Reviewed, UniProtKB/Swiss-Prot P21763 (T2R1_RHOSH)

Names and origin

Protein names

Recommended name:
    Type-2 restriction enzyme RsrI
      Short name=R.RsrI
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme RsrI
    Endonuclease RsrI

Gene names

Name:

rsrIR

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes the double-stranded sequence GAATTC and cleaves after G-1.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Magnesium.
Subunit structure	Homodimer.

Ontologies

Keywords
Biological process	Restriction system
Ligand	Magnesium
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro Type II site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.2
	Chain	2 – 277	276	Type-2 restriction enzyme RsrI		PRO_0000077357

Sequences

	Sequence		Length	Mass (Da)
	P21763-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 672E812D258E70B2	FASTA	277	30,630
	10 20 30 40 50 60 MAGEVEFKGK GQALRLGIQQ ELGGGPLSIF GAAAQKHDLS IREVTAGVLT KLAEDFPNLE 70 80 90 100 110 120 FQLRTSLTKK AINEKLRSFD PRLGQALFVE SASIRPDGGI TEVKDRHGNW RVILVGESKH 130 140 150 160 170 180 QGNDVEKILA GVLQGKAKDQ DFMAAGNAIE RMHKNVLELR NYMLDEKHFP YVVFLQGSNF 190 200 210 220 230 240 ATESFEVTRP DGRVVKIVHD SGMLNRIDRV TASSLSREIN QNYCENIVVR AGSFDHMFQI 250 260 270 ASLYCKAAPW TAGEMAEAML AVAKTSLRII ADDLDQN

References

[1]	"Comparison of the nucleotide and amino acid sequences of the RsrI and EcoRI restriction endonucleases." Stephenson F.H., Ballard B.T., Boyer H.W., Rosenberg J.M., Greene P.J. Gene 85:1-13(1989) [PubMed: 2695392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-35.
[2]	"Restriction endonuclease RsrI from Rhodobacter sphaeroides, an isoschizomer of EcoRI: purification and properties." Aiken C., Gumport R.I. Nucleic Acids Res. 16:7901-7916(1988) [PubMed: 2843805] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-41.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X14697 Genomic DNA. Translation: CAA32827.1.
PIR	JW0016. S03688.
3D structure databases
HSSP	HSSP built from PDB template 1CKQ based on UniProtKB P00642.
ModBase	Search...
Protein family/group databases
REBASE	1572. RsrI.
Enzyme and pathway databases
BRENDA	3.1.21.4. 2796.
Family and domain databases
InterPro	IPR004221. Restrict_endonuc_II_EcoRI. IPR011336. Restrict_endonuc_II_EcoRI/MunI. IPR018131. Restrict_endonuc_II_EcoRI_Pbac. [Graphical view]
Gene3D	G3DSA:3.40.580.10. Restrict_endonuc_II_EcoRI/MunI. 1 hit.
Pfam	PF02963. EcoRI. 1 hit. [Graphical view]
PIRSF	PIRSF001002. Restrict_endonuc_II_EcoRI. 1 hit.
ProDom	PD039825. EcoRI. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

T2R1_RHOSH

Accession

Primary (citable) accession number: P21763

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)