Q9UTN3 (CID14_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	684 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus 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 Cell division Mitosis mRNA processing
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	biological regulation Non-traceable author statement. Source: PomBase cell division Inferred from electronic annotation. Source: UniProtKB-KW 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_component	TRAMP complex Inferred from direct assay Ref.4. Source: PomBase nucleolus 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 mutant phenotype Ref.2. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 684	684	Poly(A) RNA polymerase cid14		PRO_0000089746
Regions
	Domain	434 – 492	59	PAP-associated
Sites
	Metal binding	298	1	Magnesium or manganese; catalytic By similarity
	Metal binding	300	1	Magnesium or manganese; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UTN3 [UniParc]. Last modified November 8, 2005. Version 2. Checksum: C2CF653A51C8D39B	FASTA	684	78,298
	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

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]	"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.
PIR	S62544.
RefSeq	NP_001018181.1. NM_001018285.2.
3D structure databases
ProteinModelPortal	Q9UTN3.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC12G12.13c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC12G12.13c.1; SPAC12G12.13c.1:pep; SPAC12G12.13c.
GeneID	3361384.
KEGG	spo:SPAC12G12.13c.
Organism-specific databases
PomBase	SPAC12G12.13c.
Phylogenomic databases
eggNOG	COG5260.
KO	K03514.
OMA	LISHEEE.
OrthoDB	EOG43BQXK.
Family and domain databases
InterPro	IPR002934. Nucleotidyltransferase. IPR002058. PAP_assoc. [Graphical view]
Pfam	PF01909. NTP_transf_2. 1 hit. PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20811434.

Entry information

Entry name

CID14_SCHPO

Accession

Primary (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:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program