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Database: UniProt
Entry: A0A016S2U3_9BILA
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Original site: A0A016S2U3_9BILA 
ID   A0A016S2U3_9BILA        Unreviewed;       231 AA.
AC   A0A016S2U3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA replication ATP-dependent helicase/nuclease {ECO:0000256|RuleBase:RU367041};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU367041};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU367041};
GN   Name=Acey_s0306.g1976 {ECO:0000313|EMBL:EYB84963.1};
GN   Synonyms=Acey-dna-2 {ECO:0000313|EMBL:EYB84963.1};
GN   ORFNames=Y032_0306g1976 {ECO:0000313|EMBL:EYB84963.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB84963.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair.
CC       Involved in Okazaki fragments processing by cleaving long flaps that
CC       escape FEN1: flaps that are longer than 27 nucleotides are coated by
CC       replication protein A complex (RPA), leading to recruit DNA2 which
CC       cleaves the flap until it is too short to bind RPA and becomes a
CC       substrate for FEN1. Also involved in 5'-end resection of DNA during
CC       double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
CC       {ECO:0000256|RuleBase:RU367041}.
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:RU367041};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367041}.
CC       Chromosome {ECO:0000256|RuleBase:RU367041}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|RuleBase:RU367041}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYB84963.1}.
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DR   EMBL; JARK01001642; EYB84963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016S2U3; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887:SF433; DNA REPLICATION ATP-DEPENDENT HELICASE_NUCLEASE DNA2; 1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU367041};
KW   ATP-binding {ECO:0000256|RuleBase:RU367041};
KW   Chromosome {ECO:0000256|RuleBase:RU367041};
KW   DNA damage {ECO:0000256|RuleBase:RU367041};
KW   DNA repair {ECO:0000256|RuleBase:RU367041};
KW   DNA replication {ECO:0000256|RuleBase:RU367041};
KW   DNA-binding {ECO:0000256|RuleBase:RU367041};
KW   Helicase {ECO:0000256|RuleBase:RU367041};
KW   Hydrolase {ECO:0000256|RuleBase:RU367041};
KW   Iron {ECO:0000256|RuleBase:RU367041};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU367041};
KW   Metal-binding {ECO:0000256|RuleBase:RU367041};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU367041};
KW   Nuclease {ECO:0000256|RuleBase:RU367041};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367041};
KW   Nucleus {ECO:0000256|RuleBase:RU367041};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT   DOMAIN          1..210
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
SQ   SEQUENCE   231 AA;  25866 MW;  F50F2CF9795F3D17 CRC64;
     MSVSLFERLQ VHSGALHSLV SQYRMNSVIG KLSSHLFYED RLVCGNNSVA EACLANSGCF
     KESTVEEDPW KVIESGLLRD SVVFVDTRAR EQADFAMIND GGGMVHNMGE ARLVRDVVER
     FLKNGVSPSD IGVMCVYRKQ VDVIKSILDP GLGIEVNSVD QYQGRDKSVV IWSLVWTDTT
     GRRCELLRDR RRVNVALTRA KHKLILIGCA ESMRSMDIMK RVVDSTKVVE V
//
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