NUCA_NOSS1
ID NUCA_NOSS1 Reviewed; 274 AA.
AC P38446;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Nuclease;
DE EC=3.1.30.-;
DE AltName: Full=Endonuclease;
DE Flags: Precursor;
GN Name=nucA; OrderedLocusNames=all7362;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OG Plasmid pCC7120alpha.
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=1343821; DOI=10.1111/j.1365-2958.1992.tb01760.x;
RA Muro-Pastor A.M., Flores E., Herrero A., Wolk C.P.;
RT "Identification, genetic analysis and characterization of a sugar-non-
RT specific nuclease from the cyanobacterium Anabaena sp. PCC 7120.";
RL Mol. Microbiol. 6:3021-3030(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-274 OF MUTANT ALA-121 IN
RP COMPLEX WITH MANGANESE IONS, AND SUBUNIT.
RX PubMed=15897201; DOI=10.1074/jbc.m501798200;
RA Ghosh M., Meiss G., Pingoud A., London R.E., Pedersen L.C.;
RT "Structural insights into the mechanism of nuclease A, a betabeta alpha
RT metal nuclease from Anabaena.";
RL J. Biol. Chem. 280:27990-27997(2005).
CC -!- FUNCTION: Catalyzes the degradation of both RNA and DNA; has the
CC potential to act as an endonuclease.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Note=Divalent metal cations. The effectiveness of the cations are
CC Mn(2+) > Mg(2+) > Ca(2+) = Co(2+).;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15897201}.
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Periplasmic or loosely attached
CC to the cytoplasmic or the outer membrane.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: The active site contains 1 hydrated divalent metal
CC cation that has only 1 direct interaction with the protein; all other
CC interactions are via water molecules.
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000305}.
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DR EMBL; X64706; CAA45962.1; -; Genomic_DNA.
DR EMBL; BA000020; BAB77120.1; -; Genomic_DNA.
DR PIR; AB2523; AB2523.
DR PIR; S28039; S28039.
DR RefSeq; WP_010999911.1; NZ_RSCN01000106.1.
DR PDB; 1ZM8; X-ray; 1.90 A; A=25-274.
DR PDB; 2O3B; X-ray; 2.30 A; A=35-274.
DR PDBsum; 1ZM8; -.
DR PDBsum; 2O3B; -.
DR AlphaFoldDB; P38446; -.
DR SMR; P38446; -.
DR EnsemblBacteria; BAB77120; BAB77120; BAB77120.
DR GeneID; 58726894; -.
DR KEGG; ana:all7362; -.
DR OMA; YVMPNQV; -.
DR OrthoDB; 1438016at2; -.
DR EvolutionaryTrace; P38446; -.
DR Proteomes; UP000002483; Plasmid pCC7120alpha.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR040255; Non-specific_endonuclease.
DR PANTHER; PTHR13966; PTHR13966; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; Periplasm; Plasmid; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..274
FT /note="Nuclease"
FT /id="PRO_0000019913"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MUTAGEN 121
FT /note="D->A: Reduced activity by over 99%."
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1ZM8"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1ZM8"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:1ZM8"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1ZM8"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:1ZM8"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:1ZM8"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:1ZM8"
SQ SEQUENCE 274 AA; 29669 MW; 7F14170915AE59BF CRC64;
MGICGKLGVA ALVALIVGCS PVQSQVPPLT ELSPSISVHL LLGNPSGATP TKLTPDNYLM
VKNQYALSYN NSKGTANWVA WQLNSSWLGN AERQDNFRPD KTLPAGWVRV TPSMYSGSGY
DRGHIAPSAD RTKTTEDNAA TFLMTNMMPQ TPDNNRNTWG NLEDYCRELV SQGKELYIVA
GPNGSLGKPL KGKVTVPKST WKIVVVLDSP GSGLEGITAN TRVIAVNIPN DPELNNDWRA
YKVSVDELES LTGYDFLSNV SPNIQTSIES KVDN
