Conserved Protein Domain Family

pfam05191: ADK_lid 
Click on image for an interactive view with Cn3D
Adenylate kinase, active site lid
Comparisons of adenylate kinases have revealed a particular divergence in the active site lid. In some organisms, particularly the Gram-positive bacteria, residues in the lid domain have been mutated to cysteines and these cysteine residues are responsible for the binding of a zinc ion. The bound zinc ion in the lid domain, is clearly structurally homologous to Zinc-finger domains. However, it is unclear whether the adenylate kinase lid is a novel zinc-finger DNA/RNA binding domain, or that the lid bound zinc serves a purely structural function.
PSSM-Id: 398731
Aligned: 463 rows
Threshold Bit Score: 37.8219
Threshold Setting Gi: 46396092
Created: 20-May-2020
Updated: 7-Aug-2020
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
Format: Row Display: Color Bits: Type Selection:
3BE4_A         132 RCTHPASGRIYHvkY-NPPKQPGIDDVTGEpLVWRDD 167 Cryptosporidium parvum Iowa II
Q2FW27         127 RRICESCGTTYHl-VfNPPKVEGICDIDGGkLYQRED 162 Staphylococcus aureus subsp. aureus NCTC 8325
BAK14664       127 RRICKTCGTSYHl-VfNPPKVDGICDKDGGeLYTRAD 162 Solibacillus silvestris StLB046
WP_012965606   127 RRICKQCGAVYNl-IyNPPKVDGKCDKCGGeLYQRDD 162 Ferroglobus placidus
WP_003775223   127 RRLCKDCGAIYHi-DnNPPKVESKCDICGGeLYQRSD 162 Erysipelothrix rhusiopathiae
WP_013719575   127 RRMCK-CGTTYHv-QfNPPKVEGKCDACGAdLYQRAD 161 Methanothrix soehngenii
WP_010073720   127 RRMCKNCGASYHv-TfNPPKVEGKCDLCEGpLVQRKD 162 Clostridium cellulovorans
jgi:Ethha_0388 123 RRVCEICGTSYHt-EyRPPKTEGICDADGGrLVQRAD 158 Ethanoligenens harbinense YUAN-3
A0B9A2         127 RRMCK-CGRSYHi-IfNPPKVPGKCDECGGeLYHRDD 161 Methanothrix thermoacetophila PT
B2A4G2         125 RRICRKCGKSYHikF-NPPQVRGVCDEDEGeLYQRDD 160 Natranaerobius thermophilus JW/NM-WN-LF
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap