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Protein

Modification methylase HaeIII

Gene

haeIIIM

Organism
Haemophilus aegyptius
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the HaeIII endonuclease.

Catalytic activityi

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB-EC
  2. DNA binding Source: InterPro

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.37. 2525.

Protein family/group databases

REBASEi3410. M.HaeIII.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase HaeIII (EC:2.1.1.37)
Short name:
M.HaeIII
Alternative name(s):
Cytosine-specific methyltransferase HaeIII
Gene namesi
Name:haeIIIM
OrganismiHaemophilus aegyptius
Taxonomic identifieri197575 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Modification methylase HaeIIIPRO_0000087878Add
BLAST

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi12 – 198Combined sources
Beta strandi23 – 297Combined sources
Turni32 – 343Combined sources
Helixi35 – 417Combined sources
Beta strandi44 – 496Combined sources
Helixi51 – 533Combined sources
Helixi56 – 583Combined sources
Beta strandi63 – 664Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 784Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 883Combined sources
Helixi89 – 10113Combined sources
Beta strandi104 – 1107Combined sources
Helixi113 – 1164Combined sources
Helixi117 – 1193Combined sources
Helixi121 – 13313Combined sources
Beta strandi135 – 1439Combined sources
Helixi144 – 1463Combined sources
Beta strandi154 – 1629Combined sources
Helixi163 – 1653Combined sources
Helixi181 – 1833Combined sources
Helixi186 – 1883Combined sources
Beta strandi189 – 1913Combined sources
Helixi197 – 1993Combined sources
Helixi203 – 2053Combined sources
Beta strandi206 – 2083Combined sources
Helixi222 – 2243Combined sources
Helixi242 – 2443Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi261 – 2633Combined sources
Turni266 – 2683Combined sources
Helixi269 – 2713Combined sources
Helixi277 – 2848Combined sources
Helixi297 – 3059Combined sources
Helixi310 – 32617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCTX-ray2.80A/B1-324[»]
3UBTX-ray2.50A/B/Y1-330[»]
ProteinModelPortaliP20589.
SMRiP20589. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20589.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 327327SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLISLFSGA GGLDLGFQKA GFRIICANEY DKSIWKTYES NHSAKLIKGD
60 70 80 90 100
ISKISSDEFP KCDGIIGGPP CQSWSEGGSL RGIDDPRGKL FYEYIRILKQ
110 120 130 140 150
KKPIFFLAEN VKGMMAQRHN KAVQEFIQEF DNAGYDVHII LLNANDYGVA
160 170 180 190 200
QDRKRVFYIG FRKELNINYL PPIPHLIKPT FKDVIWDLKD NPIPALDKNK
210 220 230 240 250
TNGNKCIYPN HEYFIGSYST IFMSRNRVRQ WNEPAFTVQA SGRQCQLHPQ
260 270 280 290 300
APVMLKVSKN LNKFVEGKEH LYRRLTVREC ARVQGFPDDF IFHYESLNDG
310 320 330
YKMIGNAVPV NLAYEIAKTI KSALEICKGN
Length:330
Mass (Da):37,686
Last modified:February 1, 1991 - v1
Checksum:i928C6D5390DBED25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24625 Genomic DNA. Translation: AAA24970.1.
AF051375 Genomic DNA. Translation: AAC05696.1.
PIRiJS0102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24625 Genomic DNA. Translation: AAA24970.1.
AF051375 Genomic DNA. Translation: AAC05696.1.
PIRiJS0102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCTX-ray2.80A/B1-324[»]
3UBTX-ray2.50A/B/Y1-330[»]
ProteinModelPortaliP20589.
SMRiP20589. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3410. M.HaeIII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.1.1.37. 2525.

Miscellaneous databases

EvolutionaryTraceiP20589.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and analysis of the HaeIII and HaeII methyltransferase genes."
    Slatko B.E., Croft R., Moran L.S., Wilson G.G.
    Gene 74:45-50(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11116 / CCUG 25716 / NCTC 8502.
  2. Zhang B.-H., Wilson G.G.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11116 / CCUG 25716 / NCTC 8502.
  3. "Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase."
    Chen L., McMillan A.M., Chang W., Ezak-Nipkay K., Lane W.S., Verdine G.L.
    Biochemistry 30:11018-11025(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 62-81.
  4. "The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing."
    Reinisch K.M., Chen L., Verdine G.L., Lipscomb W.N.
    Cell 82:143-153(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiMTH3_HAEAE
AccessioniPrimary (citable) accession number: P20589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 1, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.