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Q9UT49 (CID13_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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 cid13

Short name=PAP
EC=2.7.7.19
Alternative name(s):
Caffeine-induced death protein 13
Polynucleotide adenylyltransferase cid13
Gene names
Name:cid13
ORF Names:SPAC821.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polymerase that creates the 3' poly(A) tail of suc22 mRNA. Ref.2

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with pab1. Ref.2

Subcellular location

Cytoplasm. Nucleus Ref.2 Ref.3.

Sequence similarities

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

Contains 1 PAP-associated domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578Poly(A) RNA polymerase cid13
PRO_0000120313

Regions

Domain275 – 33056PAP-associated
Compositional bias551 – 5566Poly-Ser

Sites

Metal binding1101Magnesium or manganese; catalytic By similarity
Metal binding1121Magnesium or manganese; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UT49 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A572D21E13552351

FASTA57865,771
        10         20         30         40         50         60 
MDNANCVGGC KFETRSFQYR RRIPYSLGAD PLPPVHPLSL KNLVDIDTDL ISSQLYELYD 

        70         80         90        100        110        120 
SIILNDSGLE RRYAFVQKLE QILKKEFPYK NIKTSLFGST QSLLASNASD IDLCIITDPP 

       130        140        150        160        170        180 
QCAPTTCEVS AAFARNGLKK VVCISTAKVP IVKVWDSELQ LSCDCNINKT ISTLNTRLMR 

       190        200        210        220        230        240 
SYVLCDPRVR PLIVMIKYWA KRRCLNDAAE GGTLTSYTIS CMVINFLQKR DPPILPSLQM 

       250        260        270        280        290        300 
LPHLQDSSTM TDGLDVSFFD DPDLVHGFGD KNEESLGILF VEFFRFFGYL FDYEHFVLSI 

       310        320        330        340        350        360 
RHGTFLSKRA KGWQFQLNNF LCVEEPFHTS RNLANTADEI TMKGIQLEFR RVFRLLAYNC 

       370        380        390        400        410        420 
NVDDACSQFT FPSLTDTSFM DDYVNELQLE IVPGFSHGRD SSDTSCTESP PEPSHFAWAF 

       430        440        450        460        470        480 
DPYNATASPY YNQNINSSID YSSIYSNDVP AIPPNVPYTF VDPYTYACYI NNNSYLPPSY 

       490        500        510        520        530        540 
MDFYTWYNSP YPKSSHHFDE RHGGDRHEKN LSNSRRYSRN KFHKKKQSSG PFQYYPDAFS 

       550        560        570 
FTPTDNNSPP SNSSSSEVVS PVSLHSEPVL STVQAFKS 

« 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]"Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide reductase mRNA."
Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III, Russell P.
Cell 109:563-573(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAB1, 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB57438.1.
PIRT41715.
RefSeqNP_593157.1. NM_001018555.2.

3D structure databases

ProteinModelPortalQ9UT49.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279633. 13 interactions.
IntActQ9UT49. 6 interactions.
MINTMINT-4709602.
STRING4896.SPAC821.04c-1.

Proteomic databases

PRIDEQ9UT49.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC821.04c.1; SPAC821.04c.1:pep; SPAC821.04c.
GeneID2543204.
KEGGspo:SPAC821.04c.

Organism-specific databases

PomBaseSPAC821.04c.

Phylogenomic databases

eggNOGCOG5260.
OrthoDBEOG75XGVD.
PhylomeDBQ9UT49.

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

NextBio20804227.

Entry information

Entry nameCID13_SCHPO
AccessionPrimary (citable) accession number: Q9UT49
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 86 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