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P16667

- T2S3_STAAU

UniProt

P16667 - T2S3_STAAU

Protein

Type-2 restriction enzyme Sau3AI

Gene

sau3AIR

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (16 Apr 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    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

    Magnesium.

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

    GO - Biological processi

    1. DNA restriction-modification system Source: UniProtKB-KW

    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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489Type-2 restriction enzyme Sau3AIPRO_0000077358Add
    BLAST

    Structurei

    Secondary structure

    1
    489
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi237 – 2459
    Helixi246 – 2483
    Helixi253 – 2597
    Helixi269 – 27810
    Beta strandi301 – 3088
    Helixi325 – 3295
    Helixi343 – 3508
    Beta strandi352 – 3609
    Beta strandi366 – 3749
    Helixi378 – 3825
    Helixi384 – 39815
    Beta strandi401 – 4066
    Beta strandi413 – 4186
    Helixi423 – 4253
    Beta strandi427 – 43610
    Beta strandi440 – 4434
    Beta strandi446 – 4483
    Beta strandi454 – 4574
    Beta strandi466 – 4705
    Beta strandi472 – 4765
    Helixi478 – 4858
    Helixi486 – 4883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2REUX-ray1.90A233-489[»]
    ProteinModelPortaliP16667.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16667.

    Family & Domainsi

    Family and domain databases

    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

    MESYLTKQAV HNRAKEAVGK SVLELNGGES IKQSKSSVGD AFENWFGKKK    50
    DSDSKPDMAE AGVELKATPF KKLKNGKYSS KERLVLNIIN YEKVANENFE 100
    TSSFLSKNNT IELAFYEYIK GTPSDNWIIK EAVLYEMHKN PIDYEIIKQD 150
    WEIINQYINE GKAHELSEGL TSYLAPCTKG ANASSLRNQP YSDIKAKQRA 200
    FSLKSGYMTS ILRKYVLGDE KIDSIVKDPF EIKEKSIEDI VFEKFQPYIN 250
    WSIDKLCEHF SINKGEKGLN YRIASAILNL KGKTTKSKPF PEVEEFEKSS 300
    IVVKTVHFNK KNVNKESMSF GAFKFEELAN EEWEDSEGYP SAQWRNFLLE 350
    TRFLFFVVKE DEDGVDIFKG IKFFSMPEED INGPVKRMWD DTVKKLKEGV 400
    TLEAVPDKST KDGWRIKNNF VDKSDDLICH VRPHTNNRDY RGGSNADKLP 450
    KKINWINRPD SDDYSDEWMT KQSFWINNDY IKKQVEDLL 489
    Length:489
    Mass (Da):56,471
    Last modified:August 1, 1990 - v1
    Checksum:iFFC3762A949B86EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32470 Genomic DNA. Translation: AAA26672.1.
    PIRiJQ0759.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32470 Genomic DNA. Translation: AAA26672.1 .
    PIRi JQ0759.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2REU X-ray 1.90 A 233-489 [» ]
    ProteinModelPortali P16667.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 1604. Sau3AI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P16667.

    Family and domain databases

    Gene3Di 3.40.600.10. 2 hits.
    InterProi IPR011337. DNA_rep_MutH/RE_typeII.
    IPR011335. Restrct_endonuc-II-like.
    [Graphical view ]
    Pfami PF02976. MutH. 1 hit.
    [Graphical view ]
    SMARTi SM00927. MutH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52980. SSF52980. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and characterization of the Sau3AI restriction and modification genes in Staphylococcus carnosus TM300."
      Seeber S., Kessler C., Goetz F.
      Gene 94:37-43(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49834 / 3A.

    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: April 16, 2014
    This is version 81 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

    External Data

    Dasty 3