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Protein

Type-1 restriction enzyme MjaXIP specificity protein

Gene

MJ0130

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Restriction system

Keywords - Ligandi

DNA-binding

Protein family/group databases

REBASEi3901. S.MjaORF132P.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-1 restriction enzyme MjaXIP specificity protein
Short name:
S.MjaXIP
Alternative name(s):
Type I restriction enzyme MjaXIP specificity protein
Short name:
S protein
Gene namesi
Ordered Locus Names:MJ0130
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Type-1 restriction enzyme MjaXIP specificity proteinPRO_0000106708Add
BLAST

Interactioni

Subunit structurei

The type I restriction/modification system is composed of three polypeptides R, M and S.By similarity

Protein-protein interaction databases

STRINGi243232.MJ_0130m.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154Combined sources
Beta strandi17 – 193Combined sources
Helixi25 – 284Combined sources
Beta strandi29 – 346Combined sources
Helixi43 – 453Combined sources
Turni46 – 483Combined sources
Beta strandi51 – 544Combined sources
Helixi56 – 605Combined sources
Beta strandi62 – 665Combined sources
Beta strandi70 – 734Combined sources
Helixi75 – 795Combined sources
Beta strandi91 – 944Combined sources
Beta strandi96 – 983Combined sources
Beta strandi102 – 1076Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi113 – 1208Combined sources
Turni122 – 1243Combined sources
Helixi127 – 13610Combined sources
Helixi138 – 1425Combined sources
Beta strandi145 – 1495Combined sources
Helixi155 – 1595Combined sources
Helixi168 – 20942Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi229 – 2324Combined sources
Helixi233 – 2364Combined sources
Beta strandi237 – 2415Combined sources
Helixi250 – 2523Combined sources
Turni253 – 2553Combined sources
Beta strandi258 – 2614Combined sources
Helixi263 – 2675Combined sources
Turni268 – 2714Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi279 – 2824Combined sources
Helixi284 – 2896Combined sources
Beta strandi300 – 3034Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi311 – 3166Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi324 – 3307Combined sources
Helixi337 – 34610Combined sources
Helixi348 – 3558Combined sources
Beta strandi357 – 3604Combined sources
Helixi365 – 3706Combined sources
Beta strandi372 – 3754Combined sources
Helixi378 – 41639Combined sources
Beta strandi418 – 4203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YF2X-ray2.40A/B1-425[»]
ProteinModelPortaliQ57594.
SMRiQ57594. Positions 1-425.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57594.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati169 – 208401; CCRAdd
BLAST
Repeati369 – 418502; DCRAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 168160DNA recognition domain 1Add
BLAST
Regioni209 – 368160DNA recognition domain 2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili169 – 20840Add
BLAST
Coiled coili369 – 41850Add
BLAST

Domaini

Contains two DNA recognition domains, each specifying recognition of one of the two defined components of the target sequence. These two domains show high sequence and structural similarities to each other and each forms a globular structure.
The two globular DNA recognition domains are structurally separated by an antiparallel double helix which is composed of two highly similar 40 residues long coiled-coil regions. These conserved regions may act as a molecular ruler for the separation between the two recognized DNA sequences.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiarCOG02626. Archaea.
COG0732. LUCA.
InParanoidiQ57594.
OMAiGMIPEDW.
PhylomeDBiQ57594.

Family and domain databases

InterProiIPR000055. Restrct_endonuc_typeI_HsdS.
[Graphical view]
PfamiPF01420. Methylase_S. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q57594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFYKEENFKK TEIGEIPEDW EIVELKDVCK KIKAGGTPKT SVEEYYKNGT
60 70 80 90 100
IPFVKIEDIT NSNKYLTNTK IKITEEGLNN SNAWIVPKNS VLFAMYGSIG
110 120 130 140 150
ETAINKIEVA TNQAILGIIP KDNILESEFL YYILAKNKNY YSKLGMQTTQ
160 170 180 190 200
KNLNAQIVKS FKIPLPPLEE QKQIAKILTK IDEGIEIIEK SINKLERIKK
210 220 230 240 250
GLMHKLLTKG IGHSRFKKSE IGEIPEDWEV FEIKDIFEVK TGTTPSTKKS
260 270 280 290 300
EYWENGEINW ITPLDLSRLN EKIYIGSSER KVTKIALEKC NLNLIPKGSI
310 320 330 340 350
IISTRAPVGY VAVLTVESTF NQGCKGLFQK NNDSVNTEFY AYYLKFKKNL
360 370 380 390 400
LENLSGGSTF KELSKSMLEN FKIPLPPLEE QKQIAKILSS VDKSIELKKQ
410 420
KKEKLQRMKK KIMELLLTGK VRVKT
Length:425
Mass (Da):48,568
Last modified:October 3, 2006 - v3
Checksum:iE196A947574FE91D
GO

Sequence cautioni

The sequence AAB98112 differs from that shown. Reason: Frameshift at position 331. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98112.1. Frameshift.

Genome annotation databases

EnsemblBacteriaiAAB98112; AAB98112; MJ_0130.
KEGGimja:MJ_0130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98112.1. Frameshift.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YF2X-ray2.40A/B1-425[»]
ProteinModelPortaliQ57594.
SMRiQ57594. Positions 1-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0130m.

Protein family/group databases

REBASEi3901. S.MjaORF132P.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98112; AAB98112; MJ_0130.
KEGGimja:MJ_0130.

Phylogenomic databases

eggNOGiarCOG02626. Archaea.
COG0732. LUCA.
InParanoidiQ57594.
OMAiGMIPEDW.
PhylomeDBiQ57594.

Miscellaneous databases

EvolutionaryTraceiQ57594.

Family and domain databases

InterProiIPR000055. Restrct_endonuc_typeI_HsdS.
[Graphical view]
PfamiPF01420. Methylase_S. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiT1S1_METJA
AccessioniPrimary (citable) accession number: Q57594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2006
Last modified: June 8, 2016
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.