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Q6GCT1

- HSDR_STAAS

UniProt

Q6GCT1 - HSDR_STAAS

Protein

Type-1 restriction enzyme R protein

Gene

hsdR

Organism
Staphylococcus aureus (strain MSSA476)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Subunit R is required for both nuclease and ATPase activities, but not for modification.By similarity

    Catalytic activityi

    Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi268 – 2747ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. Type I site-specific deoxyribonuclease activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Restriction system

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Protein family/group databases

    REBASEi9413. SauMSSORF170P.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type-1 restriction enzyme R protein (EC:3.1.21.3)
    Alternative name(s):
    Type I restriction enzyme R protein
    Gene namesi
    Name:hsdR
    Ordered Locus Names:SAS0170
    OrganismiStaphylococcus aureus (strain MSSA476)
    Taxonomic identifieri282459 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002201: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 929929Type-1 restriction enzyme R proteinPRO_0000077269Add
    BLAST

    Interactioni

    Subunit structurei

    The type I restriction/modification system is composed of three polypeptides R, M and S.By similarity

    Protein-protein interaction databases

    STRINGi282459.SAS0170.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6GCT1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini254 – 418165Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the HsdR family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0610.
    HOGENOMiHOG000003518.
    KOiK01153.
    OMAiNNGYIWH.
    OrthoDBiEOG6JTCB4.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR027417. P-loop_NTPase.
    IPR007409. Restrct_endonuc_type1_HsdR_N.
    IPR004473. Restrct_endonuc_typeI_HsdR.
    IPR022625. TypeI_RM_Rsu_C.
    [Graphical view]
    PfamiPF12008. EcoR124_C. 1 hit.
    PF04313. HSDR_N. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00348. hsdR. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6GCT1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYQSEYALE NEMMNQLEQL GYERVTIRDN KQLLDNFRTI LNERHADKLE    50
    GNPLTDKEFQ RLLTMIDGKS IFESARILRD KLPLRRDDES EVYLSFLDTK 100
    SWCKNKFQVT NQVSVEDTYK ARYDVTILIN GLPLVQVELK RRGIDINEAF 150
    NQVKRYRKQN YTGLFRYIQM FIISNGVETR YFSNNDSELL KSHMFYWSDK 200
    QNNRINTLQS FAESFMRPCQ LAKMISRYMI INETDRILMA MRPYQVYAVE 250
    ALIQQATETG NNGYVWHTTG SGKTLTSFKA SQILSQQDDI KKVIFLVDRK 300
    DLDSQTEEEF NKFAKGAVDK TFNTSQLVRQ LNDKSLPLIV TTIQKMAKAI 350
    QGNAHLLEQY KTNKVVFIID ECHRSQFGDM HRLVKQHFKN AQYFGFTGTP 400
    RFPENSSQDG RTTADIFGRC LHTYLIRDAI HDGNVLGFSV DYINTFKNKA 450
    LKAEDNSMVE AIDTEEVWLA DKRVELVTRH IINNHDKYTR NRQYSSIFTV 500
    QSIHALIKYY ETFKRLNKKL EQPLTIAGIF TFKPNEDDRD GEVPYHSREK 550
    LEIMISDYNK KFETNFSTDT TNEYFNHISK NVKKGVKDSK IDILIVVNMF 600
    LTGFDSKVLN TLYVDKNLMY HDLIQAYSRT NRVEKESKPF GKIVNYRDLK 650
    KETDDALRVF SQTNDTDTIL MRSYEEYKKE FMDAYRELKM IVPTPHMVDD 700
    IQDEEELKRF VEAYRLLAKI ILRLKAFDEF EFTIDEIGMD EQENEDYKSK 750
    YLAVYDQVKR ATAEKNKVSI LNDIDFEIEM MRNDTINVNY IMNILRQIDL 800
    EDKAEQRRNQ EQIRRILDHA DDPTLRLKRD LIREFIDNVV PSLNKDDDID 850
    QEYVNFESIK KEAEFKGFAG ERSIDEQALK TISNDYQYSG VVNPHHLKKM 900
    IGDLPLKEKR KARKAIESFV AETTEKYGV 929
    Length:929
    Mass (Da):109,253
    Last modified:July 19, 2004 - v1
    Checksum:i1F8E22880C217804
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571857 Genomic DNA. Translation: CAG41938.1.
    RefSeqiYP_042292.1. NC_002953.3.

    Genome annotation databases

    GeneIDi2862691.
    KEGGisas:SAS0170.
    PATRICi19549686. VBIStaAur96780_0181.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571857 Genomic DNA. Translation: CAG41938.1 .
    RefSeqi YP_042292.1. NC_002953.3.

    3D structure databases

    ProteinModelPortali Q6GCT1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 282459.SAS0170.

    Protein family/group databases

    REBASEi 9413. SauMSSORF170P.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2862691.
    KEGGi sas:SAS0170.
    PATRICi 19549686. VBIStaAur96780_0181.

    Phylogenomic databases

    eggNOGi COG0610.
    HOGENOMi HOG000003518.
    KOi K01153.
    OMAi NNGYIWH.
    OrthoDBi EOG6JTCB4.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR027417. P-loop_NTPase.
    IPR007409. Restrct_endonuc_type1_HsdR_N.
    IPR004473. Restrct_endonuc_typeI_HsdR.
    IPR022625. TypeI_RM_Rsu_C.
    [Graphical view ]
    Pfami PF12008. EcoR124_C. 1 hit.
    PF04313. HSDR_N. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00348. hsdR. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MSSA476.

    Entry informationi

    Entry nameiHSDR_STAAS
    AccessioniPrimary (citable) accession number: Q6GCT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and magnesium as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.By similarity

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3