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F7UQG7 (F7UQG7_SYNYG) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
GTPase Der RuleBase RU004481 HAMAP-Rule MF_00195
Alternative name(s):
GTP-binding protein EngA HAMAP-Rule MF_00195
Gene names
Name:slr1974 EMBL BAK50379.1
Synonyms:der HAMAP-Rule MF_00195 EMBL BAK50379.1
Ordered Locus Names:SYNGTS_1631 EMBL BAK50379.1
OrganismSynechocystis sp. (strain PCC 6803 / GT-S) [Complete proteome] [HAMAP]
Taxonomic identifier1111707 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

GTPase that plays an essential role in the late steps of ribosome biogenesis By similarity. RuleBase RU004481 HAMAP-Rule MF_00195 SAAS SAAS016484

Subunit structure

Associates with the 50S ribosomal subunit By similarity. HAMAP-Rule MF_00195 SAAS SAAS016484

Sequence similarities

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family. RuleBase RU004481 HAMAP-Rule MF_00195

Contains 1 KH-like domain. HAMAP-Rule MF_00195

Contains 2 G (guanine nucleotide-binding) domains. HAMAP-Rule MF_00195

Contains EngA-type G (guanine nucleotide-binding) domains. SAAS SAAS016484

Contains KH-like domain. SAAS SAAS016484

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain6 – 121116G 1 By similarity HAMAP-Rule MF_00195
Domain178 – 296119G 2 By similarity HAMAP-Rule MF_00195
Domain352 – 43988KH-like By similarity HAMAP-Rule MF_00195
Nucleotide binding10 – 178GTP 1 By similarity HAMAP-Rule MF_00195
Nucleotide binding57 – 615GTP 1 By similarity HAMAP-Rule MF_00195
Nucleotide binding120 – 1234GTP 1 By similarity HAMAP-Rule MF_00195
Nucleotide binding183 – 1908GTP 2 By similarity HAMAP-Rule MF_00195
Nucleotide binding230 – 2345GTP 2 By similarity HAMAP-Rule MF_00195
Nucleotide binding295 – 2984GTP 2 By similarity HAMAP-Rule MF_00195

Sequences

Sequence LengthMass (Da)Tools
F7UQG7 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 7FF771EAF7D6CC76

FASTA45250,826
        10         20         30         40         50         60 
MSLPIVAIIG RPNVGKSTFV NRLAGNQQAI VHDQPGITRD RTYRPAFWRD RDFQVVDTGG 

        70         80         90        100        110        120 
LVFNDDSEFL PEIREQANLA LAEAKAAIFV VDGQQGPTAS DEEIAQWLRQ QSVPVILAVN 

       130        140        150        160        170        180 
KCESPDQGAI QAAEFWHLGL GEPYPMSAIH GSGTGDLLDA LLEYLPAPQE EPEEDEIKVA 

       190        200        210        220        230        240 
IVGRPNVGKS SLLNALTGEQ RAIVSPISGT TRDAIDMVVE RNGQKYRLID TAGIRRKKNV 

       250        260        270        280        290        300 
DYGAEFFGIN RAFKAIRRAD VVLFVLDVLD GVTEQDLKLA GRIIEDGRAV VLVINKWDAV 

       310        320        330        340        350        360 
EKDSYTIYEH REQLMARLYF MDWAEMIFVS AQTGLRVQKI LDCVDIAAQE HRRRVTTAVI 

       370        380        390        400        410        420 
NEVLEEAVSW HSPPTTRQGK QGKIYYGTQV STQPPAIALF VNDPNRFNDN YRRYIEKQFR 

       430        440        450 
KQLGFFGSPI RLFWRGKKVR EMEGSRNRAT KV 

« Hide

References

[1]"Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / GT-S.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012205 Genomic DNA. Translation: BAK50379.1.
RefSeqNP_441526.1. NC_000911.1.
YP_005651584.1. NC_017277.1.
YP_007451408.1. NC_020286.1.

3D structure databases

ProteinModelPortalF7UQG7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK50379; BAK50379; SYNGTS_1631.
GeneID954938.
KEGGsyn:slr1974.
syy:SYNGTS_1631.
syz:MYO_116460.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK03977.

Enzyme and pathway databases

BioCycSSP1148:GJOT-1651-MONOMER.

Family and domain databases

Gene3D3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPMF_00195. GTPase_Der.
InterProIPR003593. AAA+_ATPase.
IPR016484. GTP-bd_EngA.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PANTHERPTHR11649:SF5. PTHR11649:SF5. 1 hit.
PfamPF01926. MMR_HSR1. 2 hits.
[Graphical view]
PIRSFPIRSF006485. GTP-binding_EngA. 1 hit.
PRINTSPR00326. GTP1OBG.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR03594. GTPase_EngA. 1 hit.
TIGR00231. small_GTP. 2 hits.
ProtoNetSearch...

Entry information

Entry nameF7UQG7_SYNYG
AccessionPrimary (citable) accession number: F7UQG7
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)