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Conserved domains on  [gi|442626737|ref|NP_001260231|]
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Post-GPI attachment to proteins 5, isoform C [Drosophila melanogaster]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10169250)

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

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List of domain hits

 Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 48-301 2.11e-76

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 232.74  E-value: 2.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLLGPHRGHWLDKLYREWHMTRAFQAASRLFQPDVVFVLGDLFDEGDMVSDKQFQEYVWRYLKMFHLPPGIPLI 127
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 128 SVAGNHDVGFHYKMHPFFMSRFESYLnnssvnlytikqihfvvinsmamegdgcmfctqaedqlknisrtlycmkyplea 207
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 208 ecartrrhpysqpILLQHFPTYRisdtmceehdapyieafrerfhvlskdatdmLGELLKPRLAFAGHSHHFCHSVNRLG 287
Cdd:cd08165  107 -------------ILLQHYPLYR-------------------------------LLQWLKPRLVLSGHTHSACEVLHYGG 142

                        250
                 ....*....|....
gi 442626737 288 IDEYTVASFSWRNK 301
Cdd:cd08165  143 IPEISVPSFSWRNR 156
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 48-301 2.11e-76

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 232.74  E-value: 2.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLLGPHRGHWLDKLYREWHMTRAFQAASRLFQPDVVFVLGDLFDEGDMVSDKQFQEYVWRYLKMFHLPPGIPLI 127
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 128 SVAGNHDVGFHYKMHPFFMSRFESYLnnssvnlytikqihfvvinsmamegdgcmfctqaedqlknisrtlycmkyplea 207
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 208 ecartrrhpysqpILLQHFPTYRisdtmceehdapyieafrerfhvlskdatdmLGELLKPRLAFAGHSHHFCHSVNRLG 287
Cdd:cd08165  107 -------------ILLQHYPLYR-------------------------------LLQWLKPRLVLSGHTHSACEVLHYGG 142

                        250
                 ....*....|....
gi 442626737 288 IDEYTVASFSWRNK 301
Cdd:cd08165  143 IPEISVPSFSWRNR 156
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
45-318 1.10e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.50  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  45 LRAMILADPHLLGPHRGHWLDKLyrewhmtRAFQAASRLFQPDVVFVLGDLFDEGdmvSDKQFQEYVwRYLKMFhlppGI 124
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVL-------AAALADINAPRPDFVVVTGDLTDDG---EPEEYAAAR-EILARL----GV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 125 PLISVAGNHDVGFHykMHPFFMSRFESYLNNSSVNLYTIKQIHFVVINS-MAMEGDGCMfctqAEDQLKNisrtlycmky 203
Cdd:COG1409   66 PVYVVPGNHDIRAA--MAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSnVPGRSSGEL----GPEQLAW---------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 204 pLEAECARTRRHPysqPILLQHFPTYRISDTMcEEHDAPYIEAFRERFhvlskdatdmlgELLKPRLAFAGHSHHFCHSV 283
Cdd:COG1409  130 -LEEELAAAPAKP---VIVFLHHPPYSTGSGS-DRIGLRNAEELLALL------------ARYGVDLVLSGHVHRYERTR 192

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442626737 284 NRlGIDEYTVASFSWRNKVNPSFMLATITPDDYVV 318
Cdd:COG1409  193 RD-GVPYIVAGSTGGQVRLPPGYRVIEVDGDGLTV 226
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 45-170 2.58e-05

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: 42.97  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737   45 LRAMILADPHLLGPHRGhwldklyrewhMTRAFQAASRLFQPDVVFVLGDLFDEGDmvSDKQFQEYvwrylkMFHLPPGI 124
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------LLELLKKLLEEGKPDLVLHAGDLVDRGP--PSEEVLEL------LERLIKYV 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 442626737  125 PLISVAGNHDVGFHYKMHPFFMSRFESYLNNSSVNLYTIKQIHFVV 170
Cdd:pfam00149  62 PVYLVRGNHDFDYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 48-301 2.11e-76

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 232.74  E-value: 2.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLLGPHRGHWLDKLYREWHMTRAFQAASRLFQPDVVFVLGDLFDEGDMVSDKQFQEYVWRYLKMFHLPPGIPLI 127
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 128 SVAGNHDVGFHYKMHPFFMSRFESYLnnssvnlytikqihfvvinsmamegdgcmfctqaedqlknisrtlycmkyplea 207
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 208 ecartrrhpysqpILLQHFPTYRisdtmceehdapyieafrerfhvlskdatdmLGELLKPRLAFAGHSHHFCHSVNRLG 287
Cdd:cd08165  107 -------------ILLQHYPLYR-------------------------------LLQWLKPRLVLSGHTHSACEVLHYGG 142

                        250
                 ....*....|....
gi 442626737 288 IDEYTVASFSWRNK 301
Cdd:cd08165  143 IPEISVPSFSWRNR 156
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 48-300 2.04e-35

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 127.46  E-value: 2.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLLGPHRGHW-------LDKLYREWHMTRAFQAASRLFQPDVVFVLGDLFDEGDMVSDKQFQEYVWRYLKMFHL 120
Cdd:cd07384    1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 121 PPG-----IPLISVAGNHDVGFHYKM-HPFFMSRFESYLnnssvnlytikqihfvvinsmamegdgcmfctqaedqlkni 194
Cdd:cd07384   81 KSPgslgsIPVIFIPGNHDIGYGGEAvFPEKVDRFEKYF----------------------------------------- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 195 srtlycmkypleaecartrrhpysqpILLQHFPTYRISDTmceehdapyieafrerfhvlskdatdmlgelLKPRLAFAG 274
Cdd:cd07384  120 --------------------------ILLTHIPLYRLLDS-------------------------------IKPVLILSG 142

                        250       260
                 ....*....|....*....|....*....
gi 442626737 275 HSHHFC---HSVNRLGIDEYTVASFSWRN 300
Cdd:cd07384  143 HDHDYCevvHKSSPGSVKEITVKSFSWRM 171
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 49-298 7.19e-21

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 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: 277370  Cd Length: 257  Bit Score: 90.54  E-value: 7.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  49 ILADPHLLGPH----RgHW----LDKLYREWHMTRAFQAASRLFQPDVVFVLGDLFDEGDMVSDKQFQEYVWRYLKMFHL 120
Cdd:cd08163    2 LVADPQLVDDHtypgR-PWilntLTEHFVDQYLRRNWRYLQKQLKPDSTFFLGDLFDGGREWADEYWKKEYFRFNRIFDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 121 PPGIPLI-SVAGNHDVGFHYKMHPFFMSRFESYLNNSSVNLyTIKQIHFVVINSMAMEGdgcmfctqaedqlknisrtly 199
Cdd:cd08163   81 KPLRKMIeSLPGNHDIGFGNGVKLPVRQRFESYFGPTSRVI-DVGNHTFVIVDTISLSN--------------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 200 cMKYPLEAECARTRRHPYSQP-------ILLQHFPTYRISDTMC---EEHDAPYIEAFRERFH-VLSKDATDMLGELLKP 268
Cdd:cd08163  139 -NDNPQVYQPAREFLHSFEAMkvnskprILLTHVPLYRPPNTSCgplREKKTPLPYGYGYQYQnVLEPSLSESILKAINP 217

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442626737 269 RLAFAGHSHHFCHSVNRL-------GIDEYTVASFSW 298
Cdd:cd08163  218 VAAFSGDDHDYCEVVHEYqfdgkegSAREITVKSISM 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
45-318 1.10e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.50  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  45 LRAMILADPHLLGPHRGHWLDKLyrewhmtRAFQAASRLFQPDVVFVLGDLFDEGdmvSDKQFQEYVwRYLKMFhlppGI 124
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVL-------AAALADINAPRPDFVVVTGDLTDDG---EPEEYAAAR-EILARL----GV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 125 PLISVAGNHDVGFHykMHPFFMSRFESYLNNSSVNLYTIKQIHFVVINS-MAMEGDGCMfctqAEDQLKNisrtlycmky 203
Cdd:COG1409   66 PVYVVPGNHDIRAA--MAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSnVPGRSSGEL----GPEQLAW---------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 204 pLEAECARTRRHPysqPILLQHFPTYRISDTMcEEHDAPYIEAFRERFhvlskdatdmlgELLKPRLAFAGHSHHFCHSV 283
Cdd:COG1409  130 -LEEELAAAPAKP---VIVFLHHPPYSTGSGS-DRIGLRNAEELLALL------------ARYGVDLVLSGHVHRYERTR 192

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442626737 284 NRlGIDEYTVASFSWRNKVNPSFMLATITPDDYVV 318
Cdd:COG1409  193 RD-GVPYIVAGSTGGQVRLPPGYRVIEVDGDGLTV 226
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 48-136 1.33e-12

uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; A functionally uncharacterized subgroup related to the metallophosphatase domain of Saccharomyces cerevisiae Cdc1, S. cerevisiae Ted1 and human MPPE1. Cdc1 is an endoplasmic reticulum-localized transmembrane lipid phosphatase and is a subunit of DNA polymerase delta. TED1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), acts together with Emp24p and Erv25p in cargo exit from the ER. The MPPE1 gene is a candidate susceptibility gene for Bipolar disorder. Proteins in this uncharacterized subgroup 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: 277373  Cd Length: 195  Bit Score: 65.92  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLLGPHRGHWLDKLYREW----HMTRAFQAASRLFQPDVVFVLGDLFDEGDMVSDKQFQEYVWRYLKMFHLPPG 123
Cdd:cd08166    1 LLVADPQILGYENEKFGLGEISRWdsdrYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                         90
                 ....*....|...
gi 442626737 124 IPLISVAGNHDVG 136
Cdd:cd08166   81 KNAIYIPGDNDIG 93
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 48-151 4.56e-08

Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces cerevisiae Ted1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1) is a metallophosphatase domain-containing protein which acts together with Emp24p and Erv25p in cargo exit from the ER. Ted1 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: 277371  Cd Length: 193  Bit Score: 52.49  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLLGPHR------GHWLDKLYREWHMTRAFQAASRLFQPDVVFVLGDLFDEgDMVSDKQFQEYVWRYLKMF--- 118
Cdd:cd08164    1 LALGDPQIEGDWPitnygfKGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLFSS-QWITDEEFEKRADRYKKRIfgr 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 442626737 119 -------------HLPPG-IPLISVAGNHDVGFHYKMHPFFMSRFES 151
Cdd:cd08164   80 sdwqvgnislaarTFENGdILLINIAGNHDVGYAGESTEARISRFEQ 126
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
46-278 5.49e-07

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 49.63  E-value: 5.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  46 RAMILADPHLlgphrghwldklyrEWHMTRAFQAASRLFQPDVVFVLGDLFDEGdmvSDKQFQEYVwRYLKMFhlppGIP 125
Cdd:COG2129    1 KILAVSDLHG--------------NFDLLEKLLELARAEDADLVILAGDLTDFG---TAEEAREVL-EELAAL----GVP 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 126 LISVAGNHDvgfhykmHPFFMSRFES----YLNNSSVNLYTIKqIHFVvinsmameGDGC--MFCTQAEDQLKNISRTLy 199
Cdd:COG2129   59 VLAVPGNHD-------DPEVLDALEEsgvhNLHGRVVEIGGLR-IAGL--------GGSRptPFGTPYEYTEEEIEERL- 121

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626737 200 cmkypleAECARTRRHpysqpILLQHFPTYRISdtmceehdapyIEAFRERFHVLSKDATDMLgELLKPRLAFAGHSHH 278
Cdd:COG2129  122 -------AKLREKDVD-----ILLTHAPPYGTT-----------LDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHE 176
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 42-277 6.72e-07

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 50.01  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  42 DDPLRAMILADPHL------LGPHRGHWLDklyREWHMTR-AFQAASRLF-QPDVVFVLGDLFDegDMVSDKQFQEYVWR 113
Cdd:cd07395    2 KGPFYFIQGADPQLglikqnNIGNGGDEWD---KEIELTEqAVQAINKLNpKPKFVVVCGDLVH--AMPGEEFREQQVSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 114 YLKMF-HLPPGIPLISVAGNHDVGfhYKMHPFFMSRF-----ESYLNnssvnlYTIKQIHFVVINSMAMEGDGcMFCTQA 187
Cdd:cd07395   77 LKDVLsKLDPDIPLVCVCGNHDVG--NTPTPETIQRYrddfgDDYFS------FWVGGVFFIVLNSQLFKDPS-KVPELA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 188 EDQLKnisrtlycmkyPLEAECARTRRHPYSQPILLQHFPtyrisdtmceehdaPYIEAFRER---FHVLSKDATDMLGE 264
Cdd:cd07395  148 SAQDQ-----------WLEEQLQIARESDAKHVVVFQHIP--------------LFLEDPDEEddyFNIPKSVRRELLDK 202

                        250
                 ....*....|....*
gi 442626737 265 LLKPRL--AFAGHSH 277
Cdd:cd07395  203 FKKAGVkaVFSGHYH 217
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 45-170 2.58e-05

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: 42.97  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737   45 LRAMILADPHLLGPHRGhwldklyrewhMTRAFQAASRLFQPDVVFVLGDLFDEGDmvSDKQFQEYvwrylkMFHLPPGI 124
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------LLELLKKLLEEGKPDLVLHAGDLVDRGP--PSEEVLEL------LERLIKYV 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 442626737  125 PLISVAGNHDVGFHYKMHPFFMSRFESYLNNSSVNLYTIKQIHFVV 170
Cdd:pfam00149  62 PVYLVRGNHDFDYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
43-161 2.65e-05

