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Protein

Terminal uridylyltransferase cid1

Gene

cid1

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

Functioni

Cytoplasmic uridylyltransferase that mediates the terminal uridylation of mRNAs with short poly(A) tails such as such as act1, hcn1 and urg1 mRNAs, hence facilitating global mRNA decay (PubMed:17353264, PubMed:17449726, PubMed:19430462, PubMed:22751018, PubMed:22885303). Uridylates the 3' ends of actin mRNAs upon S-phase arrest (PubMed:17353264). Has also a weak poly(A) polymerase (PAP) activity (PubMed:22751018, PubMed:22885303). Residue His-336 is responsible for the specificity for UTP (PubMed:22751018, PubMed:22885303). Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis (PubMed:10757807).5 Publications

Caution

Has been first identified as a cytoplasmic poly(A) polymerase (PAP) implicated in cell cycle checkpoint controls (PubMed:12218190). Further studies showed that cid1 had robust poly(U) polymerase activity in vitro and that is was rather an RNA uridylyltransferase (PubMed:17353264, PubMed:17449726).3 Publications

Catalytic activityi

UTP + RNA(n) = diphosphate + RNA(n+1).7 Publications
ATP + RNA(n) = diphosphate + RNA(n+1).3 Publications

Cofactori

Mg2+2 Publications, Mn2+1 Publication

Kineticsi

Mutation of His-336 to Asn decreases the Km for ATP to 65 µM and increases the Km for UTP to 45 µM.1 Publication
  1. KM=12 µM for UTP1 Publication
  2. KM=312 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei90Substrate4 Publications1
    Metal bindingi101Magnesium; catalytic1 Publication1
    Binding sitei101Substrate1 Publication1
    Metal bindingi103Magnesium; catalytic1 Publication1
    Binding sitei103Substrate1 Publication1
    Binding sitei171Substrate2 Publications1
    Binding sitei193Substrate4 Publications1
    Binding sitei197Substrate4 Publications1
    Binding sitei211Substrate1 Publication1
    Binding sitei336Substrate4 Publications1
    Binding sitei340Substrate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    • polyuridylation-dependent decapping of nuclear-transcribed mRNA Source: PomBase
    • RNA 3' uridylation Source: PomBase

    Keywordsi

    Molecular functionNucleotidyltransferase, Transferase
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Terminal uridylyltransferase cid1Curated (EC:2.7.7.195 Publications, EC:2.7.7.526 Publications)
    Short name:
    TUTase cid1Curated
    Alternative name(s):
    Caffeine-induced death protein 11 Publication
    Poly(A) polymerase cid11 Publication
    Short name:
    PAP1 Publication
    Poly(U) polymerase cid11 Publication
    Short name:
    PUP1 Publication
    Gene namesi
    Name:cid11 Publication
    ORF Names:SPAC19D5.03
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    Proteomesi
    • UP000002485 Componenti: Chromosome I

    Organism-specific databases

    EuPathDBiFungiDB:SPAC19D5.03
    PomBaseiSPAC19D5.03 cid1

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Stabilizes urg1 transcripts (PubMed:19430462).1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi88F → D: Impairs catalytic activity. 1 Publication1
    Mutagenesisi101D → A: Abolishes catalytic activity but does not affect RNA binding; when associated with A-103. 2 Publications1
    Mutagenesisi103D → A: Abolishes catalytic activity but does not affect RNA binding; when associated with A-101. 2 Publications1
    Mutagenesisi133K → A: Impairs binding to RNA; when associated with A-137; A-321 and A-323. Impairs also binding to RNA; when associated with A-137; A-277 and A-282. 1 Publication1
    Mutagenesisi137R → A: Impairs binding to RNA; when associated with A-133; A-321 and A-323. Impairs also binding to RNA; when associated with A-133; A-277 and A-282. 1 Publication1
    Mutagenesisi144K → A: Reduces association with a 15-mer A stretch but does not affect association with a 15-mer U stretch. 1 Publication1
    Mutagenesisi160D → A: Abolishes catalytic activity. 2 Publications1
    Mutagenesisi164N → P: Predominantly performs monouridylation. 1 Publication1
    Mutagenesisi165N → A or P: Abolishes catalytic activity. 2 Publications1
    Mutagenesisi277R → A: Impairs binding to RNA; when associated with A-282; A-133 and A-137. Impairs also binding to RNA; when associated with A-282; A-321 and A-323. 1 Publication1
    Mutagenesisi282K → A: Impairs binding to RNA; when associated with A-277; A-133 and A-137. Impairs also binding to RNA; when associated with A-277; A-321 and A-323. 1 Publication1
    Mutagenesisi321K → A: Impairs binding to RNA; when associated with A-323; A-277 and A-282. Impairs also binding to RNA; when associated with A-323; A-133 and A-137. 1 Publication1
    Mutagenesisi323R → A: Impairs binding to RNA; when associated with A-321; A-277 and A-282. Impairs also binding to RNA; when associated with A-321; A-133 and A-137. 1 Publication1
    Mutagenesisi330D → A: Leads to diminished TUTase activity. 1 Publication1
    Mutagenesisi332F → A: Reduces capacity for binding RNAs. 1 Publication1
    Mutagenesisi333E → A: Leads to diminished TUTase activity. 1 Publication1
    Mutagenesisi336H → A or N: Abolishes the UTP specificity and converts Cid1 from a TUTase into a poly(A) polymerase (PAP). 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001203121 – 405Terminal uridylyltransferase cid1Add BLAST405

    Proteomic databases

    MaxQBiO13833
    PaxDbiO13833
    PRIDEiO13833

    PTM databases

    iPTMnetiO13833

    Interactioni

    Protein-protein interaction databases

    BioGridi278883, 28 interactors
    STRINGi4896.SPAC19D5.03.1

    Structurei

    Secondary structure

    1405
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliO13833
    SMRiO13833
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini267 – 336PAP-associatedSequence analysisAdd BLAST70

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni168 – 172Substrate binding3 Publications5
    Regioni211 – 212Substrate binding4 Publications2

    Sequence similaritiesi

    Belongs to the DNA polymerase type-B-like family.Curated

    Phylogenomic databases

    InParanoidiO13833
    KOiK13291
    OMAiWASHHEI
    OrthoDBiEOG092C34LM
    PhylomeDBiO13833

    Family and domain databases

    InterProiView protein in InterPro
    IPR002058 PAP_assoc
    IPR002934 Polymerase_NTP_transf_dom
    PfamiView protein in Pfam
    PF01909 NTP_transf_2, 1 hit
    PF03828 PAP_assoc, 1 hit

    Sequencei

    Sequence statusi: Complete.

    O13833-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNISSAQFIP GVHTVEEIEA EIHKNLHISK SCSYQKVPNS HKEFTKFCYE
    60 70 80 90 100
    VYNEIKISDK EFKEKRAALD TLRLCLKRIS PDAELVAFGS LESGLALKNS
    110 120 130 140 150
    DMDLCVLMDS RVQSDTIALQ FYEELIAEGF EGKFLQRARI PIIKLTSDTK
    160 170 180 190 200
    NGFGASFQCD IGFNNRLAIH NTLLLSSYTK LDARLKPMVL LVKHWAKRKQ
    210 220 230 240 250
    INSPYFGTLS SYGYVLMVLY YLIHVIKPPV FPNLLLSPLK QEKIVDGFDV
    260 270 280 290 300
    GFDDKLEDIP PSQNYSSLGS LLHGFFRFYA YKFEPREKVV TFRRPDGYLT
    310 320 330 340 350
    KQEKGWTSAT EHTGSADQII KDRYILAIED PFEISHNVGR TVSSSGLYRI
    360 370 380 390 400
    RGEFMAASRL LNSRSYPIPY DSLFEEAPIP PRRQKKTDEQ SNKKLLNETD

    GDNSE
    Length:405
    Mass (Da):46,257
    Last modified:November 1, 1999 - v2
    Checksum:i0AA24B4411B61027
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CU329670 Genomic DNA Translation: CAB50789.1
    AF105076 mRNA Translation: AAD16889.1
    PIRiT37963
    RefSeqiNP_594901.1, NM_001020330.2

    Genome annotation databases

    EnsemblFungiiSPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03
    GeneIDi2542420
    KEGGispo:SPAC19D5.03

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CU329670 Genomic DNA Translation: CAB50789.1
    AF105076 mRNA Translation: AAD16889.1
    PIRiT37963
    RefSeqiNP_594901.1, NM_001020330.2

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4E7XX-ray3.20A/B/C/D1-405[»]
    4E80X-ray3.02A/B/C/D1-405[»]
    4E8FX-ray2.60A/B1-405[»]
    4EP7X-ray2.28A/B40-377[»]
    4FH3X-ray2.00A33-377[»]
    4FH5X-ray2.30A33-377[»]
    4FHPX-ray2.50A33-377[»]
    4FHVX-ray2.10A33-377[»]
    4FHWX-ray2.50A33-377[»]
    4FHXX-ray2.70A33-377[»]
    4FHYX-ray2.70A33-377[»]
    4NKTX-ray1.90A/B40-377[»]
    4NKUX-ray1.94A/B40-377[»]
    4UD4X-ray1.74A/B40-405[»]
    4UD5X-ray2.52A/B40-405[»]
    ProteinModelPortaliO13833
    SMRiO13833
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi278883, 28 interactors
    STRINGi4896.SPAC19D5.03.1

    PTM databases

    iPTMnetiO13833

    Proteomic databases

    MaxQBiO13833
    PaxDbiO13833
    PRIDEiO13833

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiSPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03
    GeneIDi2542420
    KEGGispo:SPAC19D5.03

    Organism-specific databases

    EuPathDBiFungiDB:SPAC19D5.03
    PomBaseiSPAC19D5.03 cid1

    Phylogenomic databases

    InParanoidiO13833
    KOiK13291
    OMAiWASHHEI
    OrthoDBiEOG092C34LM
    PhylomeDBiO13833

    Miscellaneous databases

    PROiPR:O13833

    Family and domain databases

    InterProiView protein in InterPro
    IPR002058 PAP_assoc
    IPR002934 Polymerase_NTP_transf_dom
    PfamiView protein in Pfam
    PF01909 NTP_transf_2, 1 hit
    PF03828 PAP_assoc, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCID1_SCHPO
    AccessioniPrimary (citable) accession number: O13833
    Secondary accession number(s): O94608
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: November 1, 1999
    Last modified: November 7, 2018
    This is version 121 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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