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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)DescriptionActionsGraphical viewLength
ChainiPRO_00001067081 – 425Type-1 restriction enzyme MjaXIP specificity proteinAdd BLAST425

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

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 15Combined sources4
Beta strandi17 – 19Combined sources3
Helixi25 – 28Combined sources4
Beta strandi29 – 34Combined sources6
Helixi43 – 45Combined sources3
Turni46 – 48Combined sources3
Beta strandi51 – 54Combined sources4
Helixi56 – 60Combined sources5
Beta strandi62 – 66Combined sources5
Beta strandi70 – 73Combined sources4
Helixi75 – 79Combined sources5
Beta strandi91 – 94Combined sources4
Beta strandi96 – 98Combined sources3
Beta strandi102 – 107Combined sources6
Beta strandi109 – 111Combined sources3
Beta strandi113 – 120Combined sources8
Turni122 – 124Combined sources3
Helixi127 – 136Combined sources10
Helixi138 – 142Combined sources5
Beta strandi145 – 149Combined sources5
Helixi155 – 159Combined sources5
Helixi168 – 209Combined sources42
Beta strandi222 – 225Combined sources4
Beta strandi229 – 232Combined sources4
Helixi233 – 236Combined sources4
Beta strandi237 – 241Combined sources5
Helixi250 – 252Combined sources3
Turni253 – 255Combined sources3
Beta strandi258 – 261Combined sources4
Helixi263 – 267Combined sources5
Turni268 – 271Combined sources4
Beta strandi273 – 275Combined sources3
Beta strandi279 – 282Combined sources4
Helixi284 – 289Combined sources6
Beta strandi300 – 303Combined sources4
Beta strandi305 – 307Combined sources3
Beta strandi311 – 316Combined sources6
Beta strandi318 – 320Combined sources3
Beta strandi324 – 330Combined sources7
Helixi337 – 346Combined sources10
Helixi348 – 355Combined sources8
Beta strandi357 – 360Combined sources4
Helixi365 – 370Combined sources6
Beta strandi372 – 375Combined sources4
Helixi378 – 416Combined sources39
Beta strandi418 – 420Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ57594.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati169 – 2081; CCRAdd BLAST40
Repeati369 – 4182; DCRAdd BLAST50

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 168DNA recognition domain 1Add BLAST160
Regioni209 – 368DNA recognition domain 2Add BLAST160

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili169 – 208Add BLAST40
Coiled coili369 – 418Add BLAST50

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YF2X-ray2.40A/B1-425[»]
ProteinModelPortaliQ57594.
SMRiQ57594.
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: November 30, 2016
This is version 91 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.