A0A0F8DI94 · A0A0F8DI94_CERFI
- ProteinUridylate kinase
- Genemcm4
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1291 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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.
Catalytic activity
- UMP + ATP = UDP + ADP
Cofactor
Note: Binds 1 Mg2+ ion per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 1109-1114 | ATP (UniProtKB | ChEBI) | |||
Binding site | 1135 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1157-1159 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1188-1191 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1195 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1226 | ATP (UniProtKB | ChEBI) | |||
Binding site | 1232 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1243 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1271 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | DNA replication preinitiation complex | |
Cellular Component | MCM complex | |
Cellular Component | nuclear pre-replicative complex | |
Cellular Component | nuclear replication fork | |
Molecular Function | (d)CMP kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | single-stranded DNA binding | |
Molecular Function | single-stranded DNA helicase activity | |
Molecular Function | UMP kinase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | DNA strand elongation involved in DNA replication | |
Biological Process | DNA unwinding involved in DNA replication | |
Biological Process | double-strand break repair via break-induced replication | |
Biological Process | mitotic DNA replication initiation | |
Biological Process | phosphorylation | |
Biological Process | premeiotic DNA replication | |
Biological Process | pyrimidine nucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUridylate kinase
- EC number
- Short namesUK
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Microascales > Ceratocystidaceae > Ceratocystis
Accessions
- Primary accessionA0A0F8DI94
Proteomes
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-123 | Polar residues | |||
Region | 1-175 | Disordered | |||
Region | 297-334 | Disordered | |||
Compositional bias | 306-331 | Polar residues | |||
Domain | 566-774 | MCM | |||
Region | 1129-1159 | NMPbind | |||
Region | 1225-1235 | LID | |||
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 statusComplete
- Length1,291
- Mass (Da)141,888
- Last updated2015-07-22 v1
- Checksum2B4153DB54948621
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-123 | Polar residues | |||
Compositional bias | 306-331 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LBBL01000085 EMBL· GenBank· DDBJ | KKF95629.1 EMBL· GenBank· DDBJ | Genomic DNA |