ID E4ZXD1_LEPMJ Unreviewed; 1323 AA.
AC E4ZXD1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=LEMA_P024930.1 {ECO:0000313|EMBL:CBX95341.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929127; CBX95341.1; -; Genomic_DNA.
DR RefSeq; XP_003838820.1; XM_003838772.1.
DR STRING; 985895.E4ZXD1; -.
DR EnsemblFungi; CBX95341; CBX95341; LEMA_P024930.1.
DR GeneID; 13288353; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_1_1; -.
DR InParanoid; E4ZXD1; -.
DR OMA; EMEMCMD; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000002668; Genome.
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:UP000002668}.
FT DOMAIN 359..527
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 695..868
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 21..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 147570 MW; 9F6CE50ACB314E40 CRC64;
MADSDDYGDE FDDTEFLYAA TQAERENTPS AFQPSPRPAK RRKVNQTVDD RPKPIPRHHN
QQSAQRRRRG PFISSDDDDD DDDSDAITRC SLTSSGSEST HDSPHVQENH RDAQHARRKQ
RTAARRKHVL DSPNQQHSPV KETVAQKRKE RIHVPTTHLD MTDMFYTQPP QEHSPPWKPR
GAIWAKSKTT IGVHKPNEPA RWTALDAMKT MSLPGRNSLS SRPQPQAPPS PGTLNSPVQT
EPSPQLPLVN AATIPDDFTL ELEDLPSDAF ASSSSSSPQK QPSARKQVVA PQASLRQTTL
FGRAAVNADL PPSQAKNRYS FVQDQKEEPP THHKLNPVAT RTWVYPTNLG TIRDYQFNIV
QRGLFNNLLV ALPTGLGKTF IAATIMLNWY RWTVDSQIVF VAPTKPLVAQ QVQACFKIAG
IPRSATTMLT GNVQTGLRAE EWKEKRVFFM TPQTLQNDLK SGYADPKKIV LLVVDEAHRA
TGGYAYVEIV SFLRRFNDSF RVLALTATPG ANVEAVQKVI DGLDISRVEI RTENSMDICS
YVHQRSVEKK VFQNSDEMEM CMDLYRQALQ PLVNTISGLN AYWSKDPCDL TPYGCQQAKS
KWTLEAGRHA NQGVKSIVHA VFAILSSISQ GMELLKYHGI GPFHVKMKDF QNESQKSKSK
YRKQILDSDA WKKLMSRLQG WMTDDNFVGH PKMEYLQEAI LEHFANAEDG HNANGASSSQ
TRVMVFANFR DSTDEIARIL KRHEPMIRPR VFVGQAAGKN SEGMTQKDQL DVIEKFKSGV
YNTLIATSIG EEGLDIGEVD LIICYDSKAS PIRMLQRMGR TGRKREGKII MLQMNGKEEN
DANKAKDSYE KMQELIAKGS HFNFHDDKSR RILPPDVKPV VDRRVVEIPP ENSQYDWLPE
PKKGRRSKKP PKKFHMPDNV ITGFVTAGRM GEELVSKGRG KKVATPVYPS EEIIEVPSLE
SVVLDDAGLL DLERRYQTVF DDDDAPMVGA LNLGLHPERQ RALIYANHNT GPGRATRAFA
ATMQRMHDVD SDRVESFKNN LHYSDYESDI SHDYLVSDAE PAPAEMDDAD DPWADDDPAS
QTLPTIKVTK AKPGPKPKPK TMAKETDESR KKAKATPKTP AARGRPRKEA LAVETPIRQS
KATSATPHTA TPNWRATGLA QEGEESSPPP TDPRFHIASQ ADTVGSDDTL GEDEVEDTQA
YLMDSELASF IVEDGDVEVP ASSLPSLDLH GVGQGTQAIV KAAQPKRTPR REKIFTSDVT
DDDAVVSSDS DDEVSLVKSR AGTSKKAAVI VADSDSEGGS EEEERVLPRI RQRRVIDDEE
DDD
//
