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O30569 (MTS1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modification methylase SmeI

Short name=M.SmeI
EC=2.1.1.72
Alternative name(s):
Adenine-specific methyltransferase SmeIP
M.CcrMI ortholog
Modification methylase SmeIP
Short name=M.SmeIP
Gene names
Name:smeIM
Synonyms:ccrM
Ordered Locus Names:R00926
ORF Names:SMc00021
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GANTC and causes specific methylation on A-2 on both strands. Ccrm-mediated methylation has important cellular functions. Appears to contribute to the accurate cell-cycle control of DNA replication and cellular morphology.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Sequence similarities

Belongs to the N(4)/N(6)-methyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Modification methylase SmeI
PRO_0000087988

Experimental info

Sequence conflict135 – 1417NPMPNFK → QPDAELQ in AAB71350. Ref.1
Sequence conflict1571P → A in AAB71350. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O30569 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 790DE7FE3D22900A

FASTA37641,442
        10         20         30         40         50         60 
MSSVVSLAEI SRAARPLNWL DSIIKGDCVA ALNALPDHSV DVVFADPPYN LQLGGTLHRP 

        70         80         90        100        110        120 
DQSLVDAVDD DWDQFASFEA YDAFTRAWLL ACRRVLKPTG TLWVIGSYHN IFRVGAILQD 

       130        140        150        160        170        180 
LHFWVLNDII WRKTNPMPNF KGRRFQNAHE TLIWATPNAK AKGYTFNYEA MKAANDDVQM 

       190        200        210        220        230        240 
RSDWLFPICS GSERLKGDDG KKVHPTQKPE ALLARILMAS TKPGDVVLDP FFGSGTTGAV 

       250        260        270        280        290        300 
AKRLGRHFVG IEREQDYIDA AAERIAAVEP LGKATLSVMT GKKAEPRVAF NTLVESGLIK 

       310        320        330        340        350        360 
PGTVLTDAKR RYSAIVRADG TLASGGEAGS IHRLGAKVQG LDACNGWTFW HFEEGSVLKP 

       370 
IDELRSVIRN DLAKLN 

« Hide

References

« Hide 'large scale' references
[1]"The CcrM DNA methyltransferase is widespread in the alpha subdivision of proteobacteria, and its essential functions are conserved in Rhizobium meliloti and Caulobacter crescentus."
Wright R., Stephens C., Shapiro L.
J. Bacteriol. 179:5869-5877(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1021.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF011894 Genomic DNA. Translation: AAB71350.1.
AL591688 Genomic DNA. Translation: CAC45498.1.
RefSeqNP_385032.1. NC_003047.1.

3D structure databases

ProteinModelPortalO30569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc00021.

Protein family/group databases

REBASE3264. M.SmeI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC45498; CAC45498; SMc00021.
GeneID1232567.
KEGGsme:SMc00021.
PATRIC23631121. VBISinMel96828_2324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0863.
HOGENOMHOG000125329.
KOK13581.
OMAFWHFEDG.
OrthoDBEOG6FV84T.
ProtClustDBCLSK864763.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-946-MONOMER.

Family and domain databases

InterProIPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR001091. RM_Methylase.
[Graphical view]
PfamPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSPR00508. S21N4MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTS1_RHIME
AccessionPrimary (citable) accession number: O30569
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries