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Protein

Type-2 restriction enzyme Sau3AI

Gene

sau3AIR

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence GATC and cleaves before G-1.

Catalytic activityi

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

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium

Protein family/group databases

REBASEi1604. Sau3AI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme Sau3AI (EC:3.1.21.4)
Short name:
R.Sau3AI
Alternative name(s):
Endonuclease Sau3AI
Type II restriction enzyme Sau3AI
Gene namesi
Name:sau3AIR
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000773581 – 489Type-2 restriction enzyme Sau3AIAdd BLAST489

Structurei

Secondary structure

1489
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 17Combined sources11
Helixi22 – 26Combined sources5
Helixi38 – 44Combined sources7
Beta strandi64 – 72Combined sources9
Beta strandi78 – 82Combined sources5
Beta strandi84 – 88Combined sources5
Helixi91 – 95Combined sources5
Turni99 – 101Combined sources3
Helixi103 – 108Combined sources6
Beta strandi109 – 117Combined sources9
Helixi124 – 126Combined sources3
Beta strandi128 – 136Combined sources9
Turni137 – 139Combined sources3
Helixi141 – 159Combined sources19
Helixi163 – 165Combined sources3
Helixi168 – 170Combined sources3
Beta strandi171 – 178Combined sources8
Helixi183 – 185Combined sources3
Beta strandi186 – 189Combined sources4
Beta strandi192 – 197Combined sources6
Beta strandi199 – 203Combined sources5
Helixi205 – 215Combined sources11
Helixi229 – 232Combined sources4
Helixi237 – 245Combined sources9
Helixi246 – 248Combined sources3
Helixi253 – 259Combined sources7
Helixi269 – 278Combined sources10
Helixi294 – 299Combined sources6
Beta strandi301 – 308Combined sources8
Helixi325 – 329Combined sources5
Helixi343 – 350Combined sources8
Beta strandi352 – 360Combined sources9
Beta strandi366 – 374Combined sources9
Helixi378 – 382Combined sources5
Helixi384 – 398Combined sources15
Beta strandi401 – 406Combined sources6
Beta strandi413 – 418Combined sources6
Helixi423 – 425Combined sources3
Beta strandi427 – 436Combined sources10
Beta strandi440 – 443Combined sources4
Beta strandi446 – 448Combined sources3
Beta strandi454 – 457Combined sources4
Beta strandi466 – 470Combined sources5
Beta strandi472 – 476Combined sources5
Helixi478 – 485Combined sources8
Helixi486 – 488Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2REUX-ray1.90A233-489[»]
4PXGX-ray2.45A/B1-489[»]
ProteinModelPortaliP16667.
SMRiP16667.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16667.

Family & Domainsi

Family and domain databases

CDDicd00583. MutH_Sau3AI. 1 hit.
Gene3Di3.40.600.10. 2 hits.
InterProiIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PfamiPF02976. MutH. 1 hit.
[Graphical view]
SMARTiSM00927. MutH. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 2 hits.

Sequencei

Sequence statusi: Complete.

P16667-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESYLTKQAV HNRAKEAVGK SVLELNGGES IKQSKSSVGD AFENWFGKKK
60 70 80 90 100
DSDSKPDMAE AGVELKATPF KKLKNGKYSS KERLVLNIIN YEKVANENFE
110 120 130 140 150
TSSFLSKNNT IELAFYEYIK GTPSDNWIIK EAVLYEMHKN PIDYEIIKQD
160 170 180 190 200
WEIINQYINE GKAHELSEGL TSYLAPCTKG ANASSLRNQP YSDIKAKQRA
210 220 230 240 250
FSLKSGYMTS ILRKYVLGDE KIDSIVKDPF EIKEKSIEDI VFEKFQPYIN
260 270 280 290 300
WSIDKLCEHF SINKGEKGLN YRIASAILNL KGKTTKSKPF PEVEEFEKSS
310 320 330 340 350
IVVKTVHFNK KNVNKESMSF GAFKFEELAN EEWEDSEGYP SAQWRNFLLE
360 370 380 390 400
TRFLFFVVKE DEDGVDIFKG IKFFSMPEED INGPVKRMWD DTVKKLKEGV
410 420 430 440 450
TLEAVPDKST KDGWRIKNNF VDKSDDLICH VRPHTNNRDY RGGSNADKLP
460 470 480
KKINWINRPD SDDYSDEWMT KQSFWINNDY IKKQVEDLL
Length:489
Mass (Da):56,471
Last modified:August 1, 1990 - v1
Checksum:iFFC3762A949B86EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32470 Genomic DNA. Translation: AAA26672.1.
PIRiJQ0759.
RefSeqiWP_000446878.1. NZ_MCFM01000001.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32470 Genomic DNA. Translation: AAA26672.1.
PIRiJQ0759.
RefSeqiWP_000446878.1. NZ_MCFM01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2REUX-ray1.90A233-489[»]
4PXGX-ray2.45A/B1-489[»]
ProteinModelPortaliP16667.
SMRiP16667.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi1604. Sau3AI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP16667.

Family and domain databases

CDDicd00583. MutH_Sau3AI. 1 hit.
Gene3Di3.40.600.10. 2 hits.
InterProiIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PfamiPF02976. MutH. 1 hit.
[Graphical view]
SMARTiSM00927. MutH. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiT2S3_STAAU
AccessioniPrimary (citable) accession number: P16667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

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.