ID W6QRV2_PENRF Unreviewed; 1670 AA.
AC W6QRV2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=PROQFM164_S05g000627 {ECO:0000313|EMBL:CDM36794.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM36794.1};
RN [1] {ECO:0000313|EMBL:CDM36794.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM36794.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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}.
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DR EMBL; HG792019; CDM36794.1; -; Genomic_DNA.
DR STRING; 1365484.W6QRV2; -.
DR OMA; LRESWFD; -.
DR OrthoDB; 170190at2759; -.
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; 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; 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; 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}.
FT DOMAIN 581..783
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 1143..1240
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1248..1312
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1320..1549
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1670 AA; 186201 MW; 3056995261536254 CRC64;
MATNNAYPIS SNSRTKLSAF RFQEGEVVPD GASSKDETTS VNGNKQHEDP GSNSVREPMQ
TSSDKGYSPP LEAQAPEPQL QESKPIKECP QTPGNKIPLA DLISNAEDSF NPAEVPEMTP
VDQVIWQHVP ASSNPDTSSQ TPAGRRRKRR HSSSPTGSPS KGTKKKVQKE PFDLNSIQVL
FKTPQHDMAA ELWSNYMDKN MVDGPDDLPP PRFANLLSSS PQTPGSSRTS RDSSGLRRAI
SCTTDFPTSR TKRRRVNELD VSRGIFQRTN SNVESGRPKS SRINYLMEKI ERSIYMATAD
AGPPGSSPLR QHVDTRRCRS SSPTKNWRLH EADEETTESP CAVPPGKVRT GKLPSLQESS
DEFGDDDLDQ GLLDLVNASE DPFIEPAHAS TEFVSLGSSE WAGLDAEKSR SWQPEDSMLN
SKPLMTIPHS TTTNETKRDD IDEFDEFEYE YDDLPDNLQE ILAKCDTKPV PVNLLNSTTA
GPSLQGSDTM NTPVNGSMHS KPPTAIPVKP EVASSDDEFD DDFDLEAIEQ TMKQAGEGGL
AHNLKGRQAI KRYRVVEITK STYVTPKGRT QPEQGLLVED EKTRDRKSII LRESWFDTPC
SKDSYIHLVG DFNVAGQCIV DNLNHMIILH PDHLISATVV ADSVDCQRRA VLQDRVKVIG
ALERPQAFGV FFHEVFQEAL KANKWDMKSL KTLVETVLGR HIEELYSIQM SIPEAVEYLM
SRMPAVLDWA DAFLHLKPQA NSMVEDRNNS KLNLSINKLL EVEEHIWSPM YGLKGNIDAT
VQVTCREDEM EKNLVVPLEL KTGRRDTSQS HRAQTALYTL LLSDRYDIDV TFGLLYYLEL
TKTLSIRAVR HELLQMIQVR NHLSGYIRER QQLPPMLKKA RQCIRCYAKT PCLIYHKLSE
DGDGETSALG EDFDAVVGHL DNGDRDFFRK WDELLTKEEG NLVKFRRELW TLLSSEREAL
GRCFGDVVID PHSAYEEKTG TRINRYHYTF VKRQASPGFS FAESQISVGE PIVISDEKGH
FALTNGYVLH TSSSHIKVGV DRKLRNARSK TTGFDEVTNQ SFRGIMEIGK EEPAALQSPD
EQLVYRIDKD EFSNGMAIVR NNLICMMDKD LFQARQLRQL IVQGQAPAFK TMSSSYSISD
PGNLNVDQRQ AIDKVMSAKD YALVLGMPGT GKTTTIAHII RALVSQGKSV LLTSYTHTAV
DNILLKIRDD NIRVLRIGAT AKIHPDVQEF ADLAAVQKST IEELKDSYEK PQVVATTCLG
INHNIFNQRI FDYCIVDEAS QITLPVCLGP IRMARTFILV GDHYQLPPLV QNKAAQEGGL
DISLFKLLSD AQPGSVVNLE HQYRMCEEIM LLSNTLIYSG RLKCGTPQVA ARSLDIPDIN
ALEKFHGEDL SHALSQSTRE ICPGVPSSPC WLRDLLTPSA KTRLVNTDPI GPAALEIAQG
NRVVNHMEVF LCSQLVESFI ACGIPARDIG VITFYRSQLS LIRQSLRRYG PDLEMHTTDK
FQGRDKAVII LSCVRSNAEN NVGELLRDWR RVNVAFTRAQ TKLLVVGSRS TLRDGNELLC
KYVRLMESKN WVYNLPSGAI DKHFFPSCTT QSQLMSPGAA LTPRSTKGKG NGKNKLPPSR
SSREPLSPLG SRQAAPGLRK PSKTGAKLFN GTKVVGNRPI LRDIVNDLTG
//
