A0A0F8DI94 · A0A0F8DI94_CERFI

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 dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.

Caution

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 binding site.

TypeIDPosition(s)Description
Binding site1109-1114ATP (UniProtKB | ChEBI)
Binding site1135a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1157-1159a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1188-1191a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1195a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1226ATP (UniProtKB | ChEBI)
Binding site1232a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1243a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site1271ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentDNA replication preinitiation complex
Cellular ComponentMCM complex
Cellular Componentnuclear pre-replicative complex
Cellular Componentnuclear replication fork
Molecular Function(d)CMP kinase activity
Molecular FunctionATP binding
Molecular Functionhydrolase activity
Molecular Functionsingle-stranded DNA binding
Molecular Functionsingle-stranded DNA helicase activity
Molecular FunctionUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological ProcessDNA strand elongation involved in DNA replication
Biological ProcessDNA unwinding involved in DNA replication
Biological Processdouble-strand break repair via break-induced replication
Biological Processmitotic DNA replication initiation
Biological Processphosphorylation
Biological Processpremeiotic DNA replication
Biological Processpyrimidine nucleotide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Uridylate kinase
  • EC number
  • Short names
    UK
  • Alternative names
    • ATP:UMP phosphotransferase
    • Deoxycytidylate kinase
      (CK
      ; dCMP kinase
      )
    • Uridine monophosphate kinase
      (UMP kinase
      ; UMPK
      )

Gene names

    • Name
      mcm4
    • ORF names
      CFO_g2033

Organism names

  • Taxonomic identifier
  • Strain
    • CFO
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Microascales > Ceratocystidaceae > Ceratocystis

Accessions

  • Primary accession
    A0A0F8DI94

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-123Polar residues
Region1-175Disordered
Region297-334Disordered
Compositional bias306-331Polar residues
Domain566-774MCM
Region1129-1159NMPbind
Region1225-1235LID

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 MCM family.
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,291
  • Mass (Da)
    141,888
  • Last updated
    2015-07-22 v1
  • Checksum
    2B4153DB54948621
MSNNDDTPRRSGRNSSLNPGQPNSPLASTPSSAAETPRLPSHMASSPMFYQSSPAPMGANPSSPLAVDSQMTDSQDMGDRTPRASQMRTIRDSSPVNYPASSSPGRSIRQQSELHSDISGMFVSQGSDYGHESRRPARTEPPASFGQQPRPVPGSTPFIPPSTPGQTPLLNSEAENNNVGNNALIWGTTINLELTRSRVHQFLMEFTPRMRMIRDGMTDAEIAETPGANDYCYRDDMLLMLEMGVQTLPVSISDIKCFPGFESLAQQVIHYPQEMVPIFDQGIRDIMVSLAAQEDQKRARERYQNQANMPAATPNSELDSEFASTPVPSHHNRHQKSMEEIAQEAQYQVRMYGMNEISNMRSLDPSDIDKMITIKGLVIRATPVIPDMKTALFKCDVCGWCHSAYNERGRITEPTECPNANCNAKNSMQIQHNRCTFEDKQILKLQETPDDVPAGQTPHSVSVMMYRDMVDCCKAGDRVVITGIYRASPVRVNPTQRAIKSVHKTYVDAVHAQKIDKKRMGIDQSTLILDGDDSQPTEVNPSIPETRKITPEEERKILEASQKPDIYEILARSLAPSIYEMDDVKKGILLQLFGGTNKTFTKGGNPRYRGDINILLCGDPSTSKSQMLGYVHKIAPRGVYTSGKGSSAVGLTAYVTRDPETRQLVLESGALVLSDGGVCCIDEFDKMGEATRSVLHEVMEQQTVSVAKAGIITTLNARTSILASANPIGSRYNPNISVPQNIDLPPTLLSRFDLVYLILDRPDDKTDRRLAKHILSLYLEDTPDHAPTENEIMPVEFLTMYISYARSNVHPKITDAAATELTNSYVEMRKLGQDVRSSEKRITATTRQLESMIRLAEAHAKMRLSLEVTRDDVIEAYRLIKSALKTAATDSQGRIDMSLLTEGTSSADRRMKEDMKKAILGVIDELTASGNTVRWAEVLRKLSESVNVQVEASDFNECMRALEMEGAMVVMAIATATRSSGSVAAKPVLRNRMAAAGRRAYSAAAPSPPPAPKKKDGMSVLPFLGVVVVGTGAYIMLVNSRKDLAEQKRAQMAAERAAAAAAATAAAAPPEEVPAPEPTTTIEPNAPAIDTPAFNPDDVTVFFVLGGPGAGKGTQCARLVSEYGFTHLSAGDLLRAEQDRPGSQFGDLIRDYIKNGQIVPMEVTIKLLENAMTETMGAEKKGRFLIDGFPRKMDQAVKFEESVCPAKLVLFFECPEKELERRLLERGKTSGRADDNIESIRKRFRTFVETSMPVVDSFADSGRVVRIDSSPSPDEVYNTTIEELTKKVGKL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-123Polar residues
Compositional bias306-331Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LBBL01000085
EMBL· GenBank· DDBJ
KKF95629.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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