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Protein

Nuclease

Gene

nucA

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the degradation of both RNA and DNA; has the potential to act as an endonuclease.

Cofactori

Mn2+, Mg2+, Ca2+, Co2+Note: Divalent metal cations. The effectiveness of the cations are Mn2+ > Mg2+ > Ca2+ = Co2+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Proton acceptor
Metal bindingi155 – 1551Manganese 1; catalytic
Metal bindingi246 – 2461Manganese 2Sequence analysis
Metal bindingi249 – 2491Manganese 2Sequence analysis
Metal bindingi255 – 2551Manganese 3Sequence analysis
Metal bindingi256 – 2561Manganese 3; via carbonyl oxygenSequence analysis
Metal bindingi265 – 2651Manganese 3Sequence analysis
Metal bindingi269 – 2691Manganese 2Sequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclease (EC:3.1.30.-)
Alternative name(s):
Endonuclease
Gene namesi
Name:nucA
Ordered Locus Names:all7362
Encoded oniPlasmid pCC7120alpha0 Publication
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
Proteomesi
  • UP000002483 Componenti: Plasmid pCC7120alpha

Subcellular locationi

  • Periplasm

  • Note: Periplasmic or loosely attached to the cytoplasmic or the outer membrane.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211D → A: Reduced activity by over 99%.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 274250NucleasePRO_0000019913Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 403Combined sources
Beta strandi57 – 615Combined sources
Beta strandi66 – 705Combined sources
Turni71 – 744Combined sources
Beta strandi75 – 8410Combined sources
Helixi85 – 873Combined sources
Helixi112 – 1143Combined sources
Turni115 – 1173Combined sources
Beta strandi121 – 1266Combined sources
Helixi128 – 1303Combined sources
Helixi135 – 1406Combined sources
Helixi144 – 1463Combined sources
Beta strandi147 – 1504Combined sources
Helixi152 – 1565Combined sources
Helixi158 – 17114Combined sources
Beta strandi176 – 1849Combined sources
Turni191 – 1933Combined sources
Beta strandi198 – 2069Combined sources
Helixi213 – 2164Combined sources
Beta strandi223 – 2297Combined sources
Helixi238 – 2414Combined sources
Helixi245 – 2528Combined sources
Turni256 – 2594Combined sources
Helixi262 – 2709Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZM8X-ray1.90A25-274[»]
2O3BX-ray2.30A35-274[»]
ProteinModelPortaliP38446.
SMRiP38446. Positions 35-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38446.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000024365.
KOiK01173.
OMAiAYNETFY.
OrthoDBiEOG6KWXVS.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
InterProiIPR018524. DNA/RNA_endonuclease_AS.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR020821. Extracellular_endonuc_su_A.
[Graphical view]
PfamiPF01223. Endonuclease_NS. 1 hit.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
[Graphical view]
PROSITEiPS01070. NUCLEASE_NON_SPEC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGICGKLGVA ALVALIVGCS PVQSQVPPLT ELSPSISVHL LLGNPSGATP
60 70 80 90 100
TKLTPDNYLM VKNQYALSYN NSKGTANWVA WQLNSSWLGN AERQDNFRPD
110 120 130 140 150
KTLPAGWVRV TPSMYSGSGY DRGHIAPSAD RTKTTEDNAA TFLMTNMMPQ
160 170 180 190 200
TPDNNRNTWG NLEDYCRELV SQGKELYIVA GPNGSLGKPL KGKVTVPKST
210 220 230 240 250
WKIVVVLDSP GSGLEGITAN TRVIAVNIPN DPELNNDWRA YKVSVDELES
260 270
LTGYDFLSNV SPNIQTSIES KVDN
Length:274
Mass (Da):29,669
Last modified:October 1, 1994 - v1
Checksum:i7F14170915AE59BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64706 Genomic DNA. Translation: CAA45962.1.
BA000020 Genomic DNA. Translation: BAB77120.1.
PIRiAB2523.
S28039.
RefSeqiWP_010999911.1. NC_003276.1.

Genome annotation databases

EnsemblBacteriaiBAB77120; BAB77120; BAB77120.
KEGGiana:all7362.
PATRICi22782505. VBINosSp37423_6664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64706 Genomic DNA. Translation: CAA45962.1.
BA000020 Genomic DNA. Translation: BAB77120.1.
PIRiAB2523.
S28039.
RefSeqiWP_010999911.1. NC_003276.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZM8X-ray1.90A25-274[»]
2O3BX-ray2.30A35-274[»]
ProteinModelPortaliP38446.
SMRiP38446. Positions 35-274.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB77120; BAB77120; BAB77120.
KEGGiana:all7362.
PATRICi22782505. VBINosSp37423_6664.

Phylogenomic databases

HOGENOMiHOG000024365.
KOiK01173.
OMAiAYNETFY.
OrthoDBiEOG6KWXVS.

Miscellaneous databases

EvolutionaryTraceiP38446.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
InterProiIPR018524. DNA/RNA_endonuclease_AS.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR020821. Extracellular_endonuc_su_A.
[Graphical view]
PfamiPF01223. Endonuclease_NS. 1 hit.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
[Graphical view]
PROSITEiPS01070. NUCLEASE_NON_SPEC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. PCC 7120."
    Muro-Pastor A.M., Flores E., Herrero A., Wolk C.P.
    Mol. Microbiol. 6:3021-3030(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.
  3. "Structural insights into the mechanism of nuclease A, a betabeta alpha metal nuclease from Anabaena."
    Ghosh M., Meiss G., Pingoud A., London R.E., Pedersen L.C.
    J. Biol. Chem. 280:27990-27997(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-274 OF MUTANT ALA-121 IN COMPLEX WITH MANGANESE IONS, SUBUNIT.

Entry informationi

Entry nameiNUCA_NOSS1
AccessioniPrimary (citable) accession number: P38446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: December 9, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site contains 1 hydrated divalent metal cation that has only 1 direct interaction with the protein; all other interactions are via water molecules.

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.