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O13833 (CID1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 protein cid1

EC=2.7.7.-
Alternative name(s):
Caffeine-induced death protein 1
Gene names
Name:cid1
ORF Names:SPAC19D5.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis. Ref.1

Cofactor

Magnesium or manganese By similarity.

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 – 405405Poly(A) RNA polymerase protein cid1
PRO_0000120312

Regions

Domain267 – 33670PAP-associated

Sites

Metal binding1011Magnesium or manganese; catalytic By similarity
Metal binding1031Magnesium or manganese; catalytic By similarity

Secondary structure

....................................................... 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O13833 [UniParc].

Last modified November 1, 1999. Version 2.
Checksum: 0AA24B4411B61027

FASTA40546,257
        10         20         30         40         50         60 
MNISSAQFIP GVHTVEEIEA EIHKNLHISK SCSYQKVPNS HKEFTKFCYE VYNEIKISDK 

        70         80         90        100        110        120 
EFKEKRAALD TLRLCLKRIS PDAELVAFGS LESGLALKNS DMDLCVLMDS RVQSDTIALQ 

       130        140        150        160        170        180 
FYEELIAEGF EGKFLQRARI PIIKLTSDTK NGFGASFQCD IGFNNRLAIH NTLLLSSYTK 

       190        200        210        220        230        240 
LDARLKPMVL LVKHWAKRKQ INSPYFGTLS SYGYVLMVLY YLIHVIKPPV FPNLLLSPLK 

       250        260        270        280        290        300 
QEKIVDGFDV GFDDKLEDIP PSQNYSSLGS LLHGFFRFYA YKFEPREKVV TFRRPDGYLT 

       310        320        330        340        350        360 
KQEKGWTSAT EHTGSADQII KDRYILAIED PFEISHNVGR TVSSSGLYRI RGEFMAASRL 

       370        380        390        400 
LNSRSYPIPY DSLFEEAPIP PRRQKKTDEQ SNKKLLNETD GDNSE 

« Hide

References

« Hide 'large scale' references
[1]"Cid1, a fission yeast protein required for S-M checkpoint control when DNA polymerase delta or epsilon is inactivated."
Wang S.-W., Toda T., MacCallum R., Harris A.L., Norbury C.
Mol. Cell. Biol. 20:3234-3244(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: 972 / ATCC 24843.
[2]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB50789.1.
AF105076 mRNA. Translation: AAD16889.1.
PIRT37963.
RefSeqNP_594901.1. NM_001020330.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4E7XX-ray3.20A/B/C/D1-405[»]
4E80X-ray3.02A/B/C/D1-405[»]
4E8FX-ray2.60A/B1-405[»]
4EP7X-ray2.28A/B40-377[»]
4FH3X-ray2.00A33-377[»]
4FH5X-ray2.30A33-377[»]
4FHPX-ray2.50A33-377[»]
4FHVX-ray2.10A33-377[»]
4FHWX-ray2.50A33-377[»]
4FHXX-ray2.70A33-377[»]
4FHYX-ray2.70A33-377[»]
4NKTX-ray1.90A/B40-377[»]
4NKUX-ray1.94A/B40-377[»]
ProteinModelPortalO13833.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278883. 27 interactions.
MINTMINT-4668341.
STRING4896.SPAC19D5.03-1.

Proteomic databases

MaxQBO13833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03.
GeneID2542420.
KEGGspo:SPAC19D5.03.

Organism-specific databases

PomBaseSPAC19D5.03.

Phylogenomic databases

eggNOGCOG5260.
KOK13291.
OMADMARIRG.
OrthoDBEOG7R8396.
PhylomeDBO13833.

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

NextBio20803478.
PROO13833.

Entry information

Entry nameCID1_SCHPO
AccessionPrimary (citable) accession number: O13833
Secondary accession number(s): O94608
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 1, 1999
Last modified: June 11, 2014
This is version 96 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references