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Conserved domains on  [gi|490219197|ref|WP_004117574|]
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MULTISPECIES: phosphodiesterase [Klebsiella]

Protein Classification

phosphodiesterase( domain architecture ID 10164715)

phosphodiesterase of the metallophosphatase (MPP) superfamily, related to Enterobacter aerogenes glycerophosphodiesterase Q and Escherichia coli 3',5'-cyclic AMP phosphodiesterase CpdA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-244 5.64e-95

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 279.55  E-value: 5.64e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTHFRSRGQKLYGFIDVNAANADVVSQLNALQERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGNHD 82
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  83 DKALFLEYLHPLCPQlgrDAQNMHYAVDDFATRLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATVFMHHPPLPL 162
Cdd:cd07402   81 DRAAMREALPEPPYD---DNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197 163 GNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLTMTQYRQAIISTIPGTVHQVPYFHEDTRP-YYDLSPASCLMHR 241
Cdd:cd07402  158 GIPWMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALdAEAPGPRNLLLHA 237


                 ...
gi 490219197 242 QVD 244
Cdd:cd07402  238 DGI 240
 
Name Accession Description Interval E-value
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-244 5.64e-95

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 279.55  E-value: 5.64e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTHFRSRGQKLYGFIDVNAANADVVSQLNALQERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGNHD 82
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  83 DKALFLEYLHPLCPQlgrDAQNMHYAVDDFATRLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATVFMHHPPLPL 162
Cdd:cd07402   81 DRAAMREALPEPPYD---DNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197 163 GNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLTMTQYRQAIISTIPGTVHQVPYFHEDTRP-YYDLSPASCLMHR 241
Cdd:cd07402  158 GIPWMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALdAEAPGPRNLLLHA 237


                 ...
gi 490219197 242 QVD 244
Cdd:cd07402  238 DGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-223 1.03e-51

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 168.72  E-value: 1.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   1 MLLAQISDTHFRSRGQKlygfiDVNAANADVVSQLNAlqERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGN 80
Cdd:COG1409    1 FRFAHISDLHLGAPDGS-----DTAEVLAAALADINA--PRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  81 HDD----KALFLEYLHPLcpqlgrDAQNMHYAVDDFATRLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATVFMH 156
Cdd:COG1409   74 HDIraamAEAYREYFGDL------PPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLH 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490219197 157 HPPLPLGNAqMDPIACENGHRLLALVERFPsLTRIFCGHNHSLTMTQYRQAIISTIPGTVHQVPYFH 223
Cdd:COG1409  148 HPPYSTGSG-SDRIGLRNAEELLALLARYG-VDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPP 212
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 3-197 2.00e-18

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 82.67  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTH-FRSRGQKLYGfidVNAAN--ADVVSQLNALQERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPG 79
Cdd:PRK11148  17 ILQITDTHlFADEHETLLG---VNTWEsyQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGIAPLRKPCVWLPG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  80 NHDDKALFLEYL--HPLCPQ----LGRDAQnmhyavddfatrLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATV 153
Cdd:PRK11148  94 NHDFQPAMYSALqdAGISPAkhvlIGEHWQ------------ILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTLV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490219197 154 FMHHPPLPLGNAQMDPIACENGHRLLALVERFPSLTRIFCGHNH 197
Cdd:PRK11148 162 LLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIH 205
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 1-99 2.86e-08

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 53.19  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197    1 MLLAQISDTHFrsrGQKLYGFiDVNAANADVVSQLN--ALQERPDAVVVSGDIVNCGRPEEYevARQILGS--LNY---- 72
Cdd:TIGR00619   1 MRILHTSDWHL---GKTLEGV-SRLAEQKAFLDDLLefAKAEQVDALLVAGDVFDTANPPAE--AQELFNAffVNLsdtg 74

                          90       100
                  ....*....|....*....|....*....
gi 490219197   73 --PLYLIPGNHDDKAlFLEYLHPLCPQLG 99
Cdd:TIGR00619  75 irPIVVISGNHDSAQ-RLSAAKKLLAELG 102
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-83 3.56e-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: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197    1 MLLAQISDTHFRsrGQKlygfidvnAANADVVSQLNAlQERPDAVVVSGDIVNCGRPEEyEVARQILGSLNY-PLYLIPG 79
Cdd:pfam00149   1 MRILVIGDLHLP--GQL--------DDLLELLKKLLE-EGKPDLVLHAGDLVDRGPPSE-EVLELLERLIKYvPVYLVRG 68


                  ....
gi 490219197   80 NHDD 83
Cdd:pfam00149  69 NHDF 72
 
Name Accession Description Interval E-value
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-244 5.64e-95

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 279.55  E-value: 5.64e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTHFRSRGQKLYGFIDVNAANADVVSQLNALQERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGNHD 82
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  83 DKALFLEYLHPLCPQlgrDAQNMHYAVDDFATRLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATVFMHHPPLPL 162
Cdd:cd07402   81 DRAAMREALPEPPYD---DNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197 163 GNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLTMTQYRQAIISTIPGTVHQVPYFHEDTRP-YYDLSPASCLMHR 241
Cdd:cd07402  158 GIPWMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALdAEAPGPRNLLLHA 237


                 ...
gi 490219197 242 QVD 244
Cdd:cd07402  238 DGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-223 1.03e-51

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 168.72  E-value: 1.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   1 MLLAQISDTHFRSRGQKlygfiDVNAANADVVSQLNAlqERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGN 80
Cdd:COG1409    1 FRFAHISDLHLGAPDGS-----DTAEVLAAALADINA--PRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  81 HDD----KALFLEYLHPLcpqlgrDAQNMHYAVDDFATRLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATVFMH 156
Cdd:COG1409   74 HDIraamAEAYREYFGDL------PPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLH 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490219197 157 HPPLPLGNAqMDPIACENGHRLLALVERFPsLTRIFCGHNHSLTMTQYRQAIISTIPGTVHQVPYFH 223
Cdd:COG1409  148 HPPYSTGSG-SDRIGLRNAEELLALLARYG-VDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPP 212
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 3-197 2.00e-18

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 82.67  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTH-FRSRGQKLYGfidVNAAN--ADVVSQLNALQERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPG 79
Cdd:PRK11148  17 ILQITDTHlFADEHETLLG---VNTWEsyQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGIAPLRKPCVWLPG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  80 NHDDKALFLEYL--HPLCPQ----LGRDAQnmhyavddfatrLLFIDSSRAGTSKGWLTEETIKWLEAQLFDGGDKPATV 153
Cdd:PRK11148  94 NHDFQPAMYSALqdAGISPAkhvlIGEHWQ------------ILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTLV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490219197 154 FMHHPPLPLGNAQMDPIACENGHRLLALVERFPSLTRIFCGHNH 197
Cdd:PRK11148 162 LLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIH 205
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
40-197 4.28e-16

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 75.05  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  40 ERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGNHDDKALfLEYLHPlcpqlgRDAQNMHYAVDDFA-TRLLF 118
Cdd:COG2129   25 EDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPEV-LDALEE------SGVHNLHGRVVEIGgLRIAG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197 119 IDSSRAGTSKGWlTEETIKWLEAQLFDGGDKPATVF-MHHPPLPLGnAQMDPIACENG-HRLLALVERF-PSLtrIFCGH 195
Cdd:COG2129   98 LGGSRPTPFGTP-YEYTEEEIEERLAKLREKDVDILlTHAPPYGTT-LDRVEDGPHVGsKALRELIEEFqPKL--VLHGH 173


                 ..
gi 490219197 196 NH 197
Cdd:COG2129  174 IH 175
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 3-82 1.27e-14

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 69.24  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTHFRSrgqklYGFIDVNAANAdvVSQLNALQerPDAVVVSGDIVNCGRPEEYEVARQILGSLN-YPLYLIPGNH 81
Cdd:cd07400    1 IAHISDLHFGE-----ERKPEVLELNL--LDEINALK--PDLVVVTGDLTQRARPAEFEEAREFLDALEpEPVVVVPGNH 71


                 .
gi 490219197  82 D 82
Cdd:cd07400   72 D 72
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
3-82 3.23e-10

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 59.04  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTHFRSRGQKlygfidvnAANADVVSQLNALQerPDAVVVSGDIVNcGRPEEYEVARQILGSLN--YPLYLIPGN 80
Cdd:COG1408   45 IVQLSDLHLGPFIGG--------ERLERLVEKINALK--PDLVVLTGDLVD-GSVAELEALLELLKKLKapLGVYAVLGN 113


                 ..
gi 490219197  81 HD 82
Cdd:COG1408  114 HD 115
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-94 6.02e-10

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: 57.67  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   3 LAQISDTHFRSRGQKLYgfidvnaaNADVVSQLNALQerPDAVVVSGDIVnCGRPEEYEVARQILGSLN--YPLYLIPGN 80
Cdd:cd07385    4 IVQLSDIHLGPFVGRTR--------LQKVVRKVNELN--PDLIVITGDLV-DGDVSVLRLLASPLSKLKapLGVYFVLGN 72

                         90
                 ....*....|....*...
gi 490219197  81 HD----DKALFLEYLHPL 94
Cdd:cd07385   73 HDyysgDVEVWIAALEKA 90
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-82 8.25e-09

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: 53.04  E-value: 8.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   4 AQISDTHFRSRgqklygfidvnaANADVVSQLNALQERPDAVVVSGDIVNCGR-PEEYEVARQILGSLNYPLYLIPGNHD 82
Cdd:cd00838    1 LVISDIHGNLE------------ALEAVLEAALAKAEKPDLVICLGDLVDYGPdPEEVELKALRLLLAGIPVYVVPGNHD 68
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 6-93 1.26e-08

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 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: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 53.43  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   6 ISDTHFrsrGQKLYGFIDVNAANADVVSQL--NALQERPDAVVVSGDIVNCGRP--EEYEVARQILGSL---NYPLYLIP 78
Cdd:cd00840    5 TADWHL---GYPLYGLSRREEDFFKAFEEIvdLAIEEKVDFVLIAGDLFDSNNPspEALKLAIEGLRRLceaGIPVFVIA 81

                         90
                 ....*....|....*....
gi 490219197  79 GNHDDKALF----LEYLHP 93
Cdd:cd00840   82 GNHDSPARVaiygLPYLRD 100
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 1-99 2.86e-08

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 53.19  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197    1 MLLAQISDTHFrsrGQKLYGFiDVNAANADVVSQLN--ALQERPDAVVVSGDIVNCGRPEEYevARQILGS--LNY---- 72
Cdd:TIGR00619   1 MRILHTSDWHL---GKTLEGV-SRLAEQKAFLDDLLefAKAEQVDALLVAGDVFDTANPPAE--AQELFNAffVNLsdtg 74

                          90       100
                  ....*....|....*....|....*....
gi 490219197   73 --PLYLIPGNHDDKAlFLEYLHPLCPQLG 99
Cdd:TIGR00619  75 irPIVVISGNHDSAQ-RLSAAKKLLAELG 102
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
1-99 4.86e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 52.61  E-value: 4.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   1 MLLAQISDTHFrsrGQKLYGFiDVNAANADVVSQL--NALQERPDAVVVSGDIVNCGRP--EEYEVARQILGSL---NYP 73
Cdd:COG0420    1 MRFLHTADWHL---GKPLHGA-SRREDQLAALDRLvdLAIEEKVDAVLIAGDLFDSANPspEAVRLLAEALRRLseaGIP 76

                         90       100
                 ....*....|....*....|....*.
gi 490219197  74 LYLIPGNHdDKALFLEYLHPLCPQLG 99
Cdd:COG0420   77 VVLIAGNH-DSPSRLSAGSPLLENLG 101
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 4-197 7.35e-08

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: 51.52  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   4 AQISDTHFRSRGQKLYGFIDVNAANADVVSQLNAlQERPDAVVVSGDIVNCGRPEEYEVARQILGSLNyPL--YLIP--- 78
Cdd:cd07383    6 LQFADLHFGEGEWTCWEGCEADLKTVEFIESVLD-EEKPDLVVLTGDLITGENTADDNATSYLDKAVS-PLveRGIPwaa 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  79 --GNHDDkalfleYlhplcpqlgrdaqnmhyavddfatrllfidssragtskGWLTEETIKWLEA-----QLFDGGDKPA 151
Cdd:cd07383   84 tfGNHDG------Y--------------------------------------DWIDPSQVEWFEStsaalKKKYGKNIPS 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490219197 152 TVFMHHPPL----------PLGNAQMDPIAC--ENGHRLLALVERfPSLTRIFCGHNH 197
Cdd:cd07383  120 LAFFHIPLPeyrevwnekgKLGGINREKVCCqkTNSGFFKALVKR-GDVKAVFCGHDH 176
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 6-87 5.73e-07

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


Pssm-ID: 443340  Cd Length: 167  Bit Score: 48.35  E-value: 5.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   6 ISDTHF--------RSRgqklyGFIDVNAANADVVSQLNALQERPDAVVVSGDIVNCGRPEEyevARQILGSLNYPLYLI 77
Cdd:COG4186    5 TSDTHFghaniikfCPR-----PFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSAEE---AREILRRLNGRKHLI 76

                         90
                 ....*....|
gi 490219197  78 PGNHDDKALF 87
Cdd:COG4186   77 RGNHDGKLLL 86
MPP_AQ1575 cd07390
Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes ...
 6-93 9.31e-07

Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. The domain present in members of this family 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: 277336  Cd Length: 170  Bit Score: 47.74  E-value: 9.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   6 ISDTHF---RSRGQKLYGFIDVNAANADVVSQLNALQERPDAVVVSGDIVNCGRPEEyeVARQILGSLNYPLYLIPGNHD 82
Cdd:cd07390    4 TSDTHFghpNVIRYTNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALGTNKAN--EALEILSLLNGHIHLIRGNHD 81

                         90
                 ....*....|.
gi 490219197  83 DKALFLEYLHP 93
Cdd:cd07390   82 KSLLMYRPLFF 92
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-83 3.56e-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: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197    1 MLLAQISDTHFRsrGQKlygfidvnAANADVVSQLNAlQERPDAVVVSGDIVNCGRPEEyEVARQILGSLNY-PLYLIPG 79
Cdd:pfam00149   1 MRILVIGDLHLP--GQL--------DDLLELLKKLLE-EGKPDLVLHAGDLVDRGPPSE-EVLELLERLIKYvPVYLVRG 68


                  ....
gi 490219197   80 NHDD 83
Cdd:pfam00149  69 NHDF 72
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 40-86 4.58e-06

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 46.15  E-value: 4.58e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490219197  40 ERPDAVVVSGDIVNCGRPEEYEVARQILGSLNYPLYLIPGNHDDKAL 86
Cdd:cd07392   22 EEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCDTPEV 68
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 29-198 1.62e-05

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 45.02  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197  29 ADVVSQLNAlQERPDAVVVSGDIVNCGRPEEY-----EVARQILGSLNYPLYLIPGNHDDKALFLEYLHPLCPQLGRDAQ 103
Cdd:cd07396   35 ERAVEEWNR-ESNLAFVVQLGDIIDGYNAKDRskealDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAY 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197 104 NMHYAV-DDFatRLLFIDssrAGTSKGWLTEETIKWLEAQL--FDGGDKPATVFMHHPplplgnaqMDPIACENGH---- 176
Cdd:cd07396  114 YYSFSPgPGF--RFLVLD---FVKFNGGIGEEQLAWLRNELtsADANGEKVIVLSHLP--------IYPEAADPQCllwn 180

                        170       180
                 ....*....|....*....|....
gi 490219197 177 --RLLALVERFPSLTRIFCGHNHS 198
Cdd:cd07396  181 yeEVLAILESYPCVKACFSGHNHE 204
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-91 4.81e-04

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 39.60  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197    1 MLLAQISDTHfrsrgqklygfidVNAANADVVsqLNALQERPDAVVVSGDIVNcgrPEEYEVARQILgslnyPLYLIPGN 80
Cdd:pfam12850   1 MRIGIISDTH-------------DNLALPEAA--LERLKGVVDLIIHAGDIVA---PEVLEELLELA-----PVLAVRGN 57

                          90
                  ....*....|.
gi 490219197   81 HDDKALFLEYL 91
Cdd:pfam12850  58 NDAAAEFATDL 68
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 35-82 4.68e-03

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 37.66  E-value: 4.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 490219197  35 LNALQerPDAVVVSGDIVNcgrpEEYEVARQIlGSLNYPLYLIPGNHD 82
Cdd:cd07397   21 LRLLQ--PDLVLFVGDFGN----ENVQLVRRI-ASLDLPKAVILGNHD 61
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 6-82 5.71e-03

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family 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: 277337  Cd Length: 175  Bit Score: 36.90  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490219197   6 ISDTH------FRSRGqkLYGFIDVNAANADVVSQLnALQERPDAVVVSGDIV-NCGRP---EEYEVARQILGSLNYPLY 75
Cdd:cd07391    3 IADLHlgyeeeLRRQG--INLPRRQKERLLERLDRL-LEELGPDRLVILGDLKhSFGRVsrqERREVPFFRLLAKDVDVI 79


                 ....*..
gi 490219197  76 LIPGNHD 82
Cdd:cd07391   80 LIRGNHD 86
 
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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