Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O13998 (OLA1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP By similarity. Negatively regulates the G2/M transition in the cell cycle. Ref.3

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03167

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.

Contains 1 OBG-type G (guanine nucleotide-binding) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Obg-like ATPase 1 HAMAP-Rule MF_03167
PRO_0000356254

Regions

Domain21 – 285265OBG-type G
Nucleotide binding30 – 356ATP By similarity

Sites

Binding site2331ATP; via carbonyl oxygen By similarity

Secondary structure

........................................................................ 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O13998 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: AEBBAF47DA1BC5F8

FASTA39244,333
        10         20         30         40         50         60 
MPPKKQQEVV KVQWGRPGNN LKTGIVGMPN VGKSTFFRAI TKSVLGNPAN YPYATIDPEE 

        70         80         90        100        110        120 
AKVAVPDERF DWLCEAYKPK SRVPAFLTVF DIAGLTKGAS TGVGLGNAFL SHVRAVDAIY 

       130        140        150        160        170        180 
QVVRAFDDAE IIHVEGDVDP IRDLSIIVDE LLIKDAEFVE KHLEGLRKIT SRGANTLEMK 

       190        200        210        220        230        240 
AKKEEQAIIE KVYQYLTETK QPIRKGDWSN REVEIINSLY LLTAKPVIYL VNMSERDFLR 

       250        260        270        280        290        300 
QKNKYLPKIK KWIDENSPGD TLIPMSVAFE ERLTNFTEEE AIEECKKLNT KSMLPKIIVT 

       310        320        330        340        350        360 
GYNALNLINY FTCGEDEVRS WTIRKGTKAP QAAGVIHTDF EKAFVVGEIM HYQDLFDYKT 

       370        380        390 
ENACRAAGKY LTKGKEYVME SGDIAHWKAG KR 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"A systematic screen reveals new elements acting at the G2/M cell cycle control."
Navarro F.J., Nurse P.
Genome Biol. 13:R36.1-R36.10(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Structure of the s. pombe ychf GTP-binding protein."
New York structural genomix research consortium (NYSGXRC)
Submitted (JAN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB11677.1.
PIRT38450.
RefSeqNP_594403.1. NM_001019834.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI3X-ray2.80A1-392[»]
ProteinModelPortalO13998.
SMRO13998. Positions 11-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277939. 7 interactions.
MINTMINT-4669602.
STRING4896.SPAC27E2.03c-1.

Proteomic databases

PaxDbO13998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC27E2.03c.1; SPAC27E2.03c.1:pep; SPAC27E2.03c.
GeneID2541434.
KEGGspo:SPAC27E2.03c.

Organism-specific databases

PomBaseSPAC27E2.03c.

Phylogenomic databases

eggNOGCOG0012.
HOGENOMHOG000087628.
KOK06942.
OMAIHVLRCF.
OrthoDBEOG7XPZG2.
PhylomeDBO13998.

Family and domain databases

Gene3D1.10.150.300. 1 hit.
3.10.20.30. 1 hit.
3.40.50.300. 2 hits.
HAMAPMF_00944. YchF_OLA1_ATPase.
InterProIPR004396. ATPase_YchF/OLA1.
IPR012675. Beta-grasp_dom.
IPR013029. DUF933.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR012676. TGS-like.
IPR023192. TGS-like_dom.
[Graphical view]
PfamPF01926. MMR_HSR1. 1 hit.
PF06071. YchF-GTPase_C. 1 hit.
[Graphical view]
PIRSFPIRSF006641. CHP00092. 1 hit.
PRINTSPR00326. GTP1OBG.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00092. TIGR00092. 1 hit.
PROSITEPS51710. G_OBG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO13998.
NextBio20802536.
PROO13998.

Entry information

Entry nameOLA1_SCHPO
AccessionPrimary (citable) accession number: O13998
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references