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Database: UniProt
Entry: B2WAT3_PYRTR
LinkDB: B2WAT3_PYRTR
Original site: B2WAT3_PYRTR 
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}.
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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
//
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