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Q7A801

- HSDR_STAAN

UniProt

Q7A801 - HSDR_STAAN

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Protein

Type-1 restriction enzyme R protein

Gene
hsdR, SA0189
Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 – 2747ATP By similarity

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-195-MONOMER.

Protein family/group databases

REBASEi5117. SauN315ORF189P.

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:SA0189
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Type-1 restriction enzyme R proteinPRO_0000077267Add
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

STRINGi158879.SA0189.

Structurei

3D structure databases

ProteinModelPortaliQ7A801.
SMRiQ7A801. Positions 2-783.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 418165Helicase ATP-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the HsdR family.

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.

Q7A801-1 [UniParc]FASTAAdd to Basket

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MAYQSEYALE NEMMNQLEQL GYERVTIRDN KQLLDNFRTI LNERHADKLE    50
GNPLTDKEFQ RLLTMIDGKS IFESARILRD KLPLRRDDES EIYLSFLDKK 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):109,294
Last modified:July 5, 2004 - v1
Checksum:i7814981B5A925187
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41410.1.
PIRiG89781.
RefSeqiNP_373432.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB41410; BAB41410; BAB41410.
GeneIDi1122965.
KEGGisau:SA0189.
PATRICi19572417. VBIStaAur116463_0198.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41410.1 .
PIRi G89781.
RefSeqi NP_373432.1. NC_002745.2.

3D structure databases

ProteinModelPortali Q7A801.
SMRi Q7A801. Positions 2-783.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0189.

Protein family/group databases

REBASEi 5117. SauN315ORF189P.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB41410 ; BAB41410 ; BAB41410 .
GeneIDi 1122965.
KEGGi sau:SA0189.
PATRICi 19572417. VBIStaAur116463_0198.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SAUR158879:GJCB-195-MONOMER.

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: N315.
  2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiHSDR_STAAN
AccessioniPrimary (citable) accession number: Q7A801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 77 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

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