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O22000

- DCTD_BPMD2

UniProt

O22000 - DCTD_BPMD2

Protein

Deoxycytidylate deaminase

Gene

36.1

Organism
Mycobacterium phage D29 (Mycobacteriophage D29)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
  1. Functioni

    Catalytic activityi

    dCMP + H2O = dUMP + NH3.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi81 – 811Zinc; catalyticBy similarity
    Active sitei83 – 831Proton donorBy similarity
    Metal bindingi107 – 1071Zinc; catalyticBy similarity
    Metal bindingi110 – 1101Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. dCMP deaminase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. nucleotide biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxycytidylate deaminase (EC:3.5.4.12)
    Alternative name(s):
    dCMP deaminase
    Gene namesi
    Name:36.1
    Synonyms:G1
    OrganismiMycobacterium phage D29 (Mycobacteriophage D29)
    Taxonomic identifieri28369 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeL5likevirus
    Virus hostiMycobacterium [TaxID: 1763]
    ProteomesiUP000002131: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 128128Deoxycytidylate deaminasePRO_0000171698Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO22000.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR016193. Cytidine_deaminase-like.
    IPR016473. dCMP_deaminase.
    IPR015517. dCMP_deaminase-rel.
    [Graphical view]
    PANTHERiPTHR11086. PTHR11086. 1 hit.
    PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
    SUPFAMiSSF53927. SSF53927. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O22000-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRPDWDEYF LGIATAAAQR SDCERSKVGA VVVKDRRVRG TGYNGAPAGA    50
    AGCSTCPRRL SGAVPGVSDY SSGATRCVAV HAEANALLYC DREDLIGATL 100
    YVTREPCYAC SNLIAASGIE RVVYPKES 128
    Length:128
    Mass (Da):13,539
    Last modified:December 15, 1998 - v2
    Checksum:iF78F1BA3DB5184D4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022214 Genomic DNA. Translation: AAC18478.1.
    U81553 Genomic DNA. Translation: AAB69099.1.
    PIRiC72804.
    RefSeqiNP_046853.1. NC_001900.1.

    Genome annotation databases

    GeneIDi1261565.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022214 Genomic DNA. Translation: AAC18478.1 .
    U81553 Genomic DNA. Translation: AAB69099.1 .
    PIRi C72804.
    RefSeqi NP_046853.1. NC_001900.1.

    3D structure databases

    ProteinModelPortali O22000.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1261565.

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR016193. Cytidine_deaminase-like.
    IPR016473. dCMP_deaminase.
    IPR015517. dCMP_deaminase-rel.
    [Graphical view ]
    PANTHERi PTHR11086. PTHR11086. 1 hit.
    Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006019. dCMP_deaminase. 1 hit.
    SUPFAMi SSF53927. SSF53927. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome structure of mycobacteriophage D29: implications for phage evolution."
      Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.
      J. Mol. Biol. 279:143-164(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Mycobacteriophage D29 contains an integration system similar to that of the temperate mycobacteriophage L5."
      Ribeiro G., Viveiros M., David H.L., Costa J.V.
      Microbiology 143:2701-2708(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-128.

    Entry informationi

    Entry nameiDCTD_BPMD2
    AccessioniPrimary (citable) accession number: O22000
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 63 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3