Conserved Protein Domain Family
PNK-3'Pase

?
TIGR01663: PNK-3'Pase 
polynucleotide 5'-kinase 3'-phosphatase
This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78
Statistics
?
PSSM-Id: 130724
View PSSM: TIGR01663
Aligned: 2 rows
Threshold Bit Score: 983.362
Threshold Setting Gi: 7299027
Created: 8-Oct-2014
Updated: 2-Oct-2020
Structure
?
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
AAK57340   2 GEVEAPGRLWLES----PPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQ 77  human
AAF54229   7 RSVGKAGKDVAARictlKPTEPEHHSIHLTAGENFVGRSRETGIRDSKCSKRQIQLQVDLKKAVVSLKVLGVNPCGVNGL 86  fruit fly
AAK57340  78 ELKPGLEGSLGVGDTLYLVNGLHpltlRWEETRTPESQPDTPPGTPLVSQDEkrDAELPKKRMRKSNpgwenlEKLLVFT 157 human
AAF54229  87 MLMQNGERELKHGDLVEIVYGRH----QFEVVFNPPPEYDKEKAEPLSTTLS--PSEKSERWDSSGN------GKLVIFT 154 fruit fly
AAK57340 158 AAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIPRKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVE 237 human
AAF54229 155 SVGVKGSEKIAGYDMDGTIIKTKSGLVFPKNTDDWQIIFPEVPEKLKNLHKDGFKICLFTNQGGIARGKINLDDFKVKIK 234 fruit fly
AAK57340 238 AVVEKLGVPFQVLVATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPAN-WAPGRKKKDFSCADRLFALN 316 human
AAF54229 235 HIVAKLGVPIQVFIAIGDGFYRKPLTGMWQHLKSEMNDGVEIQEDRCFFVGDAAGRPETgKGATKRRKDHSLVDRLFAAN 314 fruit fly
AAK57340 317 LGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSGPLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNR 396 human
AAF54229 315 VGISFYTPEVHFLGKQVEQWNKPDFEPTSVQDQVSLLDPDDLTLDDHPCEMVIMVGLPGSGKSHFCSSFFQPRGYKIVNA 394 fruit fly
AAK57340 397 DTLGSWQRCVTTCETALKQGKRVAIDNTNPDAASRARYVQCARAAGVPCRCFLFTATLEQARHNNRFREMTDSSHIPVSD 476 human
AAF54229 395 DTLGSTQNCLTACKRFLDSGQSCVVDNTNVDAASRKKFLQLASEKMIPCRCLVMNVPVAQVKHNIAFRELSDSARTKIKD 474 fruit fly
AAK57340 477 MVMYGYRKQFEAPTLAEGFSAILEIPFR-LWVEPRLGRLYCQFSEG 521 human
AAF54229 475 MVFNMMKKKYQEPALDEGFISIHKVNFKpNFADEKQEKLYKMYLVE 520 fruit fly
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap