ID B2WCF2_PYRTR Unreviewed; 1053 AA.
AC B2WCF2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=PTRG_07661 {ECO:0000313|EMBL:EDU50580.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU50580.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231622; EDU50580.1; -; Genomic_DNA.
DR RefSeq; XP_001937993.1; XM_001937958.1.
DR AlphaFoldDB; B2WCF2; -.
DR STRING; 426418.B2WCF2; -.
DR EnsemblFungi; EDU50580; EDU50580; PTRG_07661.
DR GeneID; 6345933; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_0_1_1; -.
DR InParanoid; B2WCF2; -.
DR OMA; EMEMCMD; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000001471; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EDU50580.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 156..324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 497..682
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 116661 MW; F607A6A75321179D CRC64;
MALPGRQSIS SRPTPQAPSS PDLLSSPIEL EETPRLETAA GKRDTATEYD FSTELADLPS
DAFSSSSSSP QKQGEVEVAG ARRHLVTPQT GLRQTTLFGR AGVDGQIAPS QANKRYNFVV
DQKAEPPTHH KLNPEAIKTW VYPTNLGTIR DYQFNIVQRG LFHNLLVALP TGLGKTFIAA
TIILNWFRWT LDAQIVFVAP TKPLVAQQIE ACYKIAGIPR SCTTMLTGGV QTGLRAEEWK
DKRVFFMTPQ TLLNDLKSGY ADPKRIVLLV VDEAHRATGA YAYVEVVSFL RRFNTSFRVV
ALTATPGADV ESVQKVIDGL EISRVEIRTE NSMDICSYVH QRKIEKQVFQ NTDEMEMCMD
LYSEALQPLV NTVAGLNAYW SKNPRDLTPF GCQQAKKKWF MEIGRNANRG LQSTVHTIFA
ILASISHGMD LLKFHGMGPF YVKMKEFQDE ATKTKSKYKK QILDSDAWKK LMVRLQGWIT
DDNFVGHPKL EYLQQVILDH FMNAGDGRNV DGAPPSQTRI MVFAHFRDSA EEIARILKRH
EPMIRPRIFV GQAHGKNSEG MTQKDQLEAV EKFKNGEFNT LIATSIGEEG LDIGEVDLII
CYDSKASPIR AYSKWHALQL SRQDWLPVPK KGRRTKKPPK KFHMPDDVIT GFVTAGRMGE
EIVAKGRGKK AAVSVYPSEE LFAVPSLESV LLDDAATRDL ESRYQTVFDD DEAPTVGMLD
LGKYPERQRV LPHTNHRIGP GRVTRAFAGT MQRMHDMDND RLDALKRDLR YSDCELNVDD
GFVVSNTEVA PVIEEDIWED DHPASQSLPI GRAKPVPKAK AKEPAKPKKA AAPKAKQKLG
PEPQENVSPM APKTPAPRAR PRKDKAAVET PIHQVRATSE TPRTKTPDWR VSGHAQEGDE
SSPPPTDPRF RLASQADTIG SDDTAGADEP QDTQAYLLDS ELASFIVEEG VEEIVPTSSL
PSIDFNGVGA GTQAVVKAAR PKRTPRREKI FTSDVTDNDA VVSSDSDDES PLKKPGNGLV
QDAPIHVEGL GRQIDAASDG ATFVIVASHV HDE
//
