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Conserved domains on  [gi|446735458|ref|WP_000812714|]
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protein-serine/threonine phosphatase [Escherichia coli]

Protein Classification

protein-serine/threonine phosphatase( domain architecture ID 10013803)

protein-serine/threonine phosphatase catalyzes the removal of phosphoryl groups from phosphorylated serines/threonines in protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pphA PRK11439
protein-serine/threonine phosphatase;
1-218 2.69e-145

protein-serine/threonine phosphatase;


:

Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 403.38  E-value: 2.69e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458   1 MKQPAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNH 80
Cdd:PRK11439   1 MKQPAPVYQRIAGHQWRHIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEEHWVRAVRGNH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  81 EQMAMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQ 160
Cdd:PRK11439  81 EQMALDALASQQMSLWLMNGGDWFIALTDNQQKQAKTLLEKCQRLPFILEVHCRTGKHVIAHADYPADVYEWQKDVDLHQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458 161 VLWSRSRLGERPNRQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
Cdd:PRK11439 161 VLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
 
Name Accession Description Interval E-value
pphA PRK11439
protein-serine/threonine phosphatase;
1-218 2.69e-145

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 403.38  E-value: 2.69e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458   1 MKQPAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNH 80
Cdd:PRK11439   1 MKQPAPVYQRIAGHQWRHIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEEHWVRAVRGNH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  81 EQMAMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQ 160
Cdd:PRK11439  81 EQMALDALASQQMSLWLMNGGDWFIALTDNQQKQAKTLLEKCQRLPFILEVHCRTGKHVIAHADYPADVYEWQKDVDLHQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458 161 VLWSRSRLGERPNRQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
Cdd:PRK11439 161 VLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 17-218 1.07e-106

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 305.39  E-value: 1.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  17 RHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNHEQMAMDALASQQMSLW 96
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAIDALRGGDDVMW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  97 LMNGGDWFIALADNQQkqaKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQ---KDVDLHQVLWSRSRLGERpN 173
Cdd:cd07424   81 RANGGGWFFDLPDEEA---KVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGfveKPEDEEEALWSRDRLQKS-Q 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446735458 174 RQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
Cdd:cd07424  157 TQPVAGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 18-88 5.68e-10

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 54.91  E-value: 5.68e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446735458   18 HIWLSGDIH--GCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHW----VRAVRGNHEQMAMDAL 88
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIkyvpVYLVRGNHDFDYGECL 78
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
24-104 7.84e-10

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 56.08  E-value: 7.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  24 DIHGCLEQLRRKLWHcrFDPWR-DLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNHEQMAMDALASQQMSLWLMNGGD 102
Cdd:COG0622    7 DTHGNLPALEAVLED--LEREGvDLIVHLGDLVGYGPDPPEVLDLLRELPIVAVRGNHDGAVLRGLRSLPETLRLELEGV 84


                 ..
gi 446735458 103 WF 104
Cdd:COG0622   85 RI 86
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 20-81 1.01e-09

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 56.82  E-value: 1.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446735458   20 WLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQ--HWVRAVRGNHE 81
Cdd:TIGR00668   4 YLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSlgDAVRLVLGNHD 67
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 23-81 3.68e-04

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 40.27  E-value: 3.68e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458    23 GDIHGCLEQLRRkLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLeqhWVRAV---------RGNHE 81
Cdd:smart00156  34 GDIHGQFDDLLR-LFDKNGQPPETNYVFLGDYVDRGPFSIEVILLL---FALKIlypnrivllRGNHE 97
 
Name Accession Description Interval E-value
pphA PRK11439
protein-serine/threonine phosphatase;
1-218 2.69e-145

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 403.38  E-value: 2.69e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458   1 MKQPAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNH 80
Cdd:PRK11439   1 MKQPAPVYQRIAGHQWRHIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEEHWVRAVRGNH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  81 EQMAMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQ 160
Cdd:PRK11439  81 EQMALDALASQQMSLWLMNGGDWFIALTDNQQKQAKTLLEKCQRLPFILEVHCRTGKHVIAHADYPADVYEWQKDVDLHQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458 161 VLWSRSRLGERPNRQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
Cdd:PRK11439 161 VLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 17-218 1.07e-106

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 305.39  E-value: 1.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  17 RHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNHEQMAMDALASQQMSLW 96
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAIDALRGGDDVMW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  97 LMNGGDWFIALADNQQkqaKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQ---KDVDLHQVLWSRSRLGERpN 173
Cdd:cd07424   81 RANGGGWFFDLPDEEA---KVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGfveKPEDEEEALWSRDRLQKS-Q 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446735458 174 RQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
Cdd:cd07424  157 TQPVAGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201
PRK09968 PRK09968
protein-serine/threonine phosphatase;
4-218 3.10e-67

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 205.90  E-value: 3.10e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458   4 PAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNHEQM 83
Cdd:PRK09968   2 PSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLLNQPWFISVKGNHEAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  84 AMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQVLW 163
Cdd:PRK09968  82 ALDAFETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKFHHLPHIIEITNDNIKYVIAHADYPGDEYDFGKEIAESELLW 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446735458 164 SRSRLGE--RPNRQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
Cdd:PRK09968 162 PVDRVQKslNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPKSGRLSFYKIK 218
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 23-210 5.09e-18

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 79.34  E-value: 5.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  23 GDIHGCLEQLRRkLWHCRFDPWRDLLISVGDVIDRGPHS------LRCLQLLEQHWVRAVRGNHEQMAMDALASQQMSLW 96
Cdd:cd00144    4 GDIHGCFDDLLR-LLEKLGFPPEDKYLFLGDYVDRGPDSvevidlLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDERT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  97 LMNGGdwfialadnqqKQAKTALEKCQH----LPFILEVhsrTGKHVIAHADYPDDVYEWQ-----------KDVDLHQV 161
Cdd:cd00144   83 LRCLR-----------KGGEELWREFNEvfnyLPLAALV---DGKILCVHGGLSPDLTLLDqirnirpienpDDQLVEDL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458 162 LWSRSRLGERPNRQGITGADHFW------------------FGHTPLRHRVDI---GNLHYIDTGAVFGG 210
Cdd:cd00144  149 LWSDPDESVGDFESSSRGGGYLFgedavdeflkknglklivRGHTPVEGGYEFlhgGKLITIFSAPNYCG 218
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 19-81 2.77e-13

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 66.80  E-value: 2.77e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446735458  19 IWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHW--VRAVRGNHE 81
Cdd:cd07422    1 TYAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGdsAVVVLGNHD 65
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
19-81 6.32e-13

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 65.96  E-value: 6.32e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446735458  19 IWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHW--VRAVRGNHE 81
Cdd:PRK00166   3 TYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGdsAVTVLGNHD 67
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 23-213 8.82e-12

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 62.15  E-value: 8.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  23 GDIHGCLEQL----------RRKLWHCRFDPWRDLlISVGDVIDRGPHSLRCLQLLEQHWVR----AVRGNHEQMAMDAL 88
Cdd:cd07423    4 GDVHGCYDELvelleklgyqKKEEGLYVHPEGRKL-VFLGDLVDRGPDSIDVLRLVMNMVKAgkalYVPGNHCNKLYRYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  89 ASQQMSLwlmNGGD------WFIALADNQQKQAKTALEKCQHLPFILEVHSrtGKHVIAHADYPDD-------------V 149
Cdd:cd07423   83 KGRNVQL---AHGLettveeLEALSKEERPEFRERFAEFLESLPSHLVLDG--GRLVVAHAGIKEEmigrgskrvrdfcL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458 150 YewqKDVDlhqvlwsrsrlGE-----RPNRQGitgadhfW-----------FGHTPLRHRVDIGNLHYIDTGAVFGGELT 213
Cdd:cd07423  158 Y---GDTT-----------GEtdedgLPVRRD-------WakdyrgkalvvYGHTPVPEPRWLNNTINIDTGCVFGGKLT 216
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 18-88 5.68e-10

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 54.91  E-value: 5.68e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446735458   18 HIWLSGDIH--GCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQHW----VRAVRGNHEQMAMDAL 88
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIkyvpVYLVRGNHDFDYGECL 78
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
24-104 7.84e-10

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 56.08  E-value: 7.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  24 DIHGCLEQLRRKLWHcrFDPWR-DLLISVGDVIDRGPHSLRCLQLLEQHWVRAVRGNHEQMAMDALASQQMSLWLMNGGD 102
Cdd:COG0622    7 DTHGNLPALEAVLED--LEREGvDLIVHLGDLVGYGPDPPEVLDLLRELPIVAVRGNHDGAVLRGLRSLPETLRLELEGV 84


                 ..
gi 446735458 103 WF 104
Cdd:COG0622   85 RI 86
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 20-81 1.01e-09

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 56.82  E-value: 1.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446735458   20 WLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLEQ--HWVRAVRGNHE 81
Cdd:TIGR00668   4 YLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSlgDAVRLVLGNHD 67
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 23-213 1.82e-09

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 55.87  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  23 GDIHGCLEQ---LRRKL---W------HcrfdPWRDLLISVGDVIDRGPHSLRCLQ----LLEQHWVRAVRGNHEQMAMD 86
Cdd:PRK13625   7 GDIHGCYQEfqaLTEKLgynWssglpvH----PDQRKLAFVGDLTDRGPHSLRMIEivweLVEKKAAYYVPGNHCNKLYR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  87 ALASQQMSlwLMNGGDWFIA----LADNQQKQAKTALEKC-QHLPFILEVHSrtGKHVIAHADYPDDvYEWQKDVDLHQV 161
Cdd:PRK13625  83 FFLGRNVT--IAHGLETTVAeyeaLPSHKQNMIKEKFITLyEQAPLYHILDE--GRLVVAHAGIRQD-YIGRQDKKVQTF 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446735458 162 LWSRSRLGE-----RPNRQgiTGADHF----W--FGHTPLRHRVDIGNLHYIDTGAVFGGELT 213
Cdd:PRK13625 158 VLYGDITGEkhpdgSPVRR--DWAKEYkgtaWivYGHTPVKEPRFVNHTVNIDTGCVFGGRLT 218
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 23-84 1.14e-06

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 47.29  E-value: 1.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458  23 GDIHGCLEQLRRKLWHCRF----DPW---RDLLISVGDVIDRGPHSLRCLQLLEQHWVRAVR---------GNHEQMA 84
Cdd:cd07425    4 GDLHGDLDRLRTILKLAGVidsnDRWiggDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKaggkvilllGNHELMN 81
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 23-81 1.86e-04

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 41.43  E-value: 1.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446735458  23 GDIHGCLEQLRRKLWHCRFDPWRDLLIsVGDVIDRGPHSLR------CLQLLEQHWVRAVRGNHE 81
Cdd:PTZ00244  58 GDTHGQYYDLLRIFEKCGFPPYSNYLF-LGDYVDRGKHSVEtitlqfCYKIVYPENFFLLRGNHE 121
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 23-81 3.68e-04

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 40.27  E-value: 3.68e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458    23 GDIHGCLEQLRRkLWHCRFDPWRDLLISVGDVIDRGPHSLRCLQLLeqhWVRAV---------RGNHE 81
Cdd:smart00156  34 GDIHGQFDDLLR-LFDKNGQPPETNYVFLGDYVDRGPFSIEVILLL---FALKIlypnrivllRGNHE 97
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 23-81 1.05e-03

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 38.02  E-value: 1.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446735458  23 GDIHGCLEQLRRKLWH--CRFDPwRDLLISVGDVIDRGPHSLRCLQLLEQ-----HWVRAVRGNHE 81
Cdd:cd00838    4 SDIHGNLEALEAVLEAalAKAEK-PDLVICLGDLVDYGPDPEEVELKALRlllagIPVYVVPGNHD 68
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 23-88 1.57e-03

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 38.58  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735458  23 GDIHGCLEQLRR--KLWHCRFDP------WRDLLIsVGDVIDRGPHSLRCLQLL------EQHWVRAVRGNHEQMAMDAL 88
Cdd:cd07419   54 GDIHGQFGDLMRlfDEYGSPVTEeagdieYIDYLF-LGDYVDRGSHSLETICLLlalkvkYPNQIHLIRGNHEAADINAL 132
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 23-81 3.31e-03

PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 37.70  E-value: 3.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446735458  23 GDIHGCLEQLRRKLWHCRFDPWRDLLIsVGDVIDRGPHSLRCLQLLEQHWVR------AVRGNHE 81
Cdd:cd07414   56 GDIHGQYYDLLRLFEYGGFPPESNYLF-LGDYVDRGKQSLETICLLLAYKIKypenffLLRGNHE 119
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 23-81 6.90e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 36.37  E-value: 6.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446735458  23 GDIHGCLEQLRRKLWHCRFD----PWRD---LLISVGDVIDRGPHSLRCLQLLEQhWVRA-----VRGNHE 81
Cdd:cd07413    5 GDVHGCAHTLDRLLDLLGYRlqggVWRHprrQALFVGDLIDRGPRIREVLHRVHA-MVDAgealcVMGNHE 74
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
19-81 8.78e-03

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 36.15  E-value: 8.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446735458  19 IWLSGDIHGCLEQLRRKLWHCRF-DPwrDLLISVGDVIDRGPHS--LRCLQLLEQHWVR--AVRGNHE 81
Cdd:COG2129    2 ILAVSDLHGNFDLLEKLLELARAeDA--DLVILAGDLTDFGTAEeaREVLEELAALGVPvlAVPGNHD 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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