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O74518 (CID12_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. 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:
Poly(A) RNA polymerase cid12

Short name=PAP
EC=2.7.7.19
Alternative name(s):
Caffeine-induced death protein 12
Polynucleotide adenylyltransferase cid12
Gene names
Name:cid12
ORF Names:SPCC663.12
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA. Ref.2

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1).

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Cid12, hrr1 and rdp1 interact forming the RNA-directed RNA polymerase complex (RDRC). The RDRC complex interacts with the RITS complex via interaction between ago1 and hrr1. Clr4 has a role in mediating this interaction.

Subcellular location

Cytoplasm. Nucleus Ref.2 Ref.3.

Sequence similarities

Belongs to the DNA polymerase type-B-like family.

Contains 1 PAP-associated domain.

Ontologies

Keywords
   Biological processCell cycle
Chromosome partition
RNA-mediated gene silencing
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polyadenylation

Inferred from sequence model. Source: PomBase

attachment of spindle microtubules to kinetochore involved in mitotic sister chromatid segregation

Inferred from mutant phenotype PubMed 16738311. Source: PomBase

chromatin silencing at centromere

Inferred from mutant phenotype Ref.2. Source: PomBase

chromatin silencing by small RNA

Inferred from mutant phenotype Ref.2. Source: PomBase

mitotic DNA damage checkpoint

Inferred from genetic interaction PubMed 16738311. Source: PomBase

mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.2PubMed 16738311. Source: PomBase

mitotic spindle assembly checkpoint

Inferred from genetic interaction PubMed 16738311. Source: PomBase

sister chromatid biorientation

Inferred from mutant phenotype PubMed 16738311. Source: PomBase

   Cellular_componentRNA-directed RNA polymerase complex

Inferred from direct assay Ref.2. Source: PomBase

cytosol

Inferred from direct assay Ref.3. Source: PomBase

nuclear RNA-directed RNA polymerase complex

Inferred from direct assay Ref.2. Source: PomBase

nucleus

Inferred from direct assay Ref.2Ref.3. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polynucleotide adenylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Poly(A) RNA polymerase cid12
PRO_0000256156

Regions

Domain209 – 26355PAP-associated

Sites

Metal binding771Magnesium or manganese; catalytic By similarity
Metal binding791Magnesium or manganese; catalytic By similarity

Amino acid modifications

Modified residue3251Phosphoserine Ref.4
Modified residue3271Phosphothreonine Ref.4
Modified residue3291Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O74518 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BF56B701691F8737

FASTA33638,558
        10         20         30         40         50         60 
MGKVLLELHS VPWNEEGLSD NARLYSFLEF VSPKIEELKY RKLLLEKLQT HIREVVLDAE 

        70         80         90        100        110        120 
LQVYGSMYIG TTLSISDVDV SLKSPRVGEL EKRRVTMVLR KYLDADADFH SSARVPRINL 

       130        140        150        160        170        180 
VDVSGIGVDL TFGNDKACRT AELQKAYNEE HPIFGRLLML LKHWLFERDL ENVHHGGIAS 

       190        200        210        220        230        240 
CALSYMLIGW LEMRFHKKGI DSEVQPIRAL LQKFFYFWGV EWTYELFVLR PLTGQIVPKL 

       250        260        270        280        290        300 
QKGWLNEVQP NLLSIEDPID RNNDIGKQSF QISMIKAAFV ASANELLSDK TWFSTFAITE 

       310        320        330 
DEMFLCKQFE NVINTKRSLV EGYDSDTESD ELQAGG 

« 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]"Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs."
Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P., Moazed D.
Cell 119:789-802(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[3]"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].
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; THR-327 AND SER-329, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA20372.1.
PIRT41543.
RefSeqNP_588273.1. NM_001023263.2.

3D structure databases

ProteinModelPortalO74518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275988. 121 interactions.
DIPDIP-60035N.
MINTMINT-4679737.
STRING4896.SPCC663.12-1.

Proteomic databases

MaxQBO74518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC663.12.1; SPCC663.12.1:pep; SPCC663.12.
GeneID2539423.
KEGGspo:SPCC663.12.

Organism-specific databases

PomBaseSPCC663.12.

Phylogenomic databases

eggNOGCOG5260.
KOK11700.
OrthoDBEOG7CNZS6.
PhylomeDBO74518.

Family and domain databases

InterProIPR002058. PAP_assoc.
[Graphical view]
PfamPF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800587.

Entry information

Entry nameCID12_SCHPO
AccessionPrimary (citable) accession number: O74518
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 83 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