Reviewed, UniProtKB/Swiss-Prot P56200 (T2CX_CITFR)

Names and origin

Protein names

Recommended name:
    Type-2 restriction enzyme Cfr10I
      Short name=R.Cfr10I
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme Cfr10I
    Endonuclease Cfr10I

Gene names

Name:

cfr10IR

Organism

Citrobacter freundii

Taxonomic identifier

546 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes the double-stranded sequence RCCGGY and cleaves after R-1.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Binds 2 magnesium ions per subunit.

Ontologies

Keywords
Biological process	Restriction system
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure
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

Chain

1 – 285

285

Type-2 restriction enzyme Cfr10I

PRO_0000077295

Sites

Metal binding

134

1

Magnesium 1 By similarity

Metal binding

134

1

Magnesium 2 By similarity

Metal binding

204

1

Magnesium 1 Probable

Secondary structure

1

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285

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

12 – 15

4

Helix

17 – 26

10

Turn

30 – 32

3

Helix

35 – 53

19

Helix

59 – 84

26

Beta strand

88 – 93

6

Turn

97 – 99

3

Helix

102 – 105

4

Helix

108 – 123

16

Beta strand

134 – 139

6

Helix

144 – 150

7

Turn

151 – 153

3

Helix

161 – 169

9

Helix

170 – 174

5

Turn

180 – 182

3

Beta strand

183 – 189

7

Helix

195 – 218

24

Beta strand

228 – 235

8

Helix

238 – 244

7

Helix

249 – 252

4

Beta strand

261 – 268

8

Helix

272 – 282

11

Sequences

	Sequence		Length	Mass (Da)
	P56200-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 5F95F49ED058D743	FASTA	285	32,016
	10 20 30 40 50 60 MDIISKSGEG NKYTINSAIA FVAYASHIDI NTTEFSKVLS GLRDFINDEA IRLGGKISDG 70 80 90 100 110 120 SFNKCNGDWY EWLIGIRAIE FFLESETNFI VVKMPNATSF DVMSIYKSCL SEFIYDLRSK 130 140 150 160 170 180 LSLNNVNLIT SNPDFSIIDI RGRREELKSM LKDISFSNIS LSTISEIDNL YKNFIDYAEL 190 200 210 220 230 240 EHIKSFLSVK TTFRPDRRLQ LAHEGSLMKA LYTHLQTRTW TINPTGIRYY AAATSIGNAD 250 260 270 280 VIGLKTVATH SITDVKSLPQ SAVDEIFKIN SVLDVDSCLS HILSS

References

[1]	"Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15-A resolution." Bozic D., Grazulis S., Siksnys V., Huber R. J. Mol. Biol. 255:176-186(1996) [PubMed: 8568865] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). Strain: RFL10.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CFR	X-ray	2.15	A	1-285	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.1.21.4. 2347.

Family and domain databases

InterPro

IPR011544. Restrct_endonuc_II_Cfr10/BsoB1.
IPR011335. Restrict_endonuc_II-like_core.
[Graphical view]

Gene3D

G3DSA:3.40.91.10. Restrct_endonuc_II_Cfr10/BsoB1. 1 hit.

ProtoNet

Search...

Entry information

Entry name

T2CX_CITFR

Accession

Primary (citable) accession number: P56200

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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