NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|332641321|gb|AEE74842|]
View 

Calcineurin-like metallo-phosphoesterase superfamily protein [Arabidopsis thaliana]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164859)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 5-308 0e+00

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, 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: 163664  Cd Length: 304  Bit Score: 642.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321   5 PRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGNHDFA 84
Cdd:cd07421    1 PRVVICVGDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHVFLCGNHDFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321  85 FSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTFESYG 164
Cdd:cd07421   81 FAAFLGVLPRPSDGSEFKSTWKEYEKNEEREGWYKGEGFENMHLQGRRWAGKMKVTFNTVRGEPYKGSIYDARPTFESYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321 165 VPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSG 244
Cdd:cd07421  161 VPHGSSDLIKAVPEEHKKFLRNLVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKSNSVEEQLKLLRTKDTSIPKIAPLSG 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332641321 245 RKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLS 308
Cdd:cd07421  241 RKNVWNIPQELADKKTIVVSGHHGKLHIDGLRLIIDEGGGFDDRPIAAIVLPSKEIIRDTDNFS 304
 
Name Accession Description Interval E-value
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 5-308 0e+00

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, 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: 163664  Cd Length: 304  Bit Score: 642.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321   5 PRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGNHDFA 84
Cdd:cd07421    1 PRVVICVGDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHVFLCGNHDFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321  85 FSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTFESYG 164
Cdd:cd07421   81 FAAFLGVLPRPSDGSEFKSTWKEYEKNEEREGWYKGEGFENMHLQGRRWAGKMKVTFNTVRGEPYKGSIYDARPTFESYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321 165 VPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSG 244
Cdd:cd07421  161 VPHGSSDLIKAVPEEHKKFLRNLVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKSNSVEEQLKLLRTKDTSIPKIAPLSG 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332641321 245 RKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLS 308
Cdd:cd07421  241 RKNVWNIPQELADKKTIVVSGHHGKLHIDGLRLIIDEGGGFDDRPIAAIVLPSKEIIRDTDNFS 304
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 7-120 4.06e-09

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: 53.76  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321    7 TVICVGDIH--GYISKLNNLWLNLQSAIDPSdfssaLVIFLGDYCDRGPETRKVIDFLISLPEKHPdqtHVFLAGNHDFA 84
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPD-----LVLHAGDLVDRGPPSEEVLELLERLIKYVP---VYLVRGNHDFD 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 332641321   85 FSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTG 120
Cdd:pfam00149  74 YGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
11-94 1.31e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 47.99  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321  11 VGDIHGYISKLNNLWLNLQSA-IDpsdfssaLVIFLGDYCDRGPETRKVIDFLISLPekhpdqtHVFLAGNHDFAFSGFL 89
Cdd:COG0622    5 ISDTHGNLPALEAVLEDLEREgVD-------LIVHLGDLVGYGPDPPEVLDLLRELP-------IVAVRGNHDGAVLRGL 70


                 ....*
gi 332641321  90 GLLPR 94
Cdd:COG0622   71 RSLPE 75
PHA02239 PHA02239
putative protein phosphatase
 7-85 1.52e-06

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 48.45  E-value: 1.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332641321   7 TVICVGDIHGYISKLNNLWLNLQSAIDPSDfssaLVIFLGDYCDRGPETRKVIDFLISLPEKhpDQTHVFLAGNHDFAF 85
Cdd:PHA02239   2 AIYVVPDIHGEYQKLLTIMDKINNERKPEE----TIVFLGDYVDRGKRSKDVVNYIFDLMSN--DDNVVTLLGNHDDEF 74
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 8-81 3.49e-06

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: 47.59  E-value: 3.49e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332641321     8 VICvGDIHGYISKLnnlwLNLQSAIDPsdFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVfLAGNH 81
Cdd:smart00156  31 TVC-GDIHGQFDDL----LRLFDKNGQ--PPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVL-LRGNH 96
 
Name Accession Description Interval E-value
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 5-308 0e+00

