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Protein

Nuclease

Gene

nucA

Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / 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)DescriptionActionsGraphical viewLength
Active sitei124Proton acceptor1
Metal bindingi155Manganese 1; catalytic1
Metal bindingi246Manganese 2Sequence analysis1
Metal bindingi249Manganese 2Sequence analysis1
Metal bindingi255Manganese 3Sequence analysis1
Metal bindingi256Manganese 3; via carbonyl oxygenSequence analysis1
Metal bindingi265Manganese 3Sequence analysis1
Metal bindingi269Manganese 2Sequence analysis1

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 / SAG 25.82 / 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)DescriptionActionsGraphical viewLength
Mutagenesisi121D → A: Reduced activity by over 99%. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001991325 – 274NucleaseAdd BLAST250

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 40Combined sources3
Beta strandi57 – 61Combined sources5
Beta strandi66 – 70Combined sources5
Turni71 – 74Combined sources4
Beta strandi75 – 84Combined sources10
Helixi85 – 87Combined sources3
Helixi112 – 114Combined sources3
Turni115 – 117Combined sources3
Beta strandi121 – 126Combined sources6
Helixi128 – 130Combined sources3
Helixi135 – 140Combined sources6
Helixi144 – 146Combined sources3
Beta strandi147 – 150Combined sources4
Helixi152 – 156Combined sources5
Helixi158 – 171Combined sources14
Beta strandi176 – 184Combined sources9
Turni191 – 193Combined sources3
Beta strandi198 – 206Combined sources9
Helixi213 – 216Combined sources4
Beta strandi223 – 229Combined sources7
Helixi238 – 241Combined sources4
Helixi245 – 252Combined sources8
Turni256 – 259Combined sources4
Helixi262 – 270Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP38446.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000024365.
KOiK01173.
OMAiAYNETFY.
OrthoDBiPOG091H0GDR.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZM8X-ray1.90A25-274[»]
2O3BX-ray2.30A35-274[»]
ProteinModelPortaliP38446.
SMRiP38446.
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.
OrthoDBiPOG091H0GDR.

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...

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: November 2, 2016
This is version 106 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.