ID B2WAT3_PYRTR Unreviewed; 673 AA.
AC B2WAT3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=PTRG_07396 {ECO:0000313|EMBL:EDU50315.1};
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:EDU50315.1, 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 -!- 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:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|RuleBase:RU363044}.
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; DS231621; EDU50315.1; -; Genomic_DNA.
DR RefSeq; XP_001937728.1; XM_001937693.1.
DR AlphaFoldDB; B2WAT3; -.
DR STRING; 426418.B2WAT3; -.
DR EnsemblFungi; EDU50315; EDU50315; PTRG_07396.
DR GeneID; 6345669; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_7_4_1; -.
DR InParanoid; B2WAT3; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 240..406
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 75435 MW; 920B3815ED109A61 CRC64;
MVRPTTKRKV EDEHHATYDK RLRTAPSFSS GSRIPALGTQ DAPVEIESSP EPEQNTTPPR
STLSVKEWGL PVDLSGGRPY YAIVGHVPGI YTGNWKAIED AYLRGYQGNK KKKFKTVDEA
WDFLEEHRHL VEQALNRDRG RAYLTSIGKA PPAKPQPRRS AGIAQHQSPL PSSSYTQSRS
YSNQSATPES EDESLTPQTA FQRPNSSLNG PQPRANNNVA AAPEVTLDPE QHYVVDLIMA
GCNVFYTGPA GCGKSAILRV FKKRLEEQRK IIFVTAPTNI AALAIGGQTT YSYAGWHMEI
GKEPLNNLKK RVLKGRQKEL FCNTDVLVVD EISMVENNFF GRLSEVMKSA RNSKEAFGGV
QIIVTGDECN FVNINLSKIH RQDDPFFRSI LNRIRLEGII QPEHKEILLN HESETEGAIE
ISTHKALVAK QNKKKIDELP GKAIAYRCKD FFLWKDHHKG DISLKKYLQR GDGGHLHYLS
DHRYEAELDL KQNMRVVLLH NLAPGLGLVN GSQGTIIGFE RYDPEKLPIK DSPLTGPHAR
YCEEEIKRFA ERNEFRPWPV VRFDNGLTET IYADCSAAER GVSEPFSLLS RTQIPLMAGY
SVTIHKAQGM TLDKVKVDLA KSFETEQPYV ALSRAKSLHG LTVLSLPAHG FGGRNREVKE
FLDSFSRNSV QVL
//