ID A0A093GTT9_DRYPU Unreviewed; 994 AA.
AC A0A093GTT9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
DE Flags: Fragment;
GN ORFNames=N307_11462 {ECO:0000313|EMBL:KFV72786.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV72786.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV72786.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV72786.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU367041};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367041}.
CC Mitochondrion {ECO:0000256|RuleBase:RU367041}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913, ECO:0000256|RuleBase:RU367041}.
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DR EMBL; KL217011; KFV72786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093GTT9; -.
DR STRING; 118200.A0A093GTT9; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; cd18041; DEXXQc_DNA2; 1.
DR CDD; cd22318; DNA2_N-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR026851; Dna2/JHS1_DEXXQ-box.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR048459; DNA2_Rift.
DR InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
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; 2.
DR Pfam; PF08696; Dna2; 1.
DR Pfam; PF21123; Dna2_Rift; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU367041};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367041};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367041};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367041};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367041};
KW DNA-binding {ECO:0000256|RuleBase:RU367041};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU367041};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU367041};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW ECO:0000256|RuleBase:RU367041}; Nuclease {ECO:0000256|RuleBase:RU367041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367041};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875}.
FT DOMAIN 42..248
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 437..533
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 593..689
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 697..763
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 772..862
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT DOMAIN 863..950
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV72786.1"
FT NON_TER 994
FT /evidence="ECO:0000313|EMBL:KFV72786.1"
SQ SEQUENCE 994 AA; 112122 MW; 664B0801ABCC5C7B CRC64;
DSSDTTLRNG LNNRYRVLEV NVIQRNGSDP EKHLTITASQ SLEDTELCIL KNGWESVPVV
PGDIIHLEGE CSSRTWVINE QSGYLVLYPD LLLSGTTISN SIRCVRRAVL SEKFRGSEFG
SRQTLIGTIL HDIFQQSVTN NLAQEKVEVL ANKVVYGKKY LKEMYHLNLK QSEIMQEVQE
YLPSFFKWVE DFMHNPANQN KMQLKLPSDG KRDDLSSKIE FVDILDVEEN IWSPRFGLKG
KIDVTARVKI HRQSGVQSRI MPLELKSGKE SNSIEHRSQV ILYTLLNLER RVDPEAGFLL
YLKTGTMYPV SGARMDRREL IKLRNHVAFY LMHSTYKAAV GRQHSQPAAL PPVVDDNQAC
KFCSQMHNCF LYSRAVEQRM DSVSLPPGMA PIIERETQHL KPSHLEYFSL WCLMLTLELQ
SEEGKKGYKN IWMLPSVERE KAGDCVGDMI RVHEVQEISE GQYLHFFQRR NGAVPGTNLL
VGDRVVVSGE ENGLLGLATG YVTGVTVTDV SCLLGRSLSK LPKNTVFRLD HEEGDFGIGV
PFENLSKLMK DSPVSERLRN LIIDFDKPRF IQHLSSVLPP EAKETVANIL KGLNKPQKQA
MKQVLLSRDY TLIVGMPGTG KTTTICALVR ILSACGFSVL LTSFTHTAVD NILLKLAKFK
VGFLRLGRAQ KVHPDIQKYT EEEICRSKSI KCVTDLEEVY NSQPVVATSC MGVNHPIFHR
KQFDFCIVDE ASQISQLTCL GPLFCSKRFV LVGDHQQLPP LVLNAEARDL GMSESLFKRL
EKNQNAVVQL TVQYRMNSKI MSLSNVLVYE GKLECGSEKV SNATVNLPNL KNLKLELADV
SKTWLKEVLD PDTPVCFLNT EKAGCKPSDI GIISPYRHQL KTITDLMAKL KESGVEVNTV
DKYQGRDKSI IIVSFVRNSN DENLGALLKD WRRLNVAITR AKHKLIMLGC VPSLCRYPPL
EKLLCHLHQN VSLTLYIFNL PTGAHESIHK CNIL
//
