ID A0A267G2K6_9PLAT Unreviewed; 1226 AA.
AC A0A267G2K6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BOX15_Mlig006861g2 {ECO:0000313|EMBL:PAA79462.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA79462.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA79462.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA79462.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA79462.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 Chromosome {ECO:0000256|RuleBase:RU367041}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913, 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:PAA79462.1}.
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DR EMBL; NIVC01000633; PAA79462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267G2K6; -.
DR STRING; 282301.A0A267G2K6; -.
DR Proteomes; UP000215902; 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; 3.90.320.10; -; 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; 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; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 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|RuleBase:RU367041};
KW Chromosome {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|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|ARBA:ARBA00023268,
KW ECO:0000256|RuleBase:RU367041}; Nuclease {ECO:0000256|RuleBase:RU367041};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367041};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902}.
FT DOMAIN 229..420
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 859..952
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 960..1186
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 23..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA79462.1"
SQ SEQUENCE 1226 AA; 131808 MW; BFB0AB5D7BDC8CA5 CRC64;
NITMKQTNIN SFFKLGSTAA QSAASTVDVV PPSPPAAPQQ QQQQQQQQKR LARRSFLSNP
RPSSASSSAS SVASAVSFDK PPNAKASNVA RTIFGRKRPP KGLNYRPDAP DLPPTKRAFL
YGEEQQKQQQ QKLTAEPIVV LSDSSNSSGA CSSNEKSPDC AVGRAAKIGK ENSDAGAAAE
LEAEADCWLP AEWRHRPEWI RGRVRSVKRL SDELELDCAG LEPCGWNFVC RLCDSWSETR
LHTGDTVQIV LSPETPWQPD HPELSVTDQQ NYFVLLPDQL LSATAVVASL GCVRRSVLDS
MYTSLEGENK VMLLGSVVHQ LFQDLLVRHQ TVPVTEASAS AAAAQLVNSG QLAQQLAALG
LSESELLAEV SQFVKHIVDW LRRHHGNDGS DGLRVNGVAD IEESVGSRRF GLKGKVDVSL
LVADAAGGDK RLPVELKTGR ASFSHEHVGQ ALLYSMMLDG PEAENSSTAD GADGALLLYL
RDGPQQQLFR PDRSRRCGLL QLRNELAGWL ARPPVIVDEG DGGSAEACEV RLAPLPDPLT
GRDRWCAACP QLLSCSLLHR LAKGEAGCSV GGRPSAEKAM RHLSERHAAY FGHWSRLLLM
ERQAGQAEAE APSAAAAASA TLLFEGQRPA RGRDGGSGQQ TLVRFRVAGT DEPPLTDVAS
EGDFAVVDSA DGCLVGLCAG LVREIACDRL ALLCDRPLKK TDLHYRIRKS NSQKSIGICL
SYLVMLMEDS PISTRLRELL IDKRPPEVTS FDHATVVSVR QFAAPLNREQ RKCLLATLAA
KDFVLLKGYP GTGKTTFLAA LVAALVHLGA RVLVSAYTHS AVDNILVKIV DTYPQVGLLR
IGQEARVHPR IRSRCLASEL QSLQQQQREG SSGATSAGVR ALVESRPVVG CTCLGALDPC
LARCQFDFAL IDEAGQAPLP ACLGPLLRLS GSGGRFLLVG DPHQLPPMVL SRRAASLGLG
RSLLCRLLNR EAVTARVTFA LTEQYRMNSC LLQLPNQLLY NGELTAHESV SQLTLPAVTL
PPRLRDPLAC LAAVWSDRLE HSLVFVSTER IDSVQAESCG RRSSLAGQAS GSSSLANPLE
ASLAVSLLRL LCPAAAAPAD VGLMSPYRDQ VALLRRRLSA ESGSQLTGVE ASTIDQFQGR
DKSLILLSMA RREAGAASAS SILSDPRRFN VAVTRAKRKL IVIGHAAGLG GLPTIDALLK
LLPAECLVRL TDREFDVLTA AGMTEC
//
