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Protein

Poly(A) RNA polymerase cid12

Gene

cid12

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi77 – 771Magnesium or manganese; catalyticBy similarity
Metal bindingi79 – 791Magnesium or manganese; catalyticBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polynucleotide adenylyltransferase activity Source: UniProtKB-EC
  4. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. chromatin silencing at centromere Source: PomBase
  2. chromatin silencing at centromere outer repeat region Source: PomBase
  3. chromatin silencing by small RNA Source: PomBase
  4. mitotic sister chromatid segregation Source: PomBase
  5. RNA polyadenylation Source: PomBase
  6. sister chromatid biorientation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell cycle, Chromosome partition, RNA-mediated gene silencing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A) RNA polymerase cid12 (EC:2.7.7.19)
Short name:
PAP
Alternative name(s):
Caffeine-induced death protein 12
Polynucleotide adenylyltransferase cid12
Gene namesi
Name:cid12
ORF Names:SPCC663.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC663.12.
PomBaseiSPCC663.12.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nuclear RNA-directed RNA polymerase complex Source: PomBase
  3. nucleus Source: PomBase
  4. RNA-directed RNA polymerase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Poly(A) RNA polymerase cid12PRO_0000256156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei325 – 3251Phosphoserine1 Publication
Modified residuei327 – 3271Phosphothreonine1 Publication
Modified residuei329 – 3291Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74518.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi275988. 122 interactions.
DIPiDIP-60035N.
MINTiMINT-4679737.
STRINGi4896.SPCC663.12-1.

Structurei

3D structure databases

ProteinModelPortaliO74518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini209 – 26355PAP-associatedAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-B-like family.Curated
Contains 1 PAP-associated domain.Curated

Phylogenomic databases

eggNOGiCOG5260.
InParanoidiO74518.
KOiK03514.
OrthoDBiEOG7CNZS6.
PhylomeDBiO74518.

Family and domain databases

InterProiIPR002058. PAP_assoc.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKVLLELHS VPWNEEGLSD NARLYSFLEF VSPKIEELKY RKLLLEKLQT
60 70 80 90 100
HIREVVLDAE LQVYGSMYIG TTLSISDVDV SLKSPRVGEL EKRRVTMVLR
110 120 130 140 150
KYLDADADFH SSARVPRINL VDVSGIGVDL TFGNDKACRT AELQKAYNEE
160 170 180 190 200
HPIFGRLLML LKHWLFERDL ENVHHGGIAS CALSYMLIGW LEMRFHKKGI
210 220 230 240 250
DSEVQPIRAL LQKFFYFWGV EWTYELFVLR PLTGQIVPKL QKGWLNEVQP
260 270 280 290 300
NLLSIEDPID RNNDIGKQSF QISMIKAAFV ASANELLSDK TWFSTFAITE
310 320 330
DEMFLCKQFE NVINTKRSLV EGYDSDTESD ELQAGG
Length:336
Mass (Da):38,558
Last modified:November 1, 1998 - v1
Checksum:iBF56B701691F8737
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20372.1.
PIRiT41543.
RefSeqiNP_588273.1. NM_001023263.2.

Genome annotation databases

EnsemblFungiiSPCC663.12.1; SPCC663.12.1:pep; SPCC663.12.
GeneIDi2539423.
KEGGispo:SPCC663.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20372.1.
PIRiT41543.
RefSeqiNP_588273.1. NM_001023263.2.

3D structure databases

ProteinModelPortaliO74518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275988. 122 interactions.
DIPiDIP-60035N.
MINTiMINT-4679737.
STRINGi4896.SPCC663.12-1.

Proteomic databases

MaxQBiO74518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC663.12.1; SPCC663.12.1:pep; SPCC663.12.
GeneIDi2539423.
KEGGispo:SPCC663.12.

Organism-specific databases

EuPathDBiFungiDB:SPCC663.12.
PomBaseiSPCC663.12.

Phylogenomic databases

eggNOGiCOG5260.
InParanoidiO74518.
KOiK03514.
OrthoDBiEOG7CNZS6.
PhylomeDBiO74518.

Miscellaneous databases

NextBioi20800587.
PROiO74518.

Family and domain databases

InterProiIPR002058. PAP_assoc.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; THR-327 AND SER-329, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCID12_SCHPO
AccessioniPrimary (citable) accession number: O74518
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1998
Last modified: April 29, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.