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Database: UniProt
Entry: A0A094B6C1_9PEZI
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ID   A0A094B6C1_9PEZI        Unreviewed;       998 AA.
AC   A0A094B6C1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN   ORFNames=V494_04816 {ECO:0000313|EMBL:KFY37306.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY37306.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY37306.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-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|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:KFY37306.1}.
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DR   EMBL; JPJW01001630; KFY37306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094B6C1; -.
DR   STRING; 1420907.A0A094B6C1; -.
DR   HOGENOM; CLU_002513_0_1_1; -.
DR   OrthoDB; 12149at2759; -.
DR   Proteomes; UP000029288; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029288}.
FT   DOMAIN          120..288
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          465..633
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..839
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..902
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..992
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  111685 MW;  07D3DC8C9903DC20 CRC64;
     MATTYSEFDA DKELEGLPSD AFSSSPEPDA RPATPQSPPE SQLLPRQRIV APLTGLRQTT
     LFGGRAADNP LPSSQVNKVH SYRVDLPPEA PTHHSLDTEA LKTWVYPTNL GAIRDYQYSI
     TKNGLFNNTL VALPTGLGKT FIAATIMLNY FRWTKDSQIV FMAPTKPLVA QQVDACFNIA
     GIPRSATTML TGEISPALRA EEWTSKRVFF MTPQTLDNDL RTGLADPKKI VLLVVDEAHR
     ATGNYSYVKV IEFMRRFTKS FRILALTATP GSSVEAVQDV INGLEISKVE IRTEESIDIQ
     QYVHQRNIDQ VILDPSEEIV KIQDLLSKTL KPLVDQLCGH NAYYNRDPLS LTPFGMLKAQ
     ETWMKSPAGK TANFGLKGMM RSLFTVLASV SHGIKLLNFH GVGPFFQTMK DFRSEAEERG
     AKLGKYKKQI MDSPHFKKMM DLVNMWINKD DFIGHPKLTY LCDTVLNHFL DAGDGRREDG
     APPSSTRIIV FCEYRGSAEE VARVLNRHAP MVRASVFVGQ AGTKHSDGMN QAKQIETIRK
     FKEGIFNVIV ATSIGEEGLD IGQVDLIVCY DASSSPIRML QRMGRTGRKR AGNIVLLLMR
     GKEEDNFIKA KDNYEAMQRM ISDGSRFNFR FDLSTRIVPR DIVPAVDKRD IEIPVENTQD
     PSLPEPKRRG KRAPKRPPKK FNMPDDVETG FQSVASMISG KKTPRKSSSI VQAIEEVVSE
     LAEDQQMKKP PLESVMLSPS DEVRLLETYQ NIAGGFETLD VSVPELNKHP KLQRSLRPTK
     RVKHGAASKR LVNMLQSMQT IDQDTLDRWE RIQDDPLPLR ARENSPDLPT SQSSIGPADF
     FSLSAEESET ETPPRRNRAA PKPRYRENLD PAPIDSFSTL SSSAGLPYPD DDEEDSDLDD
     FIVRDDETPK AYPARGRETI FSSVSPPPKA RPFFEPTQFT ATQDSMDGED ELPDISTLVG
     KFGRSAGKPV EVREEEEVGG GRRKRRRVVV EDSDDDDE
//
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