Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Type-1 restriction enzyme R protein

Gene

hsdR

Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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)DescriptionActionsGraphical viewLength
Nucleotide bindingi268 – 274ATPPROSITE-ProRule annotation7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Protein family/group databases

REBASEi11264. SsaAORF53P.

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:SSP0054
OrganismiStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Taxonomic identifieri342451 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000006371 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000772721 – 930Type-1 restriction enzyme R proteinAdd BLAST930

Proteomic databases

PRIDEiQ4A127.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi342451.SSP0054.

Structurei

3D structure databases

ProteinModelPortaliQ4A127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini254 – 418Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST165

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DZR. Bacteria.
COG0610. LUCA.
HOGENOMiHOG000003518.
KOiK01153.
OMAiQLEKHNK.
OrthoDBiPOG091H00V2.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006935. Helicase/UvrB_N.
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.

Q4A127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVYQSEFALE TEMMEQLKSN GYETVTIRNE QQLLDNFRSI LNERHADKLN
60 70 80 90 100
GDPLTDKEFQ RLLTMINGKG IFESARILRD KMPLKRDDES EVYLSFLDTR
110 120 130 140 150
HWCQNKFQIT NQVSVDDTYK ARYDVTILIN GLPLVQIELK RRGIDINEAF
160 170 180 190 200
NQVMRYRKQN YTGLFRYIQL FIISNGIDTR YISNNDGEIY KSHMFYWSDK
210 220 230 240 250
ENNRINTLNE FTETFLRPCH IAKMISRYMI LNETDNILMA MRPYQVHAVE
260 270 280 290 300
ALIHQATETS NNGYIWHTTG SGKTLTSFKA SQVLSEQDDI KKVIFLVDRK
310 320 330 340 350
DLDSQTEEEF NKFSKGSVDK TNNTAQLVKQ LKDKSLPLIV TTIQKMSKAI
360 370 380 390 400
QNNAEALDQY KTDKVVFIID ECHRSQFGDM HRIVRQHFNN AQYFGFTGTP
410 420 430 440 450
RFEENQSQDG RSTADIFGRC LHTYLIKDAI HDGNVLGFSV DYINTIKAQN
460 470 480 490 500
IDTETDELVE GINTDEVWLS DQRVELIARH ITENHDKYTR NRQYSAIFTV
510 520 530 540 550
QSIPALVKYY DAFKKISKDY EHPLKVAGVF SYAANEERNE GEVDEAHSRG
560 570 580 590 600
KLEEVIQDYN LNFGTNFSTD TFQEYFNHIS KNVKKGVKDN KIDVLIVVNM
610 620 630 640 650
FLTGFDSKVL NTLYVDKNLK YHDLIQAYSR TNRVEKETKP FGKIVNYRDL
660 670 680 690 700
KQNTDNALKL FSQTEDTDRV LMRDYDEYKA EFVDALAELK AVALKPQDMD
710 720 730 740 750
QVQDENEKKA FVEAFRLVSK LVLRLKAFDE FDFTKANIGM NEQEFEDYKS
760 770 780 790 800
KYFAIYDEVK PKRGEVEKVS ILNDIDFEIE ILRNDRINVS YIMDLVRQID
810 820 830 840 850
LKDKAEQQRN RDQIRRMLDN ADDPTLRLKR DLLREFIDDV IPELSEEDNI
860 870 880 890 900
DEAYILFENA KRESEFNQFA QQQAVDEQVL KDITGEYEYS GIVNQDHLKE
910 920 930
LVGDKKLREK RQTKKAVTSF VEEVSEKYSS
Length:930
Mass (Da):108,873
Last modified:September 13, 2005 - v1
Checksum:i559FA69A2AC96E24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE17199.1.
RefSeqiWP_002511775.1. NC_007350.1.

Genome annotation databases

EnsemblBacteriaiBAE17199; BAE17199; SSP0054.
GeneIDi3617259.
KEGGissp:SSP0054.
PATRICi19621587. VBIStaSap90642_0054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE17199.1.
RefSeqiWP_002511775.1. NC_007350.1.

3D structure databases

ProteinModelPortaliQ4A127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342451.SSP0054.

Protein family/group databases

REBASEi11264. SsaAORF53P.

Proteomic databases

PRIDEiQ4A127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE17199; BAE17199; SSP0054.
GeneIDi3617259.
KEGGissp:SSP0054.
PATRICi19621587. VBIStaSap90642_0054.

Phylogenomic databases

eggNOGiENOG4105DZR. Bacteria.
COG0610. LUCA.
HOGENOMiHOG000003518.
KOiK01153.
OMAiQLEKHNK.
OrthoDBiPOG091H00V2.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006935. Helicase/UvrB_N.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiHSDR_STAS1
AccessioniPrimary (citable) accession number: Q4A127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: November 2, 2016
This is version 76 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.