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, 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: 163664  Cd Length: 304  Bit Score: 642.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321   5 PRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGNHDFA 84
Cdd:cd07421    1 PRVVICVGDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHVFLCGNHDFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321  85 FSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTFESYG 164
Cdd:cd07421   81 FAAFLGVLPRPSDGSEFKSTWKEYEKNEEREGWYKGEGFENMHLQGRRWAGKMKVTFNTVRGEPYKGSIYDARPTFESYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321 165 VPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSG 244
Cdd:cd07421  161 VPHGSSDLIKAVPEEHKKFLRNLVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKSNSVEEQLKLLRTKDTSIPKIAPLSG 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332641321 245 RKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLS 308
Cdd:cd07421  241 RKNVWNIPQELADKKTIVVSGHHGKLHIDGLRLIIDEGGGFDDRPIAAIVLPSKEIIRDTDNFS 304
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 9-89 4.12e-17

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: 78.57  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321   9 ICVGDIHGYISKLNNLWLNLQsaidpsDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQtHVFLAGNHDFAFSGF 88
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLG------FPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDN-VFLLRGNHEFMLLNF 73


                 .
gi 332641321  89 L 89
Cdd:cd00144   74 L 74
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 7-120 4.06e-09

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: 53.76  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321    7 TVICVGDIH--GYISKLNNLWLNLQSAIDPSdfssaLVIFLGDYCDRGPETRKVIDFLISLPEKHPdqtHVFLAGNHDFA 84
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPD-----LVLHAGDLVDRGPPSEEVLELLERLIKYVP---VYLVRGNHDFD 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 332641321   85 FSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTG 120
Cdd:pfam00149  74 YGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 12-82 1.95e-07

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: 51.67  E-value: 1.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332641321  12 GDIHGYISKLNNLWLNLQSAIDPS--DFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVfLAGNHD 82
Cdd:cd07419   54 GDIHGQFGDLMRLFDEYGSPVTEEagDIEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHL-IRGNHE 125
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
11-94 1.31e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 47.99  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321  11 VGDIHGYISKLNNLWLNLQSA-IDpsdfssaLVIFLGDYCDRGPETRKVIDFLISLPekhpdqtHVFLAGNHDFAFSGFL 89
Cdd:COG0622    5 ISDTHGNLPALEAVLEDLEREgVD-------LIVHLGDLVGYGPDPPEVLDLLRELP-------IVAVRGNHDGAVLRGL 70


                 ....*
gi 332641321  90 GLLPR 94
Cdd:COG0622   71 RSLPE 75
PHA02239 PHA02239
putative protein phosphatase
 7-85 1.52e-06

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 48.45  E-value: 1.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332641321   7 TVICVGDIHGYISKLNNLWLNLQSAIDPSDfssaLVIFLGDYCDRGPETRKVIDFLISLPEKhpDQTHVFLAGNHDFAF 85
Cdd:PHA02239   2 AIYVVPDIHGEYQKLLTIMDKINNERKPEE----TIVFLGDYVDRGKRSKDVVNYIFDLMSN--DDNVVTLLGNHDDEF 74
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 8-81 3.49e-06

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: 47.59  E-value: 3.49e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332641321     8 VICvGDIHGYISKLnnlwLNLQSAIDPsdFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVfLAGNH 81
Cdd:smart00156  31 TVC-GDIHGQFDDL----LRLFDKNGQ--PPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVL-LRGNH 96
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 8-82 2.16e-05

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 45.19  E-value: 2.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332641321   8 VICVGDIHGYISKLNNLWLnlqsaiDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQThVFLAGNHD 82
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFK------EGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNI-TLLRGNHE 112
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 9-86 2.68e-05

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: 43.02  E-value: 2.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332641321   9 ICVGDIHGYISKLNNLWLNLQSAIDPSDFssalVIFLGDYCDRGPETRKVIDFLISLpEKHPDQTHVfLAGNHDFAFS 86
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDL----VICLGDLVDYGPDPEEVELKALRL-LLAGIPVYV-VPGNHDILVT 72
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 8-82 3.86e-05

