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Protein

Type-2 restriction enzyme StsI

Gene

stsIR

Organism
Streptococcus sanguinis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequences GGATG and CATCC and cleaves respectively 15 bases after G-1 and 14 bases before C-1.

Catalytic activityi

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Protein family/group databases

REBASEi1784. StsI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme StsI (EC:3.1.21.4)
Short name:
R.StsI
Alternative name(s):
Endonuclease StsI
Type II restriction enzyme StsI
Gene namesi
Name:stsIR
OrganismiStreptococcus sanguinis
Taxonomic identifieri1305 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 602601Type-2 restriction enzyme StsIPRO_0000077368Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP29346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.91.30. 1 hit.
InterProiIPR011335. Restrct_endonuc-II-like.
IPR011578. Restrct_endonuc_C/endonuc_I.
IPR015334. Restrct_endonuc_II_FokI_C.
IPR004233. Restrct_endonuc_II_FokI_cat.
IPR004234. Restrct_endonuc_II_FokI_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P29346-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTISINEYSD LNNLAFGLGQ DVSQDLKELV KVASIFMPDS KIHKWLIDTR
60 70 80 90 100
LEEVVTDLNL RYELKSVITN TPISVTWKQL TGTRTKREAN SLVQAVFPGQ
110 120 130 140 150
CSRLAIVDWA AKNYVSVAVA FGLLKFHRAD KTFTISEIGI QAVKLYDSEE
160 170 180 190 200
LAELDKFLYE RLLEYPYAAW LIRLLGNQPS KQFSKFDLGE HFGFIDELGF
210 220 230 240 250
ETAPIEIFLN GLAQAEIDGD KTAAQKIKSN FESTSDKYMR WLAGVLVTAG
260 270 280 290 300
LATSTTKKVT HTYKNRKFEL TLGTVYQITA KGLTALKEVN GKSRYPRSRK
310 320 330 340 350
RVMWEFLATK DKEAIAKKTS RSLMLKHLTE KKNPIQAEVI ATLINTDYPT
360 370 380 390 400
LEITPEEVID DCIGLNRIGI EILIDGDKLT LNDKLFDFEI PVQKDVVLEK
410 420 430 440 450
SDIEKFKNQL RTELTNIDHS YLKGIDIASK KKTSNVENTE FEAISTKIFT
460 470 480 490 500
DELGFSGKHL GGSNKPDGLL WDDDCAIILD SKAYSEGFPL TASHTDAMGR
510 520 530 540 550
YLRQFTERKE EIKPTWWDIA PEHLDNTYFA YVSGSFSGNY KEQLQKFRQD
560 570 580 590 600
TNHLGGALEF VKLLLLANNY KTQKMSKKEV KKSILDYNIS YEEYAPLLAE

IE
Length:602
Mass (Da):68,392
Last modified:January 23, 2007 - v2
Checksum:i8FFCC465145F5B99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11101 Genomic DNA. Translation: BAA01875.1.
PIRiS35495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11101 Genomic DNA. Translation: BAA01875.1.
PIRiS35495.

3D structure databases

ProteinModelPortaliP29346.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi1784. StsI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.91.30. 1 hit.
InterProiIPR011335. Restrct_endonuc-II-like.
IPR011578. Restrct_endonuc_C/endonuc_I.
IPR015334. Restrct_endonuc_II_FokI_C.
IPR004233. Restrct_endonuc_II_FokI_cat.
IPR004234. Restrct_endonuc_II_FokI_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence analysis of the StsI restriction-modification gene: presence of homology to FokI restriction-modification enzymes."
    Kita K., Suisha M., Kotani H., Yanase H., Kato N.
    Nucleic Acids Res. 20:4167-4172(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22.
    Strain: 54.

Entry informationi

Entry nameiT2S1_STRSA
AccessioniPrimary (citable) accession number: P29346
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

External Data

Dasty 3

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 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.