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Protein

Poly(A) RNA polymerase cid14

Gene

cid14

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

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.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 bindingi298 – 2981Magnesium or manganese; catalyticBy similarity
Metal bindingi300 – 3001Magnesium or manganese; catalyticBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • polynucleotide adenylyltransferase activity Source: PomBase
  • ribosomal large subunit binding Source: PomBase
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process Source: PomBase
  • rRNA 3'-end processing Source: PomBase
  • rRNA catabolic process Source: PomBase
  • snoRNA catabolic process Source: PomBase
  • tRNA catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.7.19. 5613.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A) RNA polymerase cid14 (EC:2.7.7.19)
Short name:
PAP
Alternative name(s):
Caffeine-induced death protein 14
Polynucleotide adenylyltransferase cid14
Gene namesi
Name:cid14
ORF Names:SPAC12G12.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC12G12.13c.
PomBaseiSPAC12G12.13c. cid14.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: PomBase
  • nucleus Source: PomBase
  • TRAMP complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 684684Poly(A) RNA polymerase cid14PRO_0000089746Add
BLAST

Proteomic databases

MaxQBiQ9UTN3.

Interactioni

Subunit structurei

Heterooligomer. Interacts with air1.2 Publications

Protein-protein interaction databases

BioGridi280460. 147 interactions.
MINTiMINT-4710930.
STRINGi4896.SPAC12G12.13c.1.

Structurei

3D structure databases

ProteinModelPortaliQ9UTN3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini434 – 49259PAP-associatedAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5260.
InParanoidiQ9UTN3.
KOiK03514.
OMAiFFHEANE.
OrthoDBiEOG7CNZS6.
PhylomeDBiQ9UTN3.

Family and domain databases

InterProiIPR002934. Nucleotidyltransferase.
IPR002058. PAP_assoc.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UTN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKSVSFNR NNYKKRKNER TEPLPRRIFK NDKPSKFKSK RKEKDKNSDA
60 70 80 90 100
YDEMLLNNNF TLLDQEEPMV EIGSKKSRND NDSEGIRDKG GVEISNKNDP
110 120 130 140 150
YIQFGKADPL EPLEKPDLPE EAIKRGEPTI LLGIPKREGR KTNPVHDKAV
160 170 180 190 200
ENNSDFIKFD WNSDEDEDSV SNDKSKNNES LKKSSKNEIP GFMRQRGRFF
210 220 230 240 250
HEANEKSDSN RKRKRQAYEL DSQSCPWHRQ YKVEREVSRI FHQDILHFID
260 270 280 290 300
YITPTPEEHA VRKTLVSRIN QAVLQKWPDV SLYVFGSFET KLYLPTSDLD
310 320 330 340 350
LVIISPEHHY RGTKKDMFVL AHHLKKLKLA SEVQVITTAN VPIIKFVDPL
360 370 380 390 400
TKVHVDISFN QPGGLKTCLV VNGFMKKYPA LRPLVIIIKH FLNMRALNEV
410 420 430 440 450
FLGGLSSYAI VCLVVSFLQL HPRLSTGSMR EEDNFGVLLL EFLELYGKQF
460 470 480 490 500
YYDAVGIAVH NGGFYFSKKK MGWLKPNQPY LLSIQDPVDF QNDVSKSSRG
510 520 530 540 550
LLRVKATFAN GFDLLTSKLY ALASRIEREG VNRVKDFPSI LSTILSVDEG
560 570 580 590 600
VRQHREHMLK CYKNNPVPLE PLVEVDALAS IDVDKLPLQD VGLQYVEDES
610 620 630 640 650
DSDETDAAKD DLFKVNESIE TNGHENFQKQ ALTSTGEQSS SNSRANPSKL
660 670 680
FNISSDDSED EVPIIEDTTA SDEESRAKKI RKRF
Length:684
Mass (Da):78,298
Last modified:November 8, 2005 - v2
Checksum:iC2CF653A51C8D39B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAI79317.1.
PIRiS62544.
RefSeqiNP_001018181.1. NM_001018285.2.

Genome annotation databases

EnsemblFungiiSPAC12G12.13c.1; SPAC12G12.13c.1:pep; SPAC12G12.13c.
GeneIDi3361384.
KEGGispo:SPAC12G12.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAI79317.1.
PIRiS62544.
RefSeqiNP_001018181.1. NM_001018285.2.

3D structure databases

ProteinModelPortaliQ9UTN3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280460. 147 interactions.
MINTiMINT-4710930.
STRINGi4896.SPAC12G12.13c.1.

Proteomic databases

MaxQBiQ9UTN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC12G12.13c.1; SPAC12G12.13c.1:pep; SPAC12G12.13c.
GeneIDi3361384.
KEGGispo:SPAC12G12.13c.

Organism-specific databases

EuPathDBiFungiDB:SPAC12G12.13c.
PomBaseiSPAC12G12.13c. cid14.

Phylogenomic databases

eggNOGiCOG5260.
InParanoidiQ9UTN3.
KOiK03514.
OMAiFFHEANE.
OrthoDBiEOG7CNZS6.
PhylomeDBiQ9UTN3.

Enzyme and pathway databases

BRENDAi2.7.7.19. 5613.

Miscellaneous databases

NextBioi20811434.
PROiQ9UTN3.

Family and domain databases

InterProiIPR002934. Nucleotidyltransferase.
IPR002058. PAP_assoc.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF03828. 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. "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.

Entry informationi

Entry nameiCID14_SCHPO
AccessioniPrimary (citable) accession number: Q9UTN3
Secondary accession number(s): Q09876, Q565C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 8, 2005
Last modified: June 24, 2015
This is version 101 of the entry and version 2 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.