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Protein

Terminal uridylyltransferase cid1

Gene

cid1

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

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

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

Manual assertion based on experiment ini

  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

    • ATP binding Source: UniProtKB-KW
    • magnesium ion binding Source: PomBase
    • polynucleotide adenylyltransferase activity Source: UniProtKB-EC
    • RNA binding Source: PomBase
    • RNA uridylyltransferase activity Source: PomBase
    • UTP binding Source: PomBase

    GO - Biological processi

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

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-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

    GO - Cellular componenti

    • cytoplasm Source: PomBase
    • cytosol Source: PomBase
    Complete GO annotation...

    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.
    PRIDEiO13833.

    Interactioni

    Protein-protein interaction databases

    BioGridi278883. 28 interactors.
    MINTiMINT-4668341.

    Structurei

    Secondary structure

    1405
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi42 – 55Combined sources14
    Helixi59 – 79Combined sources21
    Beta strandi84 – 89Combined sources6
    Helixi90 – 93Combined sources4
    Beta strandi97 – 99Combined sources3
    Beta strandi102 – 107Combined sources6
    Helixi115 – 127Combined sources13
    Beta strandi131 – 137Combined sources7
    Beta strandi140 – 147Combined sources8
    Beta strandi159 – 164Combined sources6
    Helixi166 – 181Combined sources16
    Helixi185 – 198Combined sources14
    Helixi204 – 206Combined sources3
    Helixi211 – 224Combined sources14
    Beta strandi226 – 228Combined sources3
    Turni234 – 236Combined sources3
    Helixi256 – 258Combined sources3
    Helixi268 – 281Combined sources14
    Turni285 – 287Combined sources3
    Beta strandi288 – 290Combined sources3
    Beta strandi292 – 294Combined sources3
    Helixi301 – 304Combined sources4
    Beta strandi310 – 313Combined sources4
    Beta strandi319 – 322Combined sources4
    Beta strandi325 – 329Combined sources5
    Beta strandi331 – 333Combined sources3
    Helixi338 – 341Combined sources4
    Helixi344 – 361Combined sources18
    Beta strandi364 – 367Combined sources4
    Helixi370 – 374Combined sources5

    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...

    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
    Contains 1 PAP-associated domain.Sequence analysis

    Phylogenomic databases

    InParanoidiO13833.
    KOiK13291.
    OMAiMENTIPH.
    OrthoDBiEOG092C34LM.
    PhylomeDBiO13833.

    Family and domain databases

    InterProiIPR002058. PAP_assoc.
    IPR002934. Polymerase_NTP_transf_dom.
    [Graphical view]
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF03828. PAP_assoc. 1 hit.
    [Graphical view]

    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.

    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.
    MINTiMINT-4668341.

    Proteomic databases

    MaxQBiO13833.
    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.
    OMAiMENTIPH.
    OrthoDBiEOG092C34LM.
    PhylomeDBiO13833.

    Miscellaneous databases

    PROiO13833.

    Family and domain databases

    InterProiIPR002058. PAP_assoc.
    IPR002934. Polymerase_NTP_transf_dom.
    [Graphical view]
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF03828. PAP_assoc. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCID1_SCHPO
    AccessioniPrimary (citable) accession number: O13833
    Secondary accession number(s): O94608
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: November 1, 1999
    Last modified: November 2, 2016
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    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 one 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.