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, 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: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 44.61  E-value: 3.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332641321   8 VICVGDIHGYISKLNNLwlnLQSAIDPSDFSsalVIFLGDYCDRGPETRKVIDFLISLPEKHPDqTHVFLAGNHD 82
Cdd:cd07416   45 VTVCGDIHGQFYDLLKL---FEVGGSPANTR---YLFLGDYVDRGYFSIECVLYLWALKILYPK-TLFLLRGNHE 112
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 9-81 4.65e-05

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: 43.44  E-value: 4.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332641321   9 ICVGDIHGYISKLNNLwLNLQSAIDPSD---FSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQ--THVFLAGNH 81
Cdd:cd07425    1 VAIGDLHGDLDRLRTI-LKLAGVIDSNDrwiGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAggKVILLLGNH 77
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 11-82 1.07e-04

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: 42.30  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332641321  11 VGDIHGYISKLnnlwlnlQSAIDPSDFSSA--LVIFLGDYCDRGPETRKVIDFLislpekhpdQTHVFLA--GNHD 82
Cdd:cd07424    6 VGDIHGHFQRL-------QRALDAVGFDPArdRLISVGDLVDRGPESLEVLELL---------KQPWFHAvqGNHE 65
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 11-125 1.84e-04

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: 42.15  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321  11 VGDIHGYISKLNNLWLNLQSAIDPSDFSSA--LVIFLGDYCDRGPETRKVIDFLISLPEKhpdQTHVFLAGNHDFAFSGF 88
Cdd:cd07413    4 IGDVHGCAHTLDRLLDLLGYRLQGGVWRHPrrQALFVGDLIDRGPRIREVLHRVHAMVDA---GEALCVMGNHEFNALAW 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 332641321  89 -LGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFED 125
Cdd:cd07413   81 hTPAPPGSGRQYVREHSPKNARQHKATLDQFEGHDWRD 118
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 9-84 4.51e-04

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: 41.17  E-value: 4.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332641321   9 ICvGDIHGYISKLnnLWLNLQSAIDPSdfssALVIFLGDYCDRGPETRKVIDFLISLPEKHPDqTHVFLAGNHDFA 84
Cdd:cd07414   54 IC-GDIHGQYYDL--LRLFEYGGFPPE----SNYLFLGDYVDRGKQSLETICLLLAYKIKYPE-NFFLLRGNHECA 121
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 11-81 5.04e-04

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.84  E-value: 5.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332641321  11 VGDIHGYISKLNNLWLNLQSAID---PSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKhpdQTHVFLAGNH 81
Cdd:PRK13625   6 IGDIHGCYQEFQALTEKLGYNWSsglPVHPDQRKLAFVGDLTDRGPHSLRMIEIVWELVEK---KAAYYVPGNH 76
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
8-83 1.17e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 39.61  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321   8 VICVGDIHGYISKLNNLWLNLQSA-IDpsdfssaLVIFLGDYCDRGP--ETRKVIDFLISLPekhpdqTHV-FLAGNHDF 83
Cdd:COG2129    2 ILAVSDLHGNFDLLEKLLELARAEdAD-------LVILAGDLTDFGTaeEAREVLEELAALG------VPVlAVPGNHDD 68
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 7-85 6.62e-03

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB belongs 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 36.07  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332641321   7 TVICVGDIHGYISklnnlwlnlQSAIDPSDFssalVIFLGDYCDRGP--ETRKVIDFLISLPEKHpdqtHVFLAGNHDFA 84
Cdd:cd07379    1 RFVCISDTHSRHP---------TISIPDGDV----LIHAGDFTEGGTpdEVKKFLDWLKSLPHPH----KIVIAGNHDLT 63


                 .
gi 332641321  85 F 85
Cdd:cd07379   64 L 64
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 8-85 9.57e-03

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 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, 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: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 37.47  E-value: 9.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332641321   8 VICVGDIHGYISKLNNLwlnLQSAIDPSdfSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQThVFLAGNHDFAF 85
Cdd:cd07418   68 VVVVGDVHGQLHDVLFL---LEDAGFPD--QNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRV-YLLRGNHESKF 139
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH