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O14045 (TPT1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 namesRecommended name:
Putative tRNA 2'-phosphotransferase

EC=2.7.1.160
Gene names
ORF Names:SPAC2C4.12c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate By similarity.

Catalytic activity

2'-phospho-[ligated tRNA] + NAD+ = mature tRNA + ADP ribose 1'',2''-phosphate + nicotinamide + H2O.

Sequence similarities

Belongs to the KptA/TPT1 family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandNAD
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA splicing, via endonucleolytic cleavage and ligation

Inferred from sequence or structural similarity. Source: PomBase

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: PomBase

   Molecular_functiontRNA 2'-phosphotransferase activity

Inferred from sequence or structural similarity. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Putative tRNA 2'-phosphotransferase
PRO_0000316237

Sequences

Sequence LengthMass (Da)Tools
O14045 [UniParc].

Last modified April 18, 2012. Version 2.
Checksum: 32F645818B1B7997

FASTA36541,028
        10         20         30         40         50         60 
MYKNMNSHEL IEESNNSGTP ATKSSSKPTK KIRPRNDLVH YSKALSKVLR HTAKANGLQI 

        70         80         90        100        110        120 
REDGYIEVDS ILKLPQFRGM GMELLLSIVK GNDKKRFTME EVEGVLYIRA NQGHSIKAVQ 

       130        140        150        160        170        180 
VPMARIDNAS SIPKVVHGTK KELWPVISKQ GLSRMKRNHI HCATGLYGDP GVISGIRKSC 

       190        200        210        220        230        240 
TLYIYIDSAK AMQDGVEFYR SENGVILTEG VNGLLSSKYF SRVETSDGEV LLDAKASPKN 

       250        260        270        280        290        300 
NRSDESDQSD PESIDPFCDN LQALSMHELE LLEEKHSNFG YSEGIIKGKM QVAQSGFDDG 

       310        320        330        340        350        360 
FKHGSRLGFQ MGKTIGTLKA KLYIFEENEQ MEILKQELDR LQESAEFHIF VANHKEEILK 


CIREK 

« 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]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB16372.2.
PIRT38523.
RefSeqNP_594515.2. NM_001019944.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC2C4.12c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC2C4.12c.1; SPAC2C4.12c.1:pep; SPAC2C4.12c.
GeneID2541572.
KEGGspo:SPAC2C4.12c.

Organism-specific databases

PomBaseSPAC2C4.12c.

Phylogenomic databases

eggNOGCOG1859.
KOK10669.
OrthoDBEOG418FXT.

Family and domain databases

InterProIPR019191. Essential_protein_Yae1_N.
IPR002745. Ptrans_KptA/Tpt1.
[Graphical view]
PfamPF01885. PTS_2-RNA. 1 hit.
PF09811. Yae1_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802666.

Entry information

Entry nameTPT1_SCHPO
AccessionPrimary (citable) accession number: O14045
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 18, 2012
Last modified: May 1, 2013
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families