ID A0A1W5D4V9_9LECA Unreviewed; 1708 AA.
AC A0A1W5D4V9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM38178.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-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: 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}.
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DR EMBL; FWEW01002291; SLM38178.1; -; Genomic_DNA.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000192927; Unassembled WGS 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: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; 2.
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; 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; PF01930; Cas_Cas4; 1.
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 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}.
FT DOMAIN 604..806
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 814..916
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 978..1069
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 1173..1268
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1280..1341
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1349..1579
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1708 AA; 187689 MW; E6B8CCD4A866B303 CRC64;
MAMLPIAASS QSKAKLKAFQ FTENKSRHSS SGDPRTEEAD KENTRALQEP PGPNASQPKA
RSQTSSQTSA LQARGECPQT PVGRLPLAEL IGNAEDAHAH GELDAPYERV LWNLSPRSSD
QANSLGTPAG RRGKKRAYSS SPSSSSPNEA SNHFAAAKRS FDLQPLQKSL KTPQVDPAGD
LWSRYSMNAI DKQSPTAPGA SKLIDLMNSS SPLTPAIHFL GRYSGLRRTL SCDTEWPTSI
SKRRKIHHSS SHEEGSAILA AQPEPGDGRS TTKLSRVSLL VGMVQERLAK PVDKADIRGP
SSSSPLPDTG SFDYDRASPL LQRAQAQAAE RALSPTENNT SEKRMRSRQQ SPEVQDQRPD
DKESSSDFGD DDIDFGLLET VDAAIASTSG TGHQITSELF MGDSIPRMTP VQPLAALGDA
DNGQPAPREA PNPEIVGSVH YLPEQTLVQT TEHQSVVQTG EETDEFGDDD SDLFAADLHD
VVAMYDSLQP QNNQAPAENM AQDEHDALPQ AVKVAVSPRN DIGKTEPVEV SSGDEFGEDL
DFEQIAVEYA SATQGFQCAT PRAESNGKKL RTIQRYLIMT VAEAQYETDK GQLRPEKILL
LQDEKTKANK AVTLRQSWFD SPCTTGSYIH LIGDFDRAGQ CIVDDARNML ILHPDHLISA
TVVADSFSCT RRAVLQDRVK ATNEANGPQV YGHILHEIFQ EAMRANRWDT QWLTVTIGSI
AARYLENLFE INVELGTALE YLKSKAPELQ AWAEVFVTAR PKAGAVVKDR NGGQALMSVN
KLLDVEEHVW SPMYGLKGNI DATVQVTMQD GEEERTLTVP FEVKTGRNNS NAAHNAQTAL
YTLLLSDRYD VEIAYGILYY METSEISRIP AIRHEIRHMV MQRNELACYV RQRLELPPML
NSSHLCGKCY AKTPCFIYHK LVDGGDGETS GMKEKFDELA KHLKPAHQEF FKKWDDLLTK
EEKDVLKFRR ELWTMSSTER EKVGRCFANV VIEPGSTFEM EEAQRISRFR YTFIKQKPAT
GFSFTESQIT NGEPIVVSDE KGHFALANGY VTNVRKHRIT VAVDRRLHNA RNQGRNFDAQ
RNQVFTGIME VFEEGREQST STLQEPEEQV LYRLDKDEFS NGMATVRNNL IRIMEKDLFG
AQALRKLVIE GVAPTFKPTP SAYTLGGSAS QANLNVDQKR AIEKVMSAND YALVLGMPGT
GKTTTIAHII RALAAQGKSI LLTSYTHTAV DNILLKIRND NIGILRIGAV AKVHPEVQEF
TDLAAVPKKT VEELKRSYSQ QVVATTCLGI NHPIFNQRVF DYCIVDEASQ ITLPVCLGPI
RMARTFILVG DHYQLPPLVQ NKEALEGGLD ISLFKLLSET HPSSIVTLEH QYRMCSDIML
LSNTLIYSGR LKCGTPAVAA RSTPIPNLAA LQQHHHTSHA TLSPSQQSIC LGPVPGSCWL
RDLLDPKIKA CFVNTDPLLP ASREEAKGSR IVNAAEATLC THLVEALLST GVPATDVGVI
TLYRSQLALL RQQLRHRCDA DGLEMHTADR FQGRDKEVVI LSLVRSNEQK NVGDLLRDWR
RVNVAFTRAR SKLLVLGSRE TLGGNELLRG FLGLVEGEGW SYDLPGGALV GHVFGGLGSQ
GLGTGTGREG SQVMGRWGSQ VRKAEEGKEG GKKVPGKEGG EKVPGKEGAK KVPGKEGGKK
VPGKVVRGSG RGILGARGVL RDVINEVL
//
