDEG SSDASLSKSR VMIFSQYRDN
     VDEIVTKLNQ HHPFLRVMSF IGQSSSKSGK KGKGFTQKEQ LEVISKFQSG NYNVLVSTSI
     GEEGLDIGDV DLIVCYDAQT SPVRMLQRMG RTGRKRQGRI VVILSKGKEE EIHRKAQAQY
     KSIQRAIMDG QGKRIQMYSG NLSRIIPSNA RPVCDKRELE I
//
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