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 45.17  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  43 DPLRAMILADPHLlGPHrghwldklYREWHMTRAFQAASRLfQPDVVFVLGDLFDEGDMVSDKqfqeyVWRYLKMFHLPP 122
Cdd:COG1408   41 DGLRIVQLSDLHL-GPF--------IGGERLERLVEKINAL-KPDLVVLTGDLVDGSVAELEA-----LLELLKKLKAPL 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442626737 123 GIplISVAGNHDvgfHYKMHPFFMSRFESY----LNNSSVNLY 161
Cdd:COG1408  106 GV--YAVLGNHD---YYAGLEELRAALEEAgvrvLRNEAVTLE 143
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 78-139 3.60e-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: 3.60e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626737  78 QAASRLFQPDVVFVLGDLFDEGdmvSDKQFQEYVWRYLKMFhlppGIPLISVAGNHDVGF-HY 139
Cdd:cd00838   19 AALAKAEKPDLVICLGDLVDYG---PDPEEVELKALRLLLA----GIPVYVVPGNHDILVtHG 74
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 44-170 9.14e-05

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: 43.42  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  44 PLRAMILADPHLlGPHRG-HWLDKLYREwhmtrafqaaSRLFQPDVVFVLGDLFDEgdmvSDKQFQEYVwRYLKMFHLPP 122
Cdd:cd07385    1 GLRIVQLSDIHL-GPFVGrTRLQKVVRK----------VNELNPDLIVITGDLVDG----DVSVLRLLA-SPLSKLKAPL 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442626737 123 GIplISVAGNHDvgfhYKMHPF--FMSRFESY----LNNSSVNLYTIKQIHFVV 170
Cdd:cd07385   65 GV--YFVLGNHD----YYSGDVevWIAALEKAgitvLRNESVELSRDGATIGLA 112
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 124-277 3.32e-04

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 41.90  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 124 IPLISVAGNHDVGF---HYKMHPFFMSRFESYLNNSSVNL----YTIKQIHFVVINSMAMEGDGcmfcTQAEDQLKNisr 196
Cdd:cd00839   69 VPYMVAPGNHEADYngsTSKIKFFMPGRGMPPSPSGSTENlwysFDVGPVHFISLSTETDFLKG----DNISPQYDW--- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737 197 tlycmkypLEAECARTRRHPYSQPILLQHFPTYrisdtmC-EEHDAPYIEAFRERFHV---LSKDATDmlgellkprLAF 272
Cdd:cd00839  142 --------LEADLAKVDRSRTPWIIVMGHRPMY------CsNDDDADCIEGEKMREALedlFYKYGVD---------LVL 198


                 ....*
gi 442626737 273 AGHSH 277
Cdd:cd00839  199 SGHVH 203
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 85-134 6.23e-04

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: 40.33  E-value: 6.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442626737  85 QPDVVFVLGDLFDEGD--MVSDKQFQEYVWRYLKmfhlpPGIPLISVAGNHD 134
Cdd:cd00840   39 KVDFVLIAGDLFDSNNpsPEALKLAIEGLRRLCE-----AGIPVFVIAGNHD 85
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
51-184 1.35e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 39.90  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  51 ADPHLlgphrghwlDKLYREWHMTRAFQAA-SRLF------QPDVVFVLGDLFDeGDMVSDKQFQEYVWRYLKMFHLppG 123
Cdd:COG0420    7 ADWHL---------GKPLHGASRREDQLAAlDRLVdlaieeKVDAVLIAGDLFD-SANPSPEAVRLLAEALRRLSEA--G 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626737 124 IPLISVAGNHDvgfhykmHPFFMSRFESYLNNSSVNLYTIKQIHFVVINSmameGDGCMFC 184
Cdd:COG0420   75 IPVVLIAGNHD-------SPSRLSAGSPLLENLGVHVFGSVEPEPVELED----GLGVAVY 124
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 48-145 5.69e-03

Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF 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: 277343 [Multi-domain]  Cd Length: 217  Bit Score: 37.72  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626737  48 MILADPHLL--GPHRGHWLDKLYREWhmtrafqaasrLFQPDVVFVLGDLFD--EGDMVS-DKQFQEYVWRYLKMFHLpp 122
Cdd:cd07398    1 LFISDLHLGlrGCRADRLLDFLLVEE-----------LDEADALYLLGDIFDlwIGDDSVvWPGAHRALARLLRLADR-- 67

                         90       100
                 ....*....|....*....|...
gi 442626737 123 GIPLISVAGNHDvgFHykMHPFF 145
Cdd:cd07398   68 GTEVIYVPGNHD--FL--LGRFF 86
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 85-144 7.53e-03

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: 36.50  E-value: 7.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626737  85 QPDVVFVLGDLFDEGDmvsDKQFQEyVWRYLKMfhLPPGiPLISVAGNHD--VGFHykmHPF 144
Cdd:cd07400   30 KPDLVVVTGDLTQRAR---PAEFEE-AREFLDA--LEPE-PVVVVPGNHDaiVALH---HPL 81
 
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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