ID A0A165JA29_XYLHT Unreviewed; 1122 AA.
AC A0A165JA29;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=L228DRAFT_216026 {ECO:0000313|EMBL:KZF25957.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF25957.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF25957.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF25957.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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}.
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DR EMBL; KV407454; KZF25957.1; -; Genomic_DNA.
DR RefSeq; XP_018191512.1; XM_018330106.1.
DR AlphaFoldDB; A0A165JA29; -.
DR STRING; 1328760.A0A165JA29; -.
DR GeneID; 28895243; -.
DR InParanoid; A0A165JA29; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000076632; 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, ECO:0000313|EMBL:KZF25957.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT DOMAIN 237..405
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 581..751
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 123988 MW; DE13451958B03438 CRC64;
MYSDDGDDDG FGGFAGIDDE DLLNAATQYD HSTTRTTARQ KGGQTGRVHQ SSTTPIIAAA
QSRPALPTSL YVRAAESKRQ RLNVVEKTGC EASAGAPLAH RGDDHASLSA HPAAYLTTDD
YGSDELDEAD DTRLDPPSSA TKAGRTPSIF LSSQSSARTP THRTITLGPQ TNLRQTTLWG
GALQTNVQNS QGAAPRRAWP LANQDELPTH HKLDPEALKT WVYPTNLGTI RDYQFNITQR
GLYHNLLVAL PTGLGKTFIA ATIMLNWFRW APESQIVFVA PTKPLVTQQV EACFGIAGIP
KSQTTLLTGS TPPGVRAEEW LKKRVFFMTP QTIINDLKSG TCDPKKIVLV VVDEAHRATG
NYAYVEVVNF LRRFNPSFRV LALTATPGAT VDAVQQVIDG LGIARVEIRT EESLDIRQYV
HSRNIETFIF DPSEEMTMVM DLFSKALQPV LDKLNQQNAY WSKDPMNLTP YGLTQARQKW
MLSDAGRSAP MGLKGMMFSI FSILATLAHA IDLLKFHGIG PFYHNLVGFK NDTGAGEKGS
KYRKQIIEST HFQQMMNRVH SWVGNENFVG HPKLEYLQSV VLNHFLDAGE GGPAASGAPP
AHTRVMIFVH YRDSAEEVVR VLKRNELIRP HVFVGQAHSR GSEGMDQKKQ LDVVHKFKIG
VYNTLVATSI GEEGLDIGEV DLIVCYDSSA SPIRMLQRMG RTGRKRTGNI ALLLMRGKEE
NSFVQAKDNY EKMQHMIASG AYFNYHEDKS FRIVPKEIQP VVDKKAIEIP VENTQPDLPE
PRKRAAPPKR PPKKFHMPDG VRAGFVRASR LQGETNSDGT TEEEAAFQVS KQSRAAQLVE
LEALPDLDEV LLSNREETEL SQRYQQVSGG DEVQVVSMPR LNAYPARQRI SSYTKLLKHG
QVTKRTVRLL HKMHSIGKEQ VEQLEENVHM EDLEGDPIEL DGLAVKLSPE PEVEDAQAFP
SQKQLSSQSL RRKQHGSYPG LRTELVSLEA ESSTDESATS GAHRGQGPTQ ETDTDMDDFI
VPDEEDVMPA ESAASSPPSV LGSSKHPYSS PRQILGCTTA ADSEEDLPDI DTLVNCPTDG
RDPSPISSIS NAKLSSSSPV RNLHRNKRAR RNIVDDSEDS DD
//
