ID W3XGE2_PESFW Unreviewed; 824 AA.
AC W3XGE2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=PFICI_02527 {ECO:0000313|EMBL:ETS84502.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS84502.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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; KI912110; ETS84502.1; -; Genomic_DNA.
DR RefSeq; XP_007829299.1; XM_007831108.1.
DR AlphaFoldDB; W3XGE2; -.
DR STRING; 1229662.W3XGE2; -.
DR GeneID; 19267540; -.
DR KEGG; pfy:PFICI_02527; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_7_4_1; -.
DR InParanoid; W3XGE2; -.
DR OMA; KLKMNAQ; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; 1.
DR Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SUPFAM; SSF55658; L9 N-domain-like; 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:UP000030651}.
FT DOMAIN 138..185
FT /note="Ribonuclease H1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01693"
FT DOMAIN 623..656
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 92482 MW; B0BC33C577EFC38C CRC64;
MADNCFSYDV SRPSRKRAAA GESASQPIVL IDSDEEEAAG EAFTVPAPKR HRVEQSLPEF
IPLDISDDEN IFHGASNLHR GRDLDAQSAP NASKHKRPHP RGDQHNSSRN APLNPSMDER
IDKMITEWTR DMSAGAKKYY VALKARQPGI FTTWPECEAQ VKGIAGWNGK TMYRTCSSLQ
EARNFARENL PNVLQEQDSR QERVNDQYNR PERDTVRSFR AEISVSNQPS EISNGQNRLK
QGHSHRNGHD LTQSGIADSR PAISRGGLSA PQQSISVKVD SGELGDADGN VEFDVADDEP
ELCKEQQEAV NHALSGRNVF MTGSGGCGKS VVVRHLLKKF RAEDKNVSIV APTGIAAFQV
SGSTTCTFMG WTQDTCREPF EQVRKNLWKK KTAKRLKSTD VLIIDEISMV SNFHFERMSR
AFTEIKGYRN QENLEPFGGC QVIAVGDFCQ LPPINGLEFC NDCGMKMTKS TGRSTTYTCP
ECPRPIAYTE QDKWAFKSEA WADCNFANVH LTKIHRQSDE KFVQMLQKGR LGRKLVQAEI
DLLMNHPCNV ENGVWLSSRR KEVTDRNESE FAKINSEQFD YWCIDKFDCA HDDLRGTVNP
VYWGKPPMER RPLDKLSEHR YSNCLSLKVG MPVILLKNVD VQAGLCNGSQ GIVVGFEDYQ
KAAPPTPPND SNYEGDEEGY RRAHRRWSET TNFMKHPGLD KQVLPVVQFH NGMRCMIQPD
CTISQLSAAE GRYSLLLRTQ IPLAQGWALT IHKSQGMTLE RLVVNLASVF EHGQAYVALS
RATALEGLKI EGGPSATNAL RNKLGPPQEV MEFLHEKFPH MFQS
//
