DNA2_CHICK
ID DNA2_CHICK Reviewed; 992 AA.
AC Q5ZKG3; F1NWZ9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=DNA replication ATP-dependent helicase/nuclease DNA2;
DE AltName: Full=DNA replication ATP-dependent helicase-like homolog;
DE Includes:
DE RecName: Full=DNA replication nuclease DNA2;
DE EC=3.1.-.-;
DE Includes:
DE RecName: Full=DNA replication ATP-dependent helicase DNA2;
DE EC=3.6.4.12;
GN Name=DNA2; Synonyms=DNA2L; ORFNames=RCJMB04_11a16;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair in
CC nucleus and mitochondrion. Involved in Okazaki fragments processing by
CC cleaving long flaps that escape FEN1: flaps that are longer than 27
CC nucleotides are coated by replication protein A complex (RPA), leading
CC to recruit DNA2 which cleaves the flap until it is too short to bind
CC RPA and becomes a substrate for FEN1. Also involved in 5'-end resection
CC of DNA during double-strand break (DSB) repair by mediating the
CC cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the
CC presence of RPA. Also involved in DNA replication checkpoint
CC independently of Okazaki fragments processing. Possesses different
CC enzymatic activities, such as single-stranded DNA (ssDNA)-dependent
CC ATPase, 5'-3' helicase and endonuclease activities. While the ATPase
CC and endonuclease activities are well-defined and play a key role in
CC Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase
CC activity is subject to debate. According to various reports, the
CC helicase activity is weak and its function remains largely unclear.
CC Helicase activity may promote the motion of DNA2 on the flap, helping
CC the nuclease function (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AJ720121; CAG31780.1; -; mRNA.
DR EMBL; AADN02028013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001006497.1; NM_001006497.1.
DR AlphaFoldDB; Q5ZKG3; -.
DR SMR; Q5ZKG3; -.
DR STRING; 9031.ENSGALP00000006419; -.
DR PaxDb; Q5ZKG3; -.
DR Ensembl; ENSGALT00000006429; ENSGALP00000006419; ENSGALG00000004037.
DR GeneID; 423688; -.
DR KEGG; gga:423688; -.
DR CTD; 1763; -.
DR VEuPathDB; HostDB:geneid_423688; -.
DR eggNOG; KOG1805; Eukaryota.
DR GeneTree; ENSGT00780000122010; -.
DR InParanoid; Q5ZKG3; -.
DR OMA; NYCEAAI; -.
DR PRO; PR:Q5ZKG3; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000004037; Expressed in spermatid and 8 other tissues.
DR ExpressionAtlas; Q5ZKG3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; ISS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; ISS:UniProtKB.
DR GO; GO:0006264; P:mitochondrial DNA replication; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR026851; Dna2.
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 PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF433; PTHR10887:SF433; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..992
FT /note="DNA replication ATP-dependent helicase/nuclease
FT DNA2"
FT /id="PRO_0000263605"
FT REGION 51..488
FT /note="Nuclease activity"
FT /evidence="ECO:0000250"
FT REGION 489..992
FT /note="Helicase activity"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 617..624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 578
FT /note="S -> T (in Ref. 1; CAG31780)"
FT /evidence="ECO:0000305"
FT CONFLICT 931
FT /note="K -> E (in Ref. 1; CAG31780)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="P -> A (in Ref. 1; CAG31780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 992 AA; 111679 MW; 34A62421494C2E6C CRC64;
MADPSNAALR SGLNNRYRVL EVRVVRGEGR DPEKHLAVSS DPSLGDTELC VLQNGWESVP
VVPGDIVHLE GDCSSGTWVI NEQSGYLILY PDLLLSGTTI SSSIRCMRKA VLSERFRGSE
CGSRQTLVGT ILHEIFQQSV TNNLSPEKVE ELAKKIVYGQ KYLKEMYHLK LKQTEIMQEI
EEYLPSFFKW TEDFVRNPAN QNKMQLKLPS ENKTGDCSST VEIVDILDIE ENIWSPRFGL
KGKIDVTARV KIHRQGGIQS RIMPLELKSG KESNSVEHRS QVILYTLLNL ERRVDPEAGF
LLYLKTGTMY PVTGTRMDRR ELIKLRNQVA FYLMHSTYKS AVGRQQSQLA ALPPLIDDSQ
ACKYCSQIHN CFLYSRAVEE RMASVSFPPA LIPIIEKETQ HLKPSHLEYF SLWYLMLTLE
MQSGDSKKGY KNIWMIPSLE REKAGDCVGN MIRVDQVQEV SEGQYLHSFQ RKNGAVPGAN
LLVGDRVVVS GEENGLLGLA TGYVREISAT KISCLLGRNL SKLPESTTFR LDHEEGDCSI
GVPFENLSKL MKDSPVSEKL RNLIIDFHKP RFIQHLSSVL PPEAKEAVAS ILKGLNKPQK
QAMKQVLLSR DYTLIVGMPG TGKTTTICAL VRILSACGFS VLLTSFTHTA VDNILLKLAK
FKVGFLRLGR AQKVHPDIRK FTEEEICRSK SIKSVTDLEE LYNSQPVVAT ACMGINHPIF
VQKQFDFCIV DEASQISQPI CLGPLFCSKR FVLVGDHQQL PPLVQNSEAR DLGMSESLFK
RLEQNQNAVV QLTVQYRMNS KIMSLSNKLV YEGKLECGSE KVSNATANLP NLKMLKLEFA
DASKTWLKEV LEPDKPVCFL NTEKAGCRPS DIGIISPYRH QLKVITDLMA RLKENRVEVN
TIDKYQGRDK SIIIVSFVRN SNDENLGALL KDWRRLNVAI TRAKHKLIMV GCVPSLRRYP
PLEKLLCHLQ SEAMIFNLPP GAHESIHKCN IL
