NUCS_PYRAB
ID NUCS_PYRAB Reviewed; 251 AA.
AC Q9V2E8; G8ZFW1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Endonuclease NucS {ECO:0000255|HAMAP-Rule:MF_00722};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00722};
DE AltName: Full=Nuclease for ssDNA;
GN Name=nucS {ECO:0000255|HAMAP-Rule:MF_00722}; OrderedLocusNames=PYRAB01260;
GN ORFNames=PAB2263;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH PCNA.
RX PubMed=22431731; DOI=10.1074/jbc.m112.346361;
RA Creze C., Ligabue A., Laurent S., Lestini R., Laptenok S.P., Kuhn J.,
RA Vos M.H., Czjzek M., Myllykallio H., Flament D.;
RT "Modulation of the Pyrococcus abyssi NucS endonuclease activity by the
RT replication clamp PCNA at functional and structural levels.";
RL J. Biol. Chem. 287:15648-15660(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), FUNCTION, DNA-BINDING, SUBUNIT,
RP INTERACTION WITH PCNA, DOMAIN, AND MUTAGENESIS OF ARG-42; ARG-70 AND
RP TRP-75.
RX PubMed=19609302; DOI=10.1038/emboj.2009.192;
RA Ren B., Kuhn J., Meslet-Cladiere L., Briffotaux J., Norais C., Lavigne R.,
RA Flament D., Ladenstein R., Myllykallio H.;
RT "Structure and function of a novel endonuclease acting on branched DNA
RT substrates.";
RL EMBO J. 28:2479-2489(2009).
CC -!- FUNCTION: Cleaves both 3' and 5' ssDNA extremities of branched DNA
CC structures. Binds to ssDNA. {ECO:0000255|HAMAP-Rule:MF_00722,
CC ECO:0000269|PubMed:19609302, ECO:0000269|PubMed:22431731}.
CC -!- ACTIVITY REGULATION: Activity is modulated by PCNA. PCNA increases the
CC binding affinity of NucS towards ssDNA as well as branched DNA
CC substrates carrying either 3' or 5' flaps. PCNA is also required for
CC optimal loading of NucS on its substrates and to direct activity
CC towards ss/dsDNA junction. {ECO:0000269|PubMed:22431731}.
CC -!- SUBUNIT: Homodimer. Interacts with PCNA. {ECO:0000269|PubMed:19609302,
CC ECO:0000269|PubMed:22431731}.
CC -!- INTERACTION:
CC Q9V2E8; Q9V2E8: nucS; NbExp=4; IntAct=EBI-7103178, EBI-7103178;
CC Q9V2E8; Q9UYX8: pcn; NbExp=3; IntAct=EBI-7103178, EBI-7103152;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00722}.
CC -!- DOMAIN: Composed of two independent domains separated by a small
CC linker. The N-terminal region contains the ssDNA binding site and the
CC C-terminal region contains the nuclease active site.
CC {ECO:0000269|PubMed:19609302}.
CC -!- SIMILARITY: Belongs to the NucS endonuclease family.
CC {ECO:0000255|HAMAP-Rule:MF_00722}.
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DR EMBL; AJ248283; CAB49050.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69502.1; -; Genomic_DNA.
DR PIR; C75200; C75200.
DR RefSeq; WP_010867250.1; NC_000868.1.
DR PDB; 2VLD; X-ray; 2.60 A; A/B=1-251.
DR PDBsum; 2VLD; -.
DR AlphaFoldDB; Q9V2E8; -.
DR SMR; Q9V2E8; -.
DR IntAct; Q9V2E8; 6.
DR MINT; Q9V2E8; -.
DR STRING; 272844.PAB2263; -.
DR EnsemblBacteria; CAB49050; CAB49050; PAB2263.
DR GeneID; 1495013; -.
DR KEGG; pab:PAB2263; -.
DR PATRIC; fig|272844.11.peg.139; -.
DR eggNOG; arCOG01304; Archaea.
DR HOGENOM; CLU_069350_1_0_2; -.
DR OMA; RCSVDYA; -.
DR OrthoDB; 96363at2157; -.
DR PhylomeDB; Q9V2E8; -.
DR BRENDA; 3.1.11.5; 5242.
DR EvolutionaryTrace; Q9V2E8; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1350.10; -; 1.
DR HAMAP; MF_00722; NucS; 1.
DR InterPro; IPR002793; Endonuclease_NucS.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR PANTHER; PTHR38814; PTHR38814; 1.
DR Pfam; PF01939; NucS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Endonuclease; Hydrolase; Nuclease.
FT CHAIN 1..251
FT /note="Endonuclease NucS"
FT /id="PRO_0000155694"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 42
FT /note="R->A: Fails to bind ssDNA."
FT /evidence="ECO:0000269|PubMed:19609302"
FT MUTAGEN 70
FT /note="R->A: Fails to bind ssDNA."
FT /evidence="ECO:0000269|PubMed:19609302"
FT MUTAGEN 75
FT /note="W->S: Fails to bind ssDNA."
FT /evidence="ECO:0000269|PubMed:19609302"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2VLD"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 28..56
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 81..92
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 98..113
FT /evidence="ECO:0007829|PDB:2VLD"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2VLD"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:2VLD"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:2VLD"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:2VLD"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2VLD"
SQ SEQUENCE 251 AA; 28831 MW; 648BB6A7CE1E0EFC CRC64;
MRKVIIKENP SEEEIKELLD LAEKHGGVVT IFARCKVHYE GRAKSELGEG DRIIIIKPDG
SFLIHQNKKR EPVNWQPPGS KVTFKENSII SIRRRPYERL EVEIIEPYSL VVFLAEDYEE
LALTGSEAEM ANLIFENPRV IEEGFKPIYR EKPIRHGIVD VMGVDKDGNI VVLELKRRKA
DLHAVSQLKR YVDSLKEEYG ENVRGILVAP SLTEGAKKLL EKEGLEFRKL EPPKKGNEKR
SKQKTLDFFT P
