3GMT,6RZE,3NDP,3TLX,5G3Z


Conserved Protein Domain Family
ADK_lid

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pfam05191: ADK_lid (This model is not part of the current CDD release)
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.
Statistics
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PSSM-Id: 516686
Aligned: 400 rows
Threshold Bit Score: 38.99
Created: 14-Feb-2025
Updated: 28-Apr-2025
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
3GMT_A        131 RRTHPASGRTYH-VKFNPPKVEGKDDVTGEpLVQRDD 166 Burkholderia pseudomallei 1710b
B1VAC7        127 RRICSHCGKVYHlDN-LPPKIEGICDKDQKkLIQRED 162 Candidatus Phytoplasma australiense
WP_016340484  126 RRICPKCGKTYH-LTALPPKQEGLCDLDGSaLIQRAD 161 Spiroplasma syrphidicola
WP_014730476  127 RRVCPECGKVYNlLT-IRPKVEGRCDNDGAeLIQRDD 162 Mesotoga prima
C5CGI1        127 RRVCPSCGKVYNlLT-IKPKNDMLCDDCNIgLIQRED 162 Kosmotoga olearia TBF 19.5.1
P38372        127 RRVSPTSGRTYH-VIFNPPKVEGICDVDGSeLIQRDD 162 Halalkalibacterium halodurans C-125
jgi:Cwoe_1361 130 RRVSAKTGRPYHvET-DPPKHEGRCDIDGSrLIQRDD 165
Q5WLP1        127 RRVSPTTGKTYH-IVYNPPKVEGKCDIDGSdLIQRDD 162 Shouchella clausii KSM-K16
WP_013254120  122 RRIAKKSGRVYHiQY-NPPAKEGICDESGEpLIQRPD 157 Sediminispirochaeta smaragdinae
WP_014245797  125 RRIAPKSGEIYNlLS-RPPKVEGKCDVSGEdLIHRKD 160 Halobacteriovorax marinus
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