ID A0A1Q5UK28_9EURO Unreviewed; 1666 AA.
AC A0A1Q5UK28;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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};
GN ORFNames=PENSUB_1541 {ECO:0000313|EMBL:OKP12809.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP12809.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP12809.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP12809.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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 -!- 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:OKP12809.1}.
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DR EMBL; MNBE01000177; OKP12809.1; -; Genomic_DNA.
DR STRING; 1316194.A0A1Q5UK28; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000186955; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955}.
FT DOMAIN 576..778
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 788..888
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 949..1046
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 1139..1230
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1243..1307
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1315..1544
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 33..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 184738 MW; 85A4B62652F87633 CRC64;
MATNNNNSYP ISSNSRTKLN AFRYKEETVA LDNTTSKNET KAVHDNKENQ SSWLNGVVES
MQTSADNADP PPQAVPLNED TKPVKECPHT PGNRIPLADL ISNAEDAFDP APGPEVTPID
HVIWQHVPAS SNPDASSQTP AGRRRKRRHS SSSAGSPTNG TSKKAQKEPL DLQSIQALFK
TPQHDLAAEL WNNYMDKNMV DGTDDLPPPR LANLLSSSPQ TPASGRTSRD SSGLRRSISC
AAEWPTSRAK RRRVNRQDPG SGRGIFSRTS SNVLDSGRNK SSRLNFLLDR IEKSLHPVPQ
VKMGPPNSSP LRQRMDAQRC RSSSPTMDRK GLVDADAARE ALIGKSADNP EAAGGAILED
SESEFGDDDL DQDFMDLAEA AADPFVDFAV DRTDFDSLGS SALSNLAAEK LESSHSALES
VFDKKPPAAQ NSMNNETKPD DFDEFEDEYG DFDDDFADAL VECDVKPTDA SNPPIAKSQP
APKVDAVSVN SAPQVPAHVP QMSAHAAAVL SDDEFDDDFD LDAIEQTMKQ TGEDAAYNLK
SRKAIKRYQI VDTAESSFVN SRGRTQPEQV LSVKDEKTDA RKVIILRESW FDTPCSKDSF
IHLVGDFNSF GQCVVDNTNH MVILHPDHLI SATVVADSVD CQRRAVLQDR VKVISQIEKP
QAFGIIFHEV FQEALMANRW DLDSLRLLVE KVLGNHVEEL YSINMTMSEA IETIMGKIPQ
VQAWADVFLQ TKPKANSLVE DRNGAKLNLS IGKLLEVEEH VWSPMYGLKG NIDATVQVTC
QDKDGLKNLV VPLELKTGKR DTNQAHRAQT ALYTLLLSDR YDVDVTFGLL YYLELSKTLS
IRGIRHELVQ MIQVRNRLVG YIRERMQLPP MLKKAQQCNK CYAKTPCLIY HKLSEDGNGE
TSALGEDFEV FTKHLNQGDR EFFRKWDELL TKEEGNLIKF KRELWTLLSN ERESYGRCFG
DVVIDPRTAH EDQNGTRINR FRYTFHKRKA SPGFSFAESQ ISVGEPIVVS DERGHFALAN
GYVTQLSTSH ITVAVDRRLH NARAKTIGFD AISNQSFRGI MEIGTDGLSE LENPDEQMVY
RIDKDEFSNG MAIVRNNLIC MMDKDLFQSR HLRRLIIEGQ PPVFKPTSSA YKLPDSESLN
VDQKQAIDKV MSAKDYALVL GMPGTGKTTT IAHIIRALVA QGKSVLLTSY THTAVDNILL
KIRDDNIRML RIGATTKIHP EVQQFADLAA IPKKTIEELK DSYEKPQVVA TTCLGVNHNI
FNQRIFDYCI VDEASQITLP VCLGPIRMAR TFILVGDHYQ LPPLVQNKAA QEGGLDVSLF
KLLSDAQPDS VVNLEHQYRM CEDIMLLSNT LIYSGRLKCG TPQVAARSLE IPNIQALKQF
HTDDVHFSEP KQEICLGPGH GRCWLNDLLV PCAKSLLINT DTLGASSLET AQGQGQRVVN
HMEAILCTQL VEALIACGIP AREIGVITFY RSQLSLLRQS LRHYSPDLEM HTTDKFQGRD
KEIVILSCVR SNAENNVGDL LRDWRRVNVA FTRARTKLLV LGSKSTLRDG NELLGKYVRL
VEGKGWAYDL PPGAAGSHGF PSAALDSTQM SFQSPNAARS PGSMKSKMSP VVKKKPASRE
PLSPLGSRQP SSGLKRPAKR GVKLFNGTSV VGNRPILQDI VNDIAG
//
