NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002296282|ref|XP_015611602|]
View 

probable inactive purple acid phosphatase 29 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10164588)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to Kluyveromyces lactis protein SIA1 that may be involved in the activation of the plasma membrane proton-ATPase by glucose; may be inactive

CATH:  3.60.21.10
Gene Ontology:  GO:0046872
PubMed:  25837850|8003970
SCOP:  3001067

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_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 51-332 6.15e-71

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 221.01  E-value: 6.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  51 TFKVVQVADMHYADGRRTGCLDVlpseaagCSDLNTTAFLYRLFRDEDPDLVVFTGDNIYGFDATD--AAKSMDAAIAPA 128
Cdd:cd07383     2 KFKILQFADLHFGEGEWTCWEGC-------EADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSPL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 129 INMNLPWAAVIGNHDqegtlsregvmrhlvgmkntlsrfnpegieidgygnynlevggvegtllanksvlnlyfldsgdy 208
Cdd:cd07383    75 VERGIPWAATFGNHD----------------------------------------------------------------- 89

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 209 stvpsigGYGWIKASQQFWFQQTSSNLQTKYmkeepkqKAAAPGLVYFHIPLPEFSSFTSSNFT--GVKQEGISSPSINS 286
Cdd:cd07383    90 -------GYDWIDPSQVEWFESTSAALKKKY-------GKNIPSLAFFHIPLPEYREVWNEKGKlgGINREKVCCQKTNS 155

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002296282 287 GFFASMVEAGDVKAAFIGHDHVNDFCGK-LNGIQLCYAGGFGYHAYG 332
Cdd:cd07383   156 GFFKALVKRGDVKAVFCGHDHGNDFCGRwKNGIWLCYGRHTGYGGYG 202
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 51-332 6.15e-71

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 221.01  E-value: 6.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  51 TFKVVQVADMHYADGRRTGCLDVlpseaagCSDLNTTAFLYRLFRDEDPDLVVFTGDNIYGFDATD--AAKSMDAAIAPA 128
Cdd:cd07383     2 KFKILQFADLHFGEGEWTCWEGC-------EADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSPL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 129 INMNLPWAAVIGNHDqegtlsregvmrhlvgmkntlsrfnpegieidgygnynlevggvegtllanksvlnlyfldsgdy 208
Cdd:cd07383    75 VERGIPWAATFGNHD----------------------------------------------------------------- 89

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 209 stvpsigGYGWIKASQQFWFQQTSSNLQTKYmkeepkqKAAAPGLVYFHIPLPEFSSFTSSNFT--GVKQEGISSPSINS 286
Cdd:cd07383    90 -------GYDWIDPSQVEWFESTSAALKKKY-------GKNIPSLAFFHIPLPEYREVWNEKGKlgGINREKVCCQKTNS 155

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002296282 287 GFFASMVEAGDVKAAFIGHDHVNDFCGK-LNGIQLCYAGGFGYHAYG 332
Cdd:cd07383   156 GFFKALVKRGDVKAVFCGHDHGNDFCGRwKNGIWLCYGRHTGYGGYG 202
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-336 1.08e-16

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 78.58  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  52 FKVVQVADMHYADGRRTGCLDVLpseAAGCSDLNttaflyrlfrDEDPDLVVFTGDNIYgfDATDAakSMDAAIAPAINM 131
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVL---AAALADIN----------APRPDFVVVTGDLTD--DGEPE--EYAAAREILARL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 132 NLPWAAVIGNHDQEGTLSREgvMRHLVGMKNTLSRfnpegieidgygNYNLEVGGVegtllanksvlNLYFLDSGDYStv 211
Cdd:COG1409    64 GVPVYVVPGNHDIRAAMAEA--YREYFGDLPPGGL------------YYSFDYGGV-----------RFIGLDSNVPG-- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 212 psiGGYGWIKASQQFWFQQTSSNLqtkymKEEPKqkaaapgLVYFHIPLpeFSSFTSSNFTGVKqegisspsiNSGFFAS 291
Cdd:COG1409   117 ---RSSGELGPEQLAWLEEELAAA-----PAKPV-------IVFLHHPP--YSTGSGSDRIGLR---------NAEELLA 170

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002296282 292 MVEAGDVKAAFIGHDHVNDFcGKLNGIQLCYAGGFGYHAYGKAGW 336
Cdd:COG1409   171 LLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTGGQVRLPPGY 214
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 52-143 5.90e-06

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: 44.90  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  52 FKVVQVADMHYADGRRTgcldvlpseaagcsdlnTTAFLYRLFRDEDPDLVVFTGDNIYGFDATDAAksmdAAIAPAINM 131
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------------LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEV----LELLERLIK 59

                          90
                  ....*....|..
gi 1002296282 132 NLPWAAVIGNHD 143
Cdd:pfam00149  60 YVPVYLVRGNHD 71
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 51-332 6.15e-71

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 221.01  E-value: 6.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  51 TFKVVQVADMHYADGRRTGCLDVlpseaagCSDLNTTAFLYRLFRDEDPDLVVFTGDNIYGFDATD--AAKSMDAAIAPA 128
Cdd:cd07383     2 KFKILQFADLHFGEGEWTCWEGC-------EADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSPL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 129 INMNLPWAAVIGNHDqegtlsregvmrhlvgmkntlsrfnpegieidgygnynlevggvegtllanksvlnlyfldsgdy 208
Cdd:cd07383    75 VERGIPWAATFGNHD----------------------------------------------------------------- 89

