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Reviewed, UniProtKB/Swiss-Prot Q9P795 (AIR1_SCHPO)

Last modified November 24, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein air1
Gene names
Name: air1
ORF Names: SPBP35G2.08c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of the TRAMP (TRF4) and TRAMP5 complexes which have a poly(A) RNA polymerase activity and are involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. Ref.2

Subunit structure

Component of the TRAMP complex (also called TRF4 complex) composed of at least mtr4, pap2/trf4 and air1. Component of the TRAMP5 complex composed of at least air1, mtr4 and trf5. Interacts with cid14. Ref.2

Subcellular location

Nucleusnucleolus By similarity.

Sequence similarities

Belongs to the AIR1 family.

Contains 3 CCHC-type zinc fingers.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentTRAMP complex Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Protein air1
PRO_0000356248

Regions

Zinc finger87 – 10418CCHC-type 1
Zinc finger125 – 14218CCHC-type 2
Zinc finger187 – 20418CCHC-type 3

Amino acid modifications

Modified residue101Phosphoserine Ref.3
Modified residue141Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9P795-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 90BDF9596AE48D2A

FASTA31335,299
        10         20         30         40         50         60 
MTVSNQKAES DDGSDIDDAA LLQKINSLPI DQSITNSVSL EKHDFQGSDD HDSSTDLSDS 

        70         80         90        100        110        120 
TLEDVEGSEW ADVSRGRYFG SDPSESIVCH NCKGNGHISK DCPHVLCTTC GAIDDHISVR 

       130        140        150        160        170        180 
CPWTKKCMNC GLLGHIAARC SEPRKRGPRV CRTCHTDTHT SSTCPLIWRY YVEKEHPVRI 

       190        200        210        220        230        240 
DVSEVRKFCY NCASDEHFGD DCTLPSRSNY PESTAFCEAN CPSGNDASNK EFFETRRKEF 

       250        260        270        280        290        300 
QLERREQNRN QKSSKQRPFH KPGNSLASRL GSKPKSFKRK HSPPSEENGN LSFHSSDGRK 

       310 
FTKTSKKNRK RKW 

« 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"RNAi-dependent and -independent RNA turnover mechanisms contribute to heterochromatic gene silencing."
Buehler M., Haas W., Gygi S.P., Moazed D.
Cell 129:707-721(2007) [PubMed: 17512405] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CID14.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-14, MASS SPECTROMETRY.

Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAB87370.1.
RefSeqNP_595383.1.

3D structure databases

HSSPHSSP built from PDB template 2CQF based on UniProtKB Q9H9Z2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9P795.

Genome annotation databases

GeneID2541349.
GenomeReviewsGene locus air1 in contig CU329671_GR.
KEGGspo:SPBP35G2.08c.
NMPDRfig|4896.1.peg.1249.

Organism-specific databases

GeneDB_SpombeSPBP35G2.08c.

Phylogenomic databases

OMARICARCY
OrthoDBEOG93FJCZ

Gene expression databases

ArrayExpressQ9P795.

Family and domain databases

InterProIPR016713. PolA_Pol_cplx_Air1/2_su.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00098. zf-CCHC. 2 hits.
[Graphical view]
PIRSFPIRSF018162. PolyA_pol_Air1/2. 1 hit.
SMARTSM00343. ZnF_C2HC. 5 hits.
[Graphical view]
PROSITEPS50158. ZF_CCHC. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAIR1_SCHPO
AccessionPrimary (citable) accession number: Q9P795
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 1, 2000
Last modified: November 24, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents