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Q9UT49

- CID13_SCHPO

UniProt

Q9UT49 - CID13_SCHPO

Protein

Poly(A) RNA polymerase cid13

Gene

cid13

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Polymerase that creates the 3' poly(A) tail of suc22 mRNA.1 Publication

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi110 – 1101Magnesium or manganese; catalyticBy similarity
    Metal bindingi112 – 1121Magnesium or manganese; catalyticBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. mRNA 3'-UTR binding Source: PomBase
    4. polynucleotide adenylyltransferase activity Source: PomBase

    GO - Biological processi

    1. biological regulation Source: PomBase
    2. mRNA polyadenylation Source: PomBase

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(A) RNA polymerase cid13 (EC:2.7.7.19)
    Short name:
    PAP
    Alternative name(s):
    Caffeine-induced death protein 13
    Polynucleotide adenylyltransferase cid13
    Gene namesi
    Name:cid13
    ORF Names:SPAC821.04c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC821.04c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase
    3. nucleus Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 578578Poly(A) RNA polymerase cid13PRO_0000120313Add
    BLAST

    Proteomic databases

    MaxQBiQ9UT49.
    PRIDEiQ9UT49.

    Interactioni

    Subunit structurei

    Interacts with pab1.1 Publication

    Protein-protein interaction databases

    BioGridi279633. 13 interactions.
    IntActiQ9UT49. 6 interactions.
    MINTiMINT-4709602.
    STRINGi4896.SPAC821.04c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UT49.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini275 – 33056PAP-associatedAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi551 – 5566Poly-Ser

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5260.
    OrthoDBiEOG75XGVD.
    PhylomeDBiQ9UT49.

    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.

    Q9UT49-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNANCVGGC KFETRSFQYR RRIPYSLGAD PLPPVHPLSL KNLVDIDTDL    50
    ISSQLYELYD SIILNDSGLE RRYAFVQKLE QILKKEFPYK NIKTSLFGST 100
    QSLLASNASD IDLCIITDPP QCAPTTCEVS AAFARNGLKK VVCISTAKVP 150
    IVKVWDSELQ LSCDCNINKT ISTLNTRLMR SYVLCDPRVR PLIVMIKYWA 200
    KRRCLNDAAE GGTLTSYTIS CMVINFLQKR DPPILPSLQM LPHLQDSSTM 250
    TDGLDVSFFD DPDLVHGFGD KNEESLGILF VEFFRFFGYL FDYEHFVLSI 300
    RHGTFLSKRA KGWQFQLNNF LCVEEPFHTS RNLANTADEI TMKGIQLEFR 350
    RVFRLLAYNC NVDDACSQFT FPSLTDTSFM DDYVNELQLE IVPGFSHGRD 400
    SSDTSCTESP PEPSHFAWAF DPYNATASPY YNQNINSSID YSSIYSNDVP 450
    AIPPNVPYTF VDPYTYACYI NNNSYLPPSY MDFYTWYNSP YPKSSHHFDE 500
    RHGGDRHEKN LSNSRRYSRN KFHKKKQSSG PFQYYPDAFS FTPTDNNSPP 550
    SNSSSSEVVS PVSLHSEPVL STVQAFKS 578
    Length:578
    Mass (Da):65,771
    Last modified:May 1, 2000 - v1
    Checksum:iA572D21E13552351
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB57438.1.
    PIRiT41715.
    RefSeqiNP_593157.1. NM_001018555.2.

    Genome annotation databases

    EnsemblFungiiSPAC821.04c.1; SPAC821.04c.1:pep; SPAC821.04c.
    GeneIDi2543204.
    KEGGispo:SPAC821.04c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB57438.1 .
    PIRi T41715.
    RefSeqi NP_593157.1. NM_001018555.2.

    3D structure databases

    ProteinModelPortali Q9UT49.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279633. 13 interactions.
    IntActi Q9UT49. 6 interactions.
    MINTi MINT-4709602.
    STRINGi 4896.SPAC821.04c-1.

    Proteomic databases

    MaxQBi Q9UT49.
    PRIDEi Q9UT49.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC821.04c.1 ; SPAC821.04c.1:pep ; SPAC821.04c .
    GeneIDi 2543204.
    KEGGi spo:SPAC821.04c.

    Organism-specific databases

    PomBasei SPAC821.04c.

    Phylogenomic databases

    eggNOGi COG5260.
    OrthoDBi EOG75XGVD.
    PhylomeDBi Q9UT49.

    Miscellaneous databases

    NextBioi 20804227.

    Family and domain databases

    InterProi IPR002934. Nucleotidyltransferase.
    IPR002058. PAP_assoc.
    [Graphical view ]
    Pfami PF01909. NTP_transf_2. 1 hit.
    PF03828. PAP_assoc. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide reductase mRNA."
      Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III, Russell P.
      Cell 109:563-573(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAB1, 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].

    Entry informationi

    Entry nameiCID13_SCHPO
    AccessioniPrimary (citable) accession number: Q9UT49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 89 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