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Conserved domains on  [gi|6969227|emb|CAA16976|]
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GPI-remodelling mannose-ethanolamine phosphate phosphodiesterase Ted1 [Schizosaccharomyces pombe]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10169247)

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_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 54-340 2.58e-81

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: 248.56  E-value: 2.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   54 MGVADPQIEGNHKIEANGFfKGTLDLWGNDLFLRHLVHMNQFWGQPDAMILLGDLVSFQHLDNEEFNKRAKRLKKITGAK 133
Cdd:cd08164   1 LALGDPQIEGDWPITNYGF-KGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLFSSQWITDEEFEKRADRYKKRIFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  134 NFWQVGNSSLPARTFENGNIPVWTIAGNHDIGYGCESSDAQISKWEQAMgpvnwvshfnvskfpvrviginslslddvqf 213
Cdd:cd08164  80 SDWQVGNISLAARTFENGDILLINIAGNHDVGYAGESTEARISRFEQLF------------------------------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  214 ydanpsdiinsksfsslgilalskeardawqflfdialepsiptILFTHVPLYKpanvcvdeprivrqldfrvksqnhls 293
Cdd:cd08164 129 --------------------------------------------ILLTHVPLYK-------------------------- 138

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6969227  294 ynttmkiFELIPSIKLVLSGHDHMGCDYEHP---------------NGAIEHTLPSAMGYFG 340
Cdd:cd08164 139 -------FFLEGKPGLILTGHDHEGCDYEYPsnpsvtwatsleesgNGVREYTVRSMMGEFG 193
 
Name Accession Description Interval E-value
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 54-340 2.58e-81

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: 248.56  E-value: 2.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   54 MGVADPQIEGNHKIEANGFfKGTLDLWGNDLFLRHLVHMNQFWGQPDAMILLGDLVSFQHLDNEEFNKRAKRLKKITGAK 133
Cdd:cd08164   1 LALGDPQIEGDWPITNYGF-KGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLFSSQWITDEEFEKRADRYKKRIFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  134 NFWQVGNSSLPARTFENGNIPVWTIAGNHDIGYGCESSDAQISKWEQAMgpvnwvshfnvskfpvrviginslslddvqf 213
Cdd:cd08164  80 SDWQVGNISLAARTFENGDILLINIAGNHDVGYAGESTEARISRFEQLF------------------------------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  214 ydanpsdiinsksfsslgilalskeardawqflfdialepsiptILFTHVPLYKpanvcvdeprivrqldfrvksqnhls 293
Cdd:cd08164 129 --------------------------------------------ILLTHVPLYK-------------------------- 138

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6969227  294 ynttmkiFELIPSIKLVLSGHDHMGCDYEHP---------------NGAIEHTLPSAMGYFG 340
Cdd:cd08164 139 -------FFLEGKPGLILTGHDHEGCDYEYPsnpsvtwatsleesgNGVREYTVRSMMGEFG 193
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
86-356 6.36e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 53.16  E-value: 6.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   86 LRHLV-HMNQfwGQPDAMILLGDLVsfQHLDNEEFNKRAKRLKKItgaknfwqvgnsslpartfengNIPVWTIAGNHDI 164
Cdd:COG1409  23 LAAALaDINA--PRPDFVVVTGDLT--DDGEPEEYAAAREILARL----------------------GVPVYVVPGNHDI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  165 gygcesSDAQISKWEQAMGPVNWVS---HFNVSkfPVRVIGINSLSLDDVqfYDANPSDIINsksfsslgilALSKEARD 241
Cdd:COG1409  77 ------RAAMAEAYREYFGDLPPGGlyySFDYG--GVRFIGLDSNVPGRS--SGELGPEQLA----------WLEEELAA 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  242 AwqflfdialePSIPTILFTHVPLYkPANVCVDEPRIVRQLDFRvksqnhlsynttmKIFELIPsIKLVLSGHDHMGcDY 321
Cdd:COG1409 137 A----------PAKPVIVFLHHPPY-STGSGSDRIGLRNAEELL-------------ALLARYG-VDLVLSGHVHRY-ER 190

                       250       260       270
                ....*....|....*....|....*....|....*
gi 6969227  322 EHPNGAIEHTLPSAMGYFGGNIGFVKLIATNDVLT 356
Cdd:COG1409 191 TRRDGVPYIVAGSTGGQVRLPPGYRVIEVDGDGLT 225
 
Name Accession Description Interval E-value
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 54-340 2.58e-81

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: 248.56  E-value: 2.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   54 MGVADPQIEGNHKIEANGFfKGTLDLWGNDLFLRHLVHMNQFWGQPDAMILLGDLVSFQHLDNEEFNKRAKRLKKITGAK 133
Cdd:cd08164   1 LALGDPQIEGDWPITNYGF-KGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLFSSQWITDEEFEKRADRYKKRIFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  134 NFWQVGNSSLPARTFENGNIPVWTIAGNHDIGYGCESSDAQISKWEQAMgpvnwvshfnvskfpvrviginslslddvqf 213
Cdd:cd08164  80 SDWQVGNISLAARTFENGDILLINIAGNHDVGYAGESTEARISRFEQLF------------------------------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  214 ydanpsdiinsksfsslgilalskeardawqflfdialepsiptILFTHVPLYKpanvcvdeprivrqldfrvksqnhls 293
Cdd:cd08164 129 --------------------------------------------ILLTHVPLYK-------------------------- 138

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6969227  294 ynttmkiFELIPSIKLVLSGHDHMGCDYEHP---------------NGAIEHTLPSAMGYFG 340
Cdd:cd08164 139 -------FFLEGKPGLILTGHDHEGCDYEYPsnpsvtwatsleesgNGVREYTVRSMMGEFG 193
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 56-340 4.04e-19

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: 84.32  E-value: 4.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   56 VADPQIEGNHKIEANGFFKGTLDLWGNDLFLRHLVHMNQFWGQPDAMILLGDLVSFQH-LDNEEFNKRAKRLKKITGAKN 134
Cdd:cd07384   3 IADPQILDETSYPPRPKPALRLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRiLDSEEWKEYLHRFQKIFFLKS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  135 fwqvgnsslparTFENGNIPVWTIAGNHDIGYGcessdaqiskweqamgpvnwvshfnvskfpvrviginslslDDVQFY 214
Cdd:cd07384  83 ------------PGSLGSIPVIFIPGNHDIGYG-----------------------------------------GEAVFP 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  215 danpsdiinsksfsslgilalskEARDAWQFLFdialepsiptILFTHVPLYkpanvcvdeprivrqldfrvksqnhlsy 294
Cdd:cd07384 110 -----------------------EKVDRFEKYF----------ILLTHIPLY---------------------------- 128

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 6969227  295 nttmKIFELIPSIkLVLSGHDHMGCDYEH---PNGAIEHTLPSAMGYFG 340
Cdd:cd07384 129 ----RLLDSIKPV-LILSGHDHDYCEVVHkssPGSVKEITVKSFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 56-337 5.94e-17

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: 80.14  E-value: 5.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   56 VADPQIEGNHKIEANGFFKGTLDLWGNDLFLR-HLVHMnQFWGQPDAMILLGDLV-SFQHLDNEEFNKRAKRLKKITGAK 133
Cdd:cd08163   3 VADPQLVDDHTYPGRPWILNTLTEHFVDQYLRrNWRYL-QKQLKPDSTFFLGDLFdGGREWADEYWKKEYFRFNRIFDPK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  134 nfwqvgnssLPARTfengnipVWTIAGNHDIGYGCESSDAQISKWEQAMGPVNwvshfnvskfpvRVIGINS---LSLDD 210
Cdd:cd08163  82 ---------PLRKM-------IESLPGNHDIGFGNGVKLPVRQRFESYFGPTS------------RVIDVGNhtfVIVDT 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  211 VQFYDANPSDIinsksfsslgilalsKEARDAWQFLFDIALEPSIPTILFTHVPLYKPANVCVDEpriVRQLDFRVKSQN 290
Cdd:cd08163 134 ISