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Database: UniProt
Entry: A0A139AG23_GONPJ
LinkDB: A0A139AG23_GONPJ
Original site: A0A139AG23_GONPJ 
ID   A0A139AG23_GONPJ        Unreviewed;       629 AA.
AC   A0A139AG23;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=M427DRAFT_320796 {ECO:0000313|EMBL:KXS15708.1};
OS   Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC   Gonapodyaceae; Gonapodya.
OX   NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS15708.1, ECO:0000313|Proteomes:UP000070544};
RN   [1] {ECO:0000313|EMBL:KXS15708.1, ECO:0000313|Proteomes:UP000070544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL478 {ECO:0000313|EMBL:KXS15708.1,
RC   ECO:0000313|Proteomes:UP000070544};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(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; KQ965760; KXS15708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139AG23; -.
DR   STRING; 1344416.A0A139AG23; -.
DR   OMA; LCENTKH; -.
DR   OrthoDB; 5474774at2759; -.
DR   Proteomes; UP000070544; 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; cd18037; DEXSc_Pif1_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049163; Pif1-like_2B_dom.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF05970; PIF1; 2.
DR   Pfam; PF21530; Pif1_2B_dom; 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:UP000070544}.
FT   DOMAIN          519..560
FT                   /note="DNA helicase Pif1-like 2B"
FT                   /evidence="ECO:0000259|Pfam:PF21530"
FT   REGION          1..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  68580 MW;  5CDC8C3DBB87BE4D CRC64;
     MSHAREVEYV SPDLFSGGIH GNRAAIGDML KSAGNSSGGP KRQSGQTSLL SYAKPTGRPL
     ATPASRPGSA SGSGGPPRPL IKSKSSTDPL PASHTPFLKK ANPADSSTAS SKPMYPLFPS
     KQQPSHQVEG VLSRRLPPTY IPNHSFPSKR RAPDTDDAST ADGAPDSRFK QAKFSSGEDG
     ASDDINVYQR FINSRGAVST RTGVAMSTGS GVGVSTVKPV TGGRESLSDE QKEVAKIVLE
     EHSSLFFTGR AGTGKSYLLR YLIKELRSRF GRDRVAVTAA TGMAAVNIDG GTVHSFAGFG
     LGLEPVDVLV KKIGYNKNAF KRWQTTKVLV IDEGVFCRGW IATDVEGARC SPTFCMAHSY
     GCDLVSMVDA ELFDKLEEVA RKVRKSSLPF GGIQLVMTGD FFQLPPVPDK QRETKFLFES
     KRFSACVPTS YNLTTAFRQS DPTFLTVLDE LRMGQLSASS VAVLRGLERT PPGWAGKEPS
     VIYSRREEVD RENERRMREI RADEREFAAT DSGDQANLKK LQSSCIAPST LKLKQDALVM
     LIKNKNQTLV NGALGKVVGF SEDSRLPIVR FDRYALDLEL EQEEWTLEQN GQVVARRRQI
     PLVLAWATSV HKAQGQTLDR LKVDLRSVL
//
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