A0AAE1H791 · A0AAE1H791_9NEOP

Function

function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per monomer.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site249
Active site405
Active site433
Binding site910-915ATP (UniProtKB | ChEBI)
Binding site936a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site958-960a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site985-988a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site992CMP (UniProtKB | ChEBI)
Binding site1026ATP (UniProtKB | ChEBI)
Binding site1033a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1044a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1072ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Function(d)CMP kinase activity
Molecular FunctionATP binding
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent cysteine-type endopeptidase activity
Molecular FunctionUMP/dUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processphosphorylation
Biological Processproteolysis
Biological Processpyrimidine nucleotide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UMP-CMP kinase
  • EC number
  • Alternative names
    • Deoxycytidylate kinase
      (CK
      ; dCMP kinase
      )
    • Uridine monophosphate/cytidine monophosphate kinase
      (UMP/CMP kinase
      ; UMP/CMPK
      )

Gene names

    • ORF names
      KUF71_025345

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PL_HMW_Pooled
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Thysanoptera > Terebrantia > Thripoidea > Thripidae > Frankliniella

Accessions

  • Primary accession
    A0AAE1H791

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region29-115Disordered
Compositional bias80-100Basic and acidic residues
Domain194-493Calpain catalytic
Domain777-812EF-hand
Region930-960NMPbind

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Belongs to the peptidase C2 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,092
  • Mass (Da)
    122,568
  • Last updated
    2024-05-29 v1
  • MD5 Checksum
    0B4A2C316E3B93EEA3FE9B912903EAF2
MRESESCGGGLALKRRQDALDGILAASQLPARSGAGLERDSAEAAVGTSWTPPSPKGSRRAACRARPRARAARTSRGRGGAVRSGEEEKVEEERRVSRCPAGGAARRGTDGALASGVRASRTGACGLSAMGEVEEEIVVRKIAADVQEYRPLWSSFGFSIVGTQVGEKGSGVRARGEVQDFHKIQAQCLSEGVLWEDPNFPAVDSSIFYSRGPPKPFEWRRPGEISGDPQFMVGGASRFDIQQGELGDCWLLAAVANLTLNDELFFQVVPAEQGFEDNYCGVFHFRFWQYGRWLDVVIDDRLPTVYGELVFLHSSTKNEFWSALLEKAYAKLHGSYEALKGGTTCEGMEDFTGGVTEMYELKEAPGNLYKILLKAYERSSLMACSIEPDPYVTEARTPSGLVKGHAYSITRVQYVDVQTPRQSGKIPLIRLRNPWGNEAEWNGPWSDQSPEWRLIPEHNKEEIGLTFDDDGEFWMSYQDFLKHFTQLEMCNLSPDSMEDDNIKKWEANTYEGEWVRGVTAGGCRNYLDTFWHNPQYRVDLTDVDEDDDENRCTVIIALMQKNRRAQRKKGMECLTIGFAVYNLGHDPDSLPKPLDYNFFKYNASCARSPSFINLREVSCRFKLPPGSYCIVPSTFEPNEQGEFILRVYSEKRNTMEEHDEEVGIGHIDPRVKDEDEDAEMAKKDEKVKALFLKLAGEDGEVDWMELKEIMDYTMRNELPSRPRPPTQHQIAPMEDDTLVGQLVNLLCGVICKDTPLGTAFASGGDQGHAADTRSSGFAKEVCRSMVAMMDADHSGKLGYEEFKILWTDIRRWRAVFKLYCKEGSGFLNAFELRQALNSAGYRLNNHILNILFHRYGASDGTITFDDFMMCAIRMKTMIGLMLIKLVQGIRRFAMSAAQKPQIVFVLGAPGSGKGTVCKNIVDNYKFVHLSAGDLLREEQNTEGSEHGDLIKEYIKLGKIVPVEITCGLLKRAIEKSGSSRFLVDGFPRNQNNLDGWEKVMSECVDVKFVLFLDCSEDVCTQRCLNRGAQGSGRTDDNLDSLKKRFNTYSNETMPIIKYYEGKNMVRRVDSNRTLPEIFEDIKTIFTPFISGS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias80-100Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHWGI010000488
EMBL· GenBank· DDBJ
KAK3916097.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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