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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)DescriptionActionsGraphical viewLength
Active sitei71PROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000878781 – 330Modification methylase HaeIIIAdd BLAST330

Proteomic databases

PRIDEiP20589.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi12 – 19Combined sources8
Beta strandi23 – 29Combined sources7
Turni32 – 34Combined sources3
Helixi35 – 41Combined sources7
Beta strandi44 – 49Combined sources6
Helixi51 – 53Combined sources3
Helixi56 – 58Combined sources3
Beta strandi63 – 66Combined sources4
Helixi71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Beta strandi83 – 85Combined sources3
Helixi86 – 88Combined sources3
Helixi89 – 101Combined sources13
Beta strandi104 – 110Combined sources7
Helixi113 – 116Combined sources4
Helixi117 – 119Combined sources3
Helixi121 – 133Combined sources13
Beta strandi135 – 143Combined sources9
Helixi144 – 146Combined sources3
Beta strandi154 – 162Combined sources9
Helixi163 – 165Combined sources3
Helixi181 – 183Combined sources3
Helixi186 – 188Combined sources3
Beta strandi189 – 191Combined sources3
Helixi197 – 199Combined sources3
Helixi203 – 205Combined sources3
Beta strandi206 – 208Combined sources3
Helixi222 – 224Combined sources3
Helixi242 – 244Combined sources3
Beta strandi255 – 258Combined sources4
Beta strandi261 – 263Combined sources3
Turni266 – 268Combined sources3
Helixi269 – 271Combined sources3
Helixi277 – 284Combined sources8
Helixi297 – 305Combined sources9
Helixi310 – 326Combined sources17

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20589.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 327SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST327

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.
IPR031303. C5_meth_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF00145. DNA_methylase. 1 hit.
[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.
RefSeqiWP_013527695.1. NZ_LZPH01000003.1.

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.
RefSeqiWP_013527695.1. NZ_LZPH01000003.1.

3D structure databases

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

Protein family/group databases

REBASEi3410. M.HaeIII.

Proteomic databases

PRIDEiP20589.

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.
IPR031303. C5_meth_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF00145. DNA_methylase. 1 hit.
[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...

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: November 2, 2016
This is version 96 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

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 one 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.