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Protein

Nuclease

Gene

nucA

Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of both DNA and RNA, double- or single-stranded, at the 3'position of the phosphodiester bond to produce 5'-phosphorylated mono-, di-, tri- and tetranucleotides. DNA is a slightly better substrate than RNA.

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.PROSITE-ProRule annotation

Cofactori

Mg2+Note: Binds 1 Mg2+ ion.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei110Proton acceptorPROSITE-ProRule annotation1 Publication1
Metal bindingi140Magnesium; catalytic1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.30.2. 5690.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclease (EC:3.1.30.2)
Alternative name(s):
Endonuclease
Cleaved into the following 3 chains:
Gene namesi
Name:nucA
Synonyms:nuc
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78R → A: Reduced activity 1000-fold. 1 Publication1
Mutagenesisi78R → K: Reduced activity 100-fold. 1 Publication1
Mutagenesisi108R → A: Reduced activity 1000-fold. 1 Publication1
Mutagenesisi108R → K: Reduced activity 50-fold. 1 Publication1
Mutagenesisi110H → A, D, E, K or Q: Reduced activity 100000-fold. 1 Publication1
Mutagenesisi110H → N: Reduced activity 1000-fold. 1 Publication1
Mutagenesisi140N → A, D or H: Reduced activity over 10000-fold. 1 Publication1
Mutagenesisi140N → Q: Reduced activity 1000-fold. 1 Publication1
Mutagenesisi148E → A, D or Q: Reduced activity over 800-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000001991422 – 266Nuclease isoform Sm2Add BLAST245
ChainiPRO_000001991523 – 266Nuclease isoform Sm3Add BLAST244
ChainiPRO_000001991625 – 266Nuclease isoform Sm1Add BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 34
Disulfide bondi222 ↔ 264

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP13717.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 32Combined sources4
Beta strandi39 – 42Combined sources4
Beta strandi50 – 53Combined sources4
Turni55 – 57Combined sources3
Beta strandi58 – 67Combined sources10
Helixi88 – 90Combined sources3
Helixi94 – 97Combined sources4
Helixi100 – 104Combined sources5
Beta strandi106 – 112Combined sources7
Helixi114 – 117Combined sources4
Helixi123 – 127Combined sources5
Helixi129 – 131Combined sources3
Beta strandi132 – 136Combined sources5
Helixi137 – 140Combined sources4
Helixi143 – 153Combined sources11
Helixi154 – 156Combined sources3
Beta strandi163 – 170Combined sources8
Beta strandi189 – 197Combined sources9
Turni201 – 203Combined sources3
Beta strandi206 – 212Combined sources7
Helixi221 – 224Combined sources4
Helixi228 – 235Combined sources8
Beta strandi238 – 240Combined sources3
Helixi245 – 251Combined sources7
Helixi258 – 261Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G8TX-ray1.10A/B22-266[»]
1QAEX-ray2.05A/B22-266[»]
1QL0X-ray1.10A/B26-266[»]
1SMNX-ray2.04A/B22-266[»]
4E3YX-ray0.95A/B22-266[»]
ProteinModelPortaliP13717.
SMRiP13717.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13717.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

P13717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFNNKMLAL AALLFAAQAS ADTLESIDNC AVGCPTGGSS NVSIVRHAYT
60 70 80 90 100
LNNNSTTKFA NWVAYHITKD TPASGKTRNW KTDPALNPAD TLAPADYTGA
110 120 130 140 150
NAALKVDRGH QAPLASLAGV SDWESLNYLS NITPQKSDLN QGAWARLEDQ
160 170 180 190 200
ERKLIDRADI SSVYTVTGPL YERDMGKLPG TQKAHTIPSA YWKVIFINNS
210 220 230 240 250
PAVNHYAAFL FDQNTPKGAD FCQFRVTVDE IEKRTGLIIW AGLPDDVQAS
260
LKSKPGVLPE LMGCKN
Length:266
Mass (Da):28,945
Last modified:February 1, 1996 - v2
Checksum:iA0FF0C1430677B9E
GO

Mass spectrometryi

Molecular mass is 26708.2 Da from positions 22 - 266. Determined by ESI. Isoform Sm2.1 Publication
Molecular mass is 26591.8 Da from positions 23 - 266. Determined by ESI. Isoform Sm3.1 Publication
Molecular mass is 26376.4 Da from positions 25 - 266. Determined by ESI. Isoform Sm1.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19495 Genomic DNA. Translation: AAA26560.1.
RefSeqiWP_015377376.1. NZ_LQAK01000005.1.

Genome annotation databases

GeneIDi23387471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19495 Genomic DNA. Translation: AAA26560.1.
RefSeqiWP_015377376.1. NZ_LQAK01000005.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G8TX-ray1.10A/B22-266[»]
1QAEX-ray2.05A/B22-266[»]
1QL0X-ray1.10A/B26-266[»]
1SMNX-ray2.04A/B22-266[»]
4E3YX-ray0.95A/B22-266[»]
ProteinModelPortaliP13717.
SMRiP13717.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP13717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23387471.

Enzyme and pathway databases

BRENDAi3.1.30.2. 5690.

Miscellaneous databases

EvolutionaryTraceiP13717.

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_SERMA
AccessioniPrimary (citable) accession number: P13717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.