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Q9UTN3 (CID14_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. 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 cid14

Short name=PAP
EC=2.7.7.19
Alternative name(s):
Caffeine-induced death protein 14
Polynucleotide adenylyltransferase cid14
Gene names
Name:cid14
ORF Names:SPAC12G12.13c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude ot their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis. Ref.2

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Heterooligomer. Interacts with air1. Ref.2 Ref.4

Subcellular location

Nucleusnucleolus 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
Cell division
Mitosis
mRNA processing
   Cellular componentNucleus
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbiological regulation

Non-traceable author statement. Source: PomBase

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process

Inferred from sequence orthology. Source: PomBase

nucleolus organization

Inferred from mutant phenotype Ref.2. Source: PomBase

rRNA 3'-end processing

Inferred from genetic interaction Ref.2. Source: PomBase

rRNA catabolic process

Inferred from genetic interaction Ref.2. Source: PomBase

snoRNA catabolic process

Inferred from sequence orthology. Source: PomBase

tRNA catabolic process

Inferred from sequence orthology. Source: PomBase

   Cellular_componentTRAMP complex

Inferred from direct assay Ref.4PubMed 20403971. Source: PomBase

nucleolus

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 mutant phenotype Ref.2. Source: PomBase

ribosomal large subunit binding

Inferred from direct assay PubMed 20403971. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 684684Poly(A) RNA polymerase cid14
PRO_0000089746

Regions

Domain434 – 49259PAP-associated

Sites

Metal binding2981Magnesium or manganese; catalytic By similarity
Metal binding3001Magnesium or manganese; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UTN3 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: C2CF653A51C8D39B

FASTA68478,298
        10         20         30         40         50         60 
MGKKSVSFNR NNYKKRKNER TEPLPRRIFK NDKPSKFKSK RKEKDKNSDA YDEMLLNNNF 

        70         80         90        100        110        120 
TLLDQEEPMV EIGSKKSRND NDSEGIRDKG GVEISNKNDP YIQFGKADPL EPLEKPDLPE 

       130        140        150        160        170        180 
EAIKRGEPTI LLGIPKREGR KTNPVHDKAV ENNSDFIKFD WNSDEDEDSV SNDKSKNNES 

       190        200        210        220        230        240 
LKKSSKNEIP GFMRQRGRFF HEANEKSDSN RKRKRQAYEL DSQSCPWHRQ YKVEREVSRI 

       250        260        270        280        290        300 
FHQDILHFID YITPTPEEHA VRKTLVSRIN QAVLQKWPDV SLYVFGSFET KLYLPTSDLD 

       310        320        330        340        350        360 
LVIISPEHHY RGTKKDMFVL AHHLKKLKLA SEVQVITTAN VPIIKFVDPL TKVHVDISFN 

       370        380        390        400        410        420 
QPGGLKTCLV VNGFMKKYPA LRPLVIIIKH FLNMRALNEV FLGGLSSYAI VCLVVSFLQL 

       430        440        450        460        470        480 
HPRLSTGSMR EEDNFGVLLL EFLELYGKQF YYDAVGIAVH NGGFYFSKKK MGWLKPNQPY 

       490        500        510        520        530        540 
LLSIQDPVDF QNDVSKSSRG LLRVKATFAN GFDLLTSKLY ALASRIEREG VNRVKDFPSI 

       550        560        570        580        590        600 
LSTILSVDEG VRQHREHMLK CYKNNPVPLE PLVEVDALAS IDVDKLPLQD VGLQYVEDES 

       610        620        630        640        650        660 
DSDETDAAKD DLFKVNESIE TNGHENFQKQ ALTSTGEQSS SNSRANPSKL FNISSDDSED 

       670        680 
EVPIIEDTTA SDEESRAKKI RKRF 

« 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]"Requirement of fission yeast Cid14 in polyadenylation of rRNAs."
Win T.Z., Draper S., Read R.L., Pearce J., Norbury C.J., Wang S.-W.
Mol. Cell. Biol. 26:1710-1721(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[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]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIR1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAI79317.1.
PIRS62544.
RefSeqNP_001018181.1. NM_001018285.2.

3D structure databases

ProteinModelPortalQ9UTN3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280460. 146 interactions.
MINTMINT-4710930.
STRING4896.SPAC12G12.13c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC12G12.13c.1; SPAC12G12.13c.1:pep; SPAC12G12.13c.
GeneID3361384.
KEGGspo:SPAC12G12.13c.

Organism-specific databases

PomBaseSPAC12G12.13c.

Phylogenomic databases

eggNOGCOG5260.
KOK03514.
OMALISHEEE.
OrthoDBEOG7CNZS6.
PhylomeDBQ9UTN3.

Family and domain databases

InterProIPR002934. Nucleotidyltransferase.
IPR002058. PAP_assoc.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20811434.

Entry information

Entry nameCID14_SCHPO
AccessionPrimary (citable) accession number: Q9UTN3
Secondary accession number(s): Q09876, Q565C4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 91 of the entry and version 2 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