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 209 stvpsigGYGWIKASQQFWFQQTSSNLQTKYmkeepkqKAAAPGLVYFHIPLPEFSSFTSSNFT--GVKQEGISSPSINS 286
Cdd:cd07383    90 -------GYDWIDPSQVEWFESTSAALKKKY-------GKNIPSLAFFHIPLPEYREVWNEKGKlgGINREKVCCQKTNS 155

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002296282 287 GFFASMVEAGDVKAAFIGHDHVNDFCGK-LNGIQLCYAGGFGYHAYG 332
Cdd:cd07383   156 GFFKALVKRGDVKAVFCGHDHGNDFCGRwKNGIWLCYGRHTGYGGYG 202
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-336 1.08e-16

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 78.58  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  52 FKVVQVADMHYADGRRTGCLDVLpseAAGCSDLNttaflyrlfrDEDPDLVVFTGDNIYgfDATDAakSMDAAIAPAINM 131
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVL---AAALADIN----------APRPDFVVVTGDLTD--DGEPE--EYAAAREILARL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 132 NLPWAAVIGNHDQEGTLSREgvMRHLVGMKNTLSRfnpegieidgygNYNLEVGGVegtllanksvlNLYFLDSGDYStv 211
Cdd:COG1409    64 GVPVYVVPGNHDIRAAMAEA--YREYFGDLPPGGL------------YYSFDYGGV-----------RFIGLDSNVPG-- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282 212 psiGGYGWIKASQQFWFQQTSSNLqtkymKEEPKqkaaapgLVYFHIPLpeFSSFTSSNFTGVKqegisspsiNSGFFAS 291
Cdd:COG1409   117 ---RSSGELGPEQLAWLEEELAAA-----PAKPV-------IVFLHHPP--YSTGSGSDRIGLR---------NAEELLA 170

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002296282 292 MVEAGDVKAAFIGHDHVNDFcGKLNGIQLCYAGGFGYHAYGKAGW 336
Cdd:COG1409   171 LLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTGGQVRLPPGY 214
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 52-143 5.90e-06

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: 44.90  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  52 FKVVQVADMHYADGRRTgcldvlpseaagcsdlnTTAFLYRLFRDEDPDLVVFTGDNIYGFDATDAAksmdAAIAPAINM 131
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------------LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEV----LELLERLIK 59

                          90
                  ....*....|..
gi 1002296282 132 NLPWAAVIGNHD 143
Cdd:pfam00149  60 YVPVYLVRGNHD 71
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
52-143 6.99e-06

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 47.10  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  52 FKVVQVADMHYadGRRTGcldvlpseaagcsdlntTAFLYRLFR---DEDPDLVVFTGDNIygfdaTDAAKSMDAAIAP- 127
Cdd:COG1408    43 LRIVQLSDLHL--GPFIG-----------------GERLERLVEkinALKPDLVVLTGDLV-----DGSVAELEALLELl 98

                          90
                  ....*....|....*..
gi 1002296282 128 -AINMNLPWAAVIGNHD 143
Cdd:COG1408    99 kKLKAPLGVYAVLGNHD 115
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 80-143 5.96e-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: 42.64  E-value: 5.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002296282  80 GCSDLNTTAFLYRLFRDEDPDLVVFTGDNIYGFDATDAAksmDAAIAPAINMNLPWAAVIGNHD 143
Cdd:cd00838     8 GNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEV---ELKALRLLLAGIPVYVVPGNHD 68
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 52-151 1.15e-04

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 43.04  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  52 FKVVQVADMHYAD-GRRTGCLDVLpseaagcsdlnttaflyRLFRDEDPDLVVFTGDNIygfdaTDAAKSMDAAIAPAIN 130
Cdd:cd07385     2 LRIVQLSDIHLGPfVGRTRLQKVV-----------------RKVNELNPDLIVITGDLV-----DGDVSVLRLLASPLSK 59

                          90       100
                  ....*....|....*....|...
gi 1002296282 131 MNLPWA--AVIGNHDQEGTLSRE 151
Cdd:cd07385    60 LKAPLGvyFVLGNHDYYSGDVEV 82
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
82-189 1.68e-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: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  82 SDLNTTAFLYRLF----RDEDPDLVVFTGDniygFDATDAAKSMDAAIAPAINMNLPWAAVIGNHD---QEGTLSREGVm 154
Cdd:COG2129     6 SDLHGNFDLLEKLlelaRAEDADLVILAGD----LTDFGTAEEAREVLEELAALGVPVLAVPGNHDdpeVLDALEESGV- 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002296282 155 RHLVGmkntlsrfnpEGIEIDGYGnynleVGGVEG 189
Cdd:COG2129    81 HNLHG----------RVVEIGGLR-----IAGLGG 100
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
95-175 4.21e-03

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 38.36  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296282  95 RDEDPDLVVFTGDnIygFD----ATDAAKSMDAAIAPAINMNLPWAAVIGNHDQegtLSREGVMRHLVGMKNT--LSRFN 168
Cdd:COG0420    36 IEEKVDAVLIAGD-L--FDsanpSPEAVRLLAEALRRLSEAGIPVVLIAGNHDS---PSRLSAGSPLLENLGVhvFGSVE 109


                  ....*..
gi 1002296282 169 PEGIEID 175
Cdd:COG0420   110 PEPVELE 116
 
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