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Protein

Modification methylase HhaI

Gene

hhaIM

Organism
Haemophilus parahaemolyticus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease.

Catalytic activityi

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

Kineticsi

  1. KM=69 nM for DNA1 Publication
  2. KM=15 nM for S-adenosyl-L-methionine (SAM)1 Publication
  1. Vmax=87.0 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei811

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

Protein family/group databases

REBASEi3421. M.HhaI.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase HhaI (EC:2.1.1.37)
Short name:
M.HhaI
Alternative name(s):
Cytosine-specific methyltransferase HhaI
Gene namesi
Name:hhaIM
OrganismiHaemophilus parahaemolyticus
Taxonomic identifieri735 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi237Q → X: Decrease in enzyme activity due to 98%-99% loss of DNA-binding activity. No change in substrate specificity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000878821 – 327Modification methylase HhaIAdd BLAST327

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 11Combined sources4
Beta strandi13 – 17Combined sources5
Turni20 – 22Combined sources3
Helixi23 – 30Combined sources8
Beta strandi34 – 39Combined sources6
Helixi43 – 53Combined sources11
Helixi61 – 63Combined sources3
Helixi66 – 68Combined sources3
Beta strandi73 – 78Combined sources6
Turni82 – 84Combined sources3
Turni86 – 89Combined sources4
Helixi92 – 94Combined sources3
Helixi96 – 98Combined sources3
Helixi100 – 111Combined sources12
Beta strandi114 – 121Combined sources8
Helixi122 – 125Combined sources4
Helixi127 – 130Combined sources4
Helixi131 – 142Combined sources12
Beta strandi148 – 153Combined sources6
Helixi154 – 156Combined sources3
Beta strandi164 – 172Combined sources9
Helixi173 – 175Combined sources3
Helixi192 – 194Combined sources3
Helixi199 – 201Combined sources3
Helixi203 – 205Combined sources3
Beta strandi213 – 216Combined sources4
Beta strandi228 – 232Combined sources5
Beta strandi240 – 243Combined sources4
Beta strandi244 – 246Combined sources3
Turni258 – 262Combined sources5
Beta strandi264 – 267Combined sources4
Beta strandi270 – 272Combined sources3
Helixi276 – 282Combined sources7
Helixi295 – 304Combined sources10
Helixi308 – 323Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
10MHX-ray2.55A1-327[»]
1FJXX-ray2.26A1-327[»]
1HMYX-ray2.50A1-327[»]
1M0EX-ray2.50A1-327[»]
1MHTX-ray2.60A1-327[»]
1SKMX-ray2.20A1-327[»]
1SVUX-ray2.66A/B1-327[»]
2C7OX-ray1.90A1-327[»]
2C7PX-ray1.70A1-327[»]
2C7QX-ray1.85A1-327[»]
2C7RX-ray1.90A1-327[»]
2HMYX-ray2.61B1-327[»]
2HR1X-ray1.96A1-327[»]
2I9KX-ray2.65A1-327[»]
2UYCX-ray2.00A1-327[»]
2UYHX-ray2.63A1-327[»]
2UZ4X-ray2.10A1-327[»]
2Z6AX-ray2.88A1-327[»]
2Z6QX-ray2.79A1-327[»]
2Z6UX-ray2.72A1-327[»]
2ZCJX-ray2.75A1-327[»]
3EEOX-ray1.94A1-327[»]
3MHTX-ray2.70A1-327[»]
4MHTX-ray2.70A1-327[»]
5CIYX-ray1.59A1-327[»]
5MHTX-ray2.70A1-327[»]
6MHTX-ray2.05A1-327[»]
7MHTX-ray2.87A1-327[»]
8MHTX-ray2.76A1-327[»]
9MHTX-ray2.39A1-327[»]
ProteinModelPortaliP05102.
SMRiP05102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05102.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 325SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST314

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.

P05102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEIKDKQLT GLRFIDLFAG LGGFRLALES CGAECVYSNE WDKYAQEVYE
60 70 80 90 100
MNFGEKPEGD ITQVNEKTIP DHDILCAGFP CQAFSISGKQ KGFEDSRGTL
110 120 130 140 150
FFDIARIVRE KKPKVVFMEN VKNFASHDNG NTLEVVKNTM NELDYSFHAK
160 170 180 190 200
VLNALDYGIP QKRERIYMIC FRNDLNIQNF QFPKPFELNT FVKDLLLPDS
210 220 230 240 250
EVEHLVIDRK DLVMTNQEIE QTTPKTVRLG IVGKGGQGER IYSTRGIAIT
260 270 280 290 300
LSAYGGGIFA KTGGYLVNGK TRKLHPRECA RVMGYPDSYK VHPSTSQAYK
310 320
QFGNSVVINV LQYIAYNIGS SLNFKPY
Length:327
Mass (Da):36,996
Last modified:August 13, 1987 - v1
Checksum:iEF8A297E1DF819EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02677 Genomic DNA. Translation: AAA24989.1.
PIRiA26260. XYHIH1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02677 Genomic DNA. Translation: AAA24989.1.
PIRiA26260. XYHIH1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
10MHX-ray2.55A1-327[»]
1FJXX-ray2.26A1-327[»]
1HMYX-ray2.50A1-327[»]
1M0EX-ray2.50A1-327[»]
1MHTX-ray2.60A1-327[»]
1SKMX-ray2.20A1-327[»]
1SVUX-ray2.66A/B1-327[»]
2C7OX-ray1.90A1-327[»]
2C7PX-ray1.70A1-327[»]
2C7QX-ray1.85A1-327[»]
2C7RX-ray1.90A1-327[»]
2HMYX-ray2.61B1-327[»]
2HR1X-ray1.96A1-327[»]
2I9KX-ray2.65A1-327[»]
2UYCX-ray2.00A1-327[»]
2UYHX-ray2.63A1-327[»]
2UZ4X-ray2.10A1-327[»]
2Z6AX-ray2.88A1-327[»]
2Z6QX-ray2.79A1-327[»]
2Z6UX-ray2.72A1-327[»]
2ZCJX-ray2.75A1-327[»]
3EEOX-ray1.94A1-327[»]
3MHTX-ray2.70A1-327[»]
4MHTX-ray2.70A1-327[»]
5CIYX-ray1.59A1-327[»]
5MHTX-ray2.70A1-327[»]
6MHTX-ray2.05A1-327[»]
7MHTX-ray2.87A1-327[»]
8MHTX-ray2.76A1-327[»]
9MHTX-ray2.39A1-327[»]
ProteinModelPortaliP05102.
SMRiP05102.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3421. M.HhaI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP05102.

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 nameiMTH1_HAEPH
AccessioniPrimary (citable) accession number: P05102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Strain ATCC 10014 was originally thought to originate from H.haemolyticus.Curated

Keywords - Technical termi

3D-structure

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.