ID A0A0M4EUJ7_DROBS Unreviewed; 1117 AA.
AC A0A0M4EUJ7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=Dbus_chrXg628 {ECO:0000313|EMBL:ALC48772.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC48772.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC48772.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC48772.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) 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: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC Nucleus {ECO:0000256|RuleBase:RU367041}. Chromosome
CC {ECO:0000256|RuleBase:RU367041}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913, ECO:0000256|RuleBase:RU367041}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012528; ALC48772.1; -; Genomic_DNA.
DR RefSeq; XP_017850094.1; XM_017994605.1.
DR AlphaFoldDB; A0A0M4EUJ7; -.
DR SMR; A0A0M4EUJ7; -.
DR STRING; 30019.A0A0M4EUJ7; -.
DR GeneID; 108605037; -.
DR OMA; NYCEAAI; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000494163; Chromosome x sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:InterPro.
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; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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; 1.
DR Pfam; PF08696; Dna2; 1.
DR Pfam; PF21123; Dna2_Rift; 1.
DR SMART; SM00382; AAA; 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 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|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 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:UP000494163}.
FT DOMAIN 660..832
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 1117 AA; 124627 MW; 067B620A7AD1FFFC CRC64;
MQTAKRVLSP SKADNVLTTH KKLKTQLSVE PAEQENLALL LDDDDDFDLS ALDAAVNAQK
LDLSCWQRCI VQLVERKPKT YDLVLELCSE RGAHEQDTAA VAKAACQLQA PWNQTPLNVG
DLISVQAQWD ATLNCYVVNK DHGYCIIHPD MLISSTAVTG SLFCRRKAVL QSRFRGIDST
NAVMLIGTLV HELLQTVLSE RLRTQAQVET ALQQMLQSAS LAQMLYAGQL SHSEIELQLH
NFVEPIVSFV AQYVEGKLPA SLPKEMYRGR IEQIEDIEEN LWVPQLGLKG KVDVSVRLRQ
QKQPVPLELK TGRASFSMEH KGQLLLYQLM HSVLGRETRS GLLLYLKEGI LREVRDGRNE
QRDLILLRND LVYYLTREVQ LPALKQQSLL LPEQPGKLLQ PFQLPEPISH HSACNNCAYN
TLCCSFASTD AALELSSSHP LQRLMPQLLQ QLTQADQEYV LHWCGLLALE EQHGNQSPQL
RAIWTESAEQ RQQQGRAICD LQLPAEHKTR CIDGRYAHKL QLSAAAASAA VNLTLSGFEL
GEYVIVSSEK RLAIAAGYIT ELSARQLCLQ LERDLGQRYA QQRFIVDKHE SQTFASFNYT
NLALLLADTP DAARLRSIVV AREPPTQSKV LPQLVLSKGA AMLRDLNKVQ QAATLRALTT
NSHLLIKGLP GTGKTQTLVA IVRLLHLLGR SVLITAQTHS AVDNLLLRLL PHKLPMLRLG
SSARIHPQLL EISEAQLTAQ CVSVEQLTAA LHAPSIVGTT CLGAGHALFQ HRRFDYCIVD
EATQVLQPTV LRALSHCERF ILVGDPEQLP PVLRSHQARQ RGADETLFQR LDCAAATAVL
TLQYRMNRSI ARLANQLTYG GALRCANEQV EQAKLQLELP ALSHASRWVL RALQPHLDQS
ALLLDTGDCA QRCADFANGS SELNSTSASI EQHFGESDAA TATANATVRS GKRRVPKYSN
YCEAAIVLQL LRSLLAAGYD GARIGVIAPY RAQVELLRKL CKELQGVEFN TVDQYQGRDK
NIIIYSCTKT GSSSSDMERL REAEILEDQR RLTVAITRAK HKLLLLGDAA CLQRYTPFRR
LLEHLPEHCR LQLQDDRMQF NWHTLLEQLQ LALNSNL
//
