O74518 (CID12_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle Chromosome partition RNA-mediated gene silencing
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from genetic interaction PubMed 16738311. Source: PomBase RNA polyadenylation Inferred from sequence model. 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 spindle assembly checkpoint Inferred from genetic interaction PubMed 16738311. Source: PomBase sister chromatid biorientation Inferred from mutant phenotype PubMed 16738311. Source: PomBase
Cellular_component	cytosol Inferred from direct assay Ref.3. Source: PomBase nuclear RNA-directed RNA polymerase complex Inferred from direct assay Ref.2. Source: PomBase
Molecular_function	ATP 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 sequence model. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 336	336	Poly(A) RNA polymerase cid12		PRO_0000256156
Regions
	Domain	209 – 263	55	PAP-associated
Sites
	Metal binding	77	1	Magnesium or manganese; catalytic By similarity
	Metal binding	79	1	Magnesium or manganese; catalytic By similarity
Amino acid modifications
	Modified residue	325	1	Phosphoserine Ref.4
	Modified residue	327	1	Phosphothreonine Ref.4
	Modified residue	329	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O74518 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: BF56B701691F8737	FASTA	336	38,558
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA20372.1.
PIR	T41543.
RefSeq	NP_588273.1. NM_001023263.2.
3D structure databases
ProteinModelPortal	O74518.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC663.12-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC663.12.1; SPCC663.12.1:pep; SPCC663.12.
GeneID	2539423.
KEGG	spo:SPCC663.12.
Organism-specific databases
PomBase	SPCC663.12.
Phylogenomic databases
eggNOG	COG5260.
KO	K11700.
OrthoDB	EOG4B8NQ6.
Family and domain databases
InterPro	IPR002058. PAP_assoc. [Graphical view]
Pfam	PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20800587.

Entry information

Entry name

CID12_SCHPO

Accession

Primary (citable) accession number: O74518

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program