ID A0A2P6TXR4_CHLSO Unreviewed; 1587 AA.
AC A0A2P6TXR4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=C2E21_2066 {ECO:0000313|EMBL:PRW58857.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW58857.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW58857.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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:PRW58857.1}.
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; LHPG02000004; PRW58857.1; -; Genomic_DNA.
DR STRING; 3076.A0A2P6TXR4; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000239899; 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: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; 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; IPR022765; Dna2/Cas4_DUF83.
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; 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; PF01930; Cas_Cas4; 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:UP000239899}.
FT DOMAIN 560..766
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 806..901
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 1167..1251
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1272..1335
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1345..1553
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1587 AA; 169145 MW; 5E8D8702AD0740DC CRC64;
MAPKKPAVAH KKQKVEAGGA NILRFFDKQP EEGAHRHEEA AARRVTPPLG AAADGPSPPP
GGGGGGAAAV AGPAAAGRPA MTKQLAALQD LAPADSFAMS QDTEAMQMQV VWHDSPGGSS
QGQPARSLSN LGRSAGLSGA QDLTAIKQRL ISAAQKPRDV RRPAGPVLAP AAGARLHPGG
EQLLEGLLAR QRPGAVQPQP QAQAQQQQQQ QQQQLQQQEL SCGSGGGNGA HRTPATQLRS
ILKRRAGGPG SSGGRRTPAS SVKFSLADSG SKGGRSRSLR GGAAAHLGSS GKKRQAGQKR
KALLELLEQV ETIVQSGGSP TDDEGGDGEA TGVALAAADG VASGPAGVEA VSDKENAAGG
APPAKPSSQE RDGVAGPTGS QQLMPPPGGV QCCGGLRGRQ QQQQQQASQQ VQQQELPPVV
RPQLAPQLAP PQAHQGNFGD DDDEDDALMT QLELQLLTQG SDSGWEDEVD VELLDQFEAA
ALRERADRSS GGAAAPAGDA AGQQAGQEAQ PGVTVGGERP EEAGGQPRYA GSREEVRYEV
RDIFSAPHEQ VLLLHNKYQK RDVYAHLQPP WCDLPYRVGD AVNVLAQLDF FEGHHHCLLN
MEQGMLILHP DVLLSGTRIT SSNECTRRSF LDERIAGDGS NDKAVKGTLT HNLIQAALTG
GLRTDPQLGA AAERIVADAT EALFEVELSE EDAMACLRQA FPGVRAWMAR FLRHEPATDA
VLGAGYDPLT NRDVRRRVAV QEVVDIEESI WSTKFGVKGM IDISTQLVLD DPQQQQAQRG
SGGWMQPAGA GGLAQQAAAQ GGRQVTVAPV EIKTGKLHET HKAQVLLYLL LMEERYGRPL
EWGMLWYTHQ PDPQLVMKRP MELACVMAVR NRLAAAIAHL ELPPLSEEKR ACNWCFQQAN
CALAHKAERG AAVTVDSFVR QSTDRGGGAL DRVQQELAGR YERAAGHMTS ADCEFLRKWE
ALVTVEEAHS VLRRPEIWGL TGDERQALGR CQAGLTLVHV DEQEGLYTFR RPDAGAIECS
FTDGEMLLLS VEGKHVAVAR GFFYTCTATQ LTVSLNKPLR PGLLWPRGPP AAAAPGGPPP
PCDPSVLWRL DRDEASSTFV RLRGNLFALF RREYETRQDP QTRQLVVGPE LPASQHAAKL
RRLVVELAPP QFAAPDPTQP DPTPPGMNSE QHVAVQRVLS AQDYALVLGM PGAGKTTTIV
AMVQALVAAG KSVLLTSYTN SAVDNILMKL AREEVPFLRL GRASGVHPAV RPWLPGGERY
PQKNTREWAR LAEAVPVFGA TCFGVNHALL KDKLFDVCII DEAGQMVLPA SLGPLLKARA
FVLVGDHNQL PPLVTCKEAE AGGLGESLFK RLSDAHPQAV VTLPVQYRMA ADIMALPNAL
IYRDALRCGT DSVAQAALEL PPGAAAAVAG LPPWLQAALD PQRRVLFLDT AAVEDARESA
NGGDSGSNAG EAQLVLRFLQ AAAAAGVAQE QLGVISPYRA QVALLDRLAR SARLDGVEAL
TVDKCQGRDK DCIVLSLVKS NGEGDAGKLL QDWRRINVAI TRAKRKLLLL GDAATLRSIP
LFARLLDLVR QHGWYLPLPP NALAGLG
//