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Q99X26

- HSDR_STAAM

UniProt

Q99X26 - HSDR_STAAM

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Protein

Type-1 restriction enzyme R protein

Gene

hsdR

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - 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)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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-195-MONOMER.

Protein family/group databases

REBASEi5123. SauMu50ORF195P.

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:SAV0195
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Type-1 restriction enzyme R proteinPRO_0000077266Add
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

STRINGi158878.SAV0195.

Structurei

3D structure databases

ProteinModelPortaliQ99X26.
SMRiQ99X26. Positions 2-783.
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.
PhylomeDBiQ99X26.

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.

Q99X26-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAYQSEYALE NEMMNQLEQL GYERVTIRDN KQLLDNFRTI LNERHADKLE
60 70 80 90 100
GNPLTDKEFQ RLLTMIDGKS IFESARILRD KLPLRRDDES EIYLSFLDKK
110 120 130 140 150
SWCKNKFQVT NQVSVEDTYK ARYDVTILIN GLPLVQVELK RRGIDINEAF
160 170 180 190 200
NQVKRYRKQN YTGLFRYIQM FIISNGVETR YFSNNDSELL KSHMFYWSDK
210 220 230 240 250
QNNRINTLQS FAESFMRPCQ LAKMISRYMI INETDRILMA MRPYQVYAVE
260 270 280 290 300
ALIQQATETG NNGYVWHTTG SGKTLTSFKA SQILSQQDDI KKVIFLVDRK
310 320 330 340 350
DLDSQTEEEF NKFAKGAVDK TFNTSQLVRQ LNDKSLPLIV TTIQKMAKAI
360 370 380 390 400
QGNAHLLEQY KTNKVVFIID ECHRSQFGDM HRLVKQHFKN AQYFGFTGTP
410 420 430 440 450
RFPENSSQDG RTTADIFGRC LHTYLIRDAI HDGNVLGFSV DYINTFKNKA
460 470 480 490 500
LKAEDNSMVE AIDTEEVWLA DKRVELVTRH IINNHDKYTR NRQYSSIFTV
510 520 530 540 550
QSIHALIKYY ETFKRLNKKL EQPLTIAGIF TFKPNEDDRD GEVPYHSREK
560 570 580 590 600
LEIMISDYNK KFETNFSTDT TNEYFNHISK NVKKGVKDSK IDILIVVNMF
610 620 630 640 650
LTGFDSKVLN TLYVDKNLMY HDLIQAYSRT NRVEKESKPF GKIVNYRDLK
660 670 680 690 700
KETDDALRVF SQTNDTDTIL MRSYEEYKKE FMDAYRELKM IVPTPHMVDD
710 720 730 740 750
IQDEEELKRF VEAYRLLAKI ILRLKAFDEF EFTIDEIGMD EQENEDYKSK
760 770 780 790 800
YLAVYDQVKR ATAEKNKVSI LNDIDFEIEM MRNDTINVNY IMNILRQIDL
810 820 830 840 850
EDKAEQRRNQ EQIRRILDHA DDPTLRLKRD LIREFIDNVV PSLNKDDDID
860 870 880 890 900
QEYVNFESIK KEAEFKGFAG ERSIDEQALK TISNDYQYSG VVNPHHLKKM
910 920
IGDLPLKEKR KARKAIESFV AETTEKYGV
Length:929
Mass (Da):109,294
Last modified:June 1, 2001 - v1
Checksum:i7814981B5A925187
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB56357.1.
RefSeqiNP_370719.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB56357; BAB56357; SAV0195.
GeneIDi1120154.
KEGGisav:SAV0195.
PATRICi19560997. VBIStaAur52173_0196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB56357.1 .
RefSeqi NP_370719.1. NC_002758.2.

3D structure databases

ProteinModelPortali Q99X26.
SMRi Q99X26. Positions 2-783.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158878.SAV0195.

Protein family/group databases

REBASEi 5123. SauMu50ORF195P.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB56357 ; BAB56357 ; SAV0195 .
GeneIDi 1120154.
KEGGi sav:SAV0195.
PATRICi 19560997. VBIStaAur52173_0196.

Phylogenomic databases

eggNOGi COG0610.
HOGENOMi HOG000003518.
KOi K01153.
OMAi NNGYIWH.
OrthoDBi EOG6JTCB4.
PhylomeDBi Q99X26.

Enzyme and pathway databases

BioCyci SAUR158878:GJJ5-195-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: Mu50 / ATCC 700699.

Entry informationi

Entry nameiHSDR_STAAM
AccessioniPrimary (citable) accession number: Q99X26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: October 1, 2014
This is version 87 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