ID A0A316VSX9_9BASI Unreviewed; 1466 AA.
AC A0A316VSX9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=IE81DRAFT_348991 {ECO:0000313|EMBL:PWN40696.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN40696.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN40696.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN40696.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ819409; PWN40696.1; -; Genomic_DNA.
DR STRING; 1522189.A0A316VSX9; -.
DR InParanoid; A0A316VSX9; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000245783; 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:0003676; F:nucleic acid 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
DR InterPro; IPR044749; FANCM_DEXDc.
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; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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, ECO:0000313|EMBL:PWN40696.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245783}.
FT DOMAIN 372..540
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 702..874
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 160441 MW; 5FBE0DA591765FE7 CRC64;
MSSAVAGAAN EHVADTDDFD FGDGDDFELD ESALLAIEAE ANSMRAAGPS KPRAPPSAPA
LPCTPKRAAT LPRRLTQTSG RALLAFETPL VPRRAAFLAD DHMQPTPPTS SPHSNFGTGS
QSSSSRRRSQ SPREDLSMAP PAKPPSSSIQ EVSFNAGPDQ AKGKERAQLD FDDFDEDGDA
SLWDDALLRG VDAIEANLKV GGSAQAVSDC EAHIAARSTM RQRDLFGQIV EDLPPQSTNR
EWDKDAYMRA AGFGGSSVGV LSQTAGQSSS ASKTGPRVAK TKQWDRTAYA KTGRRYRKDT
EAMRRKKNGL PVPEDDEEGQ VDWDNARPYE PANEARDVIP ELQPMKLRID EEAAKEWIYP
TNKEKRSYQF DIVQKALYSN TLVALPTGLG KTFIAAVVIL NYFNWFPDGK IIFVAPTRQL
VAQQQYACHR ICGLPWETAV ELTGATKRGL RNDQWETKRI FYMTPQCFEN DLCSSAVDAR
DVCCVVVDEA HRATGNYAYG NVIRYLTQRN PYFRILALTA TPGNKSEKVQ EVVDNLHISH
IEIRTEEAID IRTYIHKKHE HPVLVPMRDE ASEVQAAWAK LMIPVVDPLF KARLIHSADP
VSLHPFALIS AGRNPGNKPI FAKNGSLRGK LGTLQAMAAA MQLLNEHSIT MFRTRVQDFA
AKKRPGINQD SAEFKRFRIQ LDSLDQTPEN MLHPKMMYLR DVVKAHFVAE QEQGRSSDTR
VMIFCSYREC VKEIVEFLNT IDDIKAVQFI GQSADRTGGS GMNQKAQEKI IFQYRQGYYN
VLVATSIGEE GLDIGEVDLI VCYEAVKDSV RMLQRVGRTG RKRDGKIVVL MSEGREEKLW
AQSKDNYKSV QKDITRGLNL ELFGDVPRLV PKHIKPTVVM RDVEQPDFIP GAVDLAQTSS
NAIKSAAKNG KDKGKNKRVA EDMPEGALMN FIAASELRKD GKLKRKSSGS AKTIRRKSGG
KRRDTSSSEE SPHERIAAAP ALALSDDSDD DLLAGGIDFR SAATATKRTN GQGPKGIMTA
TSLQGSASHP KGRRLGVRRQ PSSAALLSSP LCNSLVANAA GLPDGNDQRA FALASGGETL
HHTRAKQDCC PSSSPAQTGC GIGKPHPLVA ALLEQHVASR DDESAPQDAI EAADAAMLVD
GGTSDVEDSF DDLEPLPLLS TQNSVSVLDA PPLPAAPAIR SAPKSAFDSG KGATTRTQGD
STKNALLTSD DTPFKPQVRR FPARPSAPGS SPLQMPPPAA RPKKRLRRGV VGCDSDQPDA
GDGIVCKDRP CGGRASSSKP AAADSRAVCQ ANGPKKHKRQ KKRISNSPTS RMLFRRSAER
DTDEEIHREL DENDEGLDTE DDADSSDREH VGHFQPTQAP RGYNQQAMYA QSLLTQAAPK
MGLDRPQRKA EFYGGRYGAL ASDEHEESPI RVARGSHRQR REIESTHAEE PSDSEDNYEL
GSFIVSDHEQ IEMASSSQRL PQTSSQ
//
