Reviewed, UniProtKB/Swiss-Prot P25239 (T257_ECOLX)

Names and origin

Protein names

Recommended name:
    Type IIS restriction enzyme Eco57I
    EC=3.1.21.4
Alternative name(s):
    Endonuclease Eco57I
Including the following 1 domains:
    1- Recommended name:
            Adenine-specific methyltransferase activity Eco57IA
                Short name=M.Eco57IA
              EC=2.1.1.72

Gene names

Name:

eco57IR

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	998 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes the double-stranded sequences CTGAAG and CTTCAG and cleaves respectively 22 bases after C-1 and 14 bases before C'-1. Also acts as a methylase that causes specific methylation on A-5 on one strand, the other strand being methylated by the Eco57IB methylase.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
Subunit structure	Monomer.

Ontologies

Keywords
Biological process	Restriction system
Molecular function	Endonuclease Hydrolase Methyltransferase Nuclease Transferase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 998	998	Type IIS restriction enzyme Eco57I
Experimental info
	Sequence conflict	42	1	I → L in AAA23389. Ref.1
	Sequence conflict	207	1	R → G in AAA23389. Ref.1
	Sequence conflict	299 – 321	23	WSIIE…FSSDI → EHHRTIILPHKAHTLSLFSL LIF in AAA23389. Ref.1
	Sequence conflict	401	1	E → V in AAA23389. Ref.1
	Sequence conflict	644	1	F → N in AAA23389. Ref.1
	Sequence conflict	816 – 823	8	PNEWYRYG → LMMVQIR in AAA23389. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25239-1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: EDB090A7FBFFCC93	FASTA	998	117,087
	10 20 30 40 50 60 MNKKDQLQRL IDKYKSDIDY YRSARYNETQ LRTDFLDQLF LILGWDITNA AGKPTNEREV 70 80 90 100 110 120 LVEEGLKARA GENTKKPDYT FRLFSERKFF LEAKKPSVDI STTIEPALQV RRYGFTAKLK 130 140 150 160 170 180 ISVLSNFEYT AIYDCSNQVK ETDSVANSRI KLYHFTELVD KFDEINNLIG RESVYTGHFD 190 200 210 220 230 240 NEWSEIENKI LRFSVDDLFL KQINDWRLLL ANEFLQIKNE LPEEKLNDLV QNYINSIVFL 250 260 270 280 290 300 RVCEDRDLEE YETLYHFAQD KDFQSLVKKL KSSDKKYNSG LFSLEYIDEL LSNANSCIWS 310 320 330 340 350 360 IIEQLYFPQS TYSFSVFSSD ILGNIYEIFL SEKVRIDELG NVKIQPKEEH IDRDVVTTPT 370 380 390 400 410 420 HIVKEIIRNT VVEYCKGKSD IEILNSKFAD IACGSGAFII EAFQFIQDIL IDYYIQNDKS 430 440 450 460 470 480 KLQQISEHTY KLKFEVKREI LCKCIYGIDK DYNATKACTF GLLLKLLEGE TTETIGKDTP 490 500 510 520 530 540 ILPALDTNIL FGNSLIDSGD KVKQEDIFSI NPFDLTNYQF DVIVGNPPYM ATEHMNQLTP 550 560 570 580 590 600 KELDIYKRKY KSAYKQFDKY FLFIERSIQI LKEYGYLGYI LPSRFIKVDA GKKLRKFLSE 610 620 630 640 650 660 NKYLSKLISF GSHQVFKNKT TYTCLLFLNK ENHDNFSFYE VKDFKKWLTR EDKYLLSSTY 670 680 690 700 710 720 QTSSLDSDTW VLEKKINDIL KLMFSKSEQL GNIVGKSNVA NGIQTSANKY YIHKEIKSEN 730 740 750 760 770 780 GFIYFEYDGI EYHIEKELTR PYFETNRSGD DSFYTYKDVE PNSFVVYPYK KVGERIQFIE 790 800 810 820 830 840 YDELKRQYPK LFEFLQVVKV HLNDKKRSIK PDPTGPNEWY RYGRSQALEN CDVDQKLIVG 850 860 870 880 890 900 ILSNGYKYSI DNHRTFVSSG GTAGYSIINI PNNVRYSIYY IQAILTSKYL EWFASIYGDI 910 920 930 940 950 960 FRGRFVARGT KVQTRMPIPT IDFDDPKQKE IHDTISSKQQ YLNKLYSQTQ KSADRDKIIF 970 980 990 ERQFEQEKIQ MDYLIKNLFD LGDLDSEIPT VEDLYKNL

References

[1]	"Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes." Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V. Nucleic Acids Res. 20:6051-6056(1992) [PubMed: 1334261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: RFL57.
[2]	"Crystallization and preliminary crystallographic studies of a bifunctional restriction endonuclease Eco57I." Tamulaitiene G., Grazulis S., Janulaitis A., Janowski R., Bujacz G., Jaskolski M. Biochim. Biophys. Acta 1698:251-254(2004) [PubMed: 15134658] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS), SEQUENCE REVISION.
[3]	"Purification and properties of the Eco57I restriction endonuclease and methylase -- prototypes of a new class (type IV)." Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V. Nucleic Acids Res. 20:6043-6049(1992) [PubMed: 1334260] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M74821 Genomic DNA. Translation: AAA23389.1. X61122 Genomic DNA. Translation: CAA43434.3.
PIR	S26426.
3D structure databases
ModBase	Search...
Protein family/group databases
REBASE	941. Eco57I.
Family and domain databases
InterPro	IPR002296. N12N6_MeTrfase. IPR002052. N6_adenine_Mtase_CS. IPR011639. Restrict_endonuc_Eco57I. IPR007409. Restrict_endonuc_I_R/III_Res_N. [Graphical view]
Pfam	PF07669. Eco57I. 1 hit. PF04313. HSDR_N. 1 hit. [Graphical view]
PRINTS	PR00507. N12N6MTFRASE.
PROSITE	PS00092. N6_MTASE. 1 hit. [Graphical view]
ProDom	P25239. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

T257_ECOLX

Accession

Primary (citable) accession number: P25239

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	September 13, 2004
Last modified:	September 2, 2008
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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