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Database: UniProt
Entry: A0A0N5CN57_THECL
LinkDB: A0A0N5CN57_THECL
Original site: A0A0N5CN57_THECL 
ID   A0A0N5CN57_THECL        Unreviewed;       432 AA.
AC   A0A0N5CN57;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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   ORFNames=TCLT_LOCUS1604 {ECO:0000313|EMBL:VDM97132.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000160301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000160301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM97132.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; UYYF01000221; VDM97132.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5CN57; -.
DR   WBParaSite; TCLT_0000160301-mRNA-1; TCLT_0000160301-mRNA-1; TCLT_0000160301.
DR   OMA; MEVEINT; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
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; PF13086; AAA_11; 2.
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:UP000276776}.
FT   DOMAIN          23..122
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          136..198
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          206..403
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
SQ   SEQUENCE   432 AA;  48947 MW;  9B7D5D1ACB3617F7 CRC64;
     MKVPVFSKMK KEDIMSISQV IRQLNRDQAR AVLRSLMAND FSIIEGFPGS GKTQTVVALV
     CCLIVLGRTV LLTSYTHSAV DNILLKLVEI VDEHKILRLG YSSAITKNLQ HLTLEAKLSK
     YSGEERIVFN YYKFQPIVAC TCLAVSTNLL FSYRRFSMTI VDEASMVLEP TVISAISVSD
     SFVLLGDHRQ LTPLVCSEEA RQEGMAKSLL ERLSVHLSAV VTLHSQYRMN EPITQLSSRL
     FYENKLQCFS FDSVNHASIY SEVYKLCLSN SLNDAIVFLD TNSIKNAVFR ATFGKHGDVF
     NDGEAEFIEG ICKLFISLGL KECDLGVISF YRYHAERLSQ KVGANIEVNT VDQYQGKDKS
     VIVLSFVWTK EKKNQRSDLL ADFRRVNVAI TRAKHKLIMI GCRKSLSRLR TNYFISLFFE
     ESKIDDLVIQ IF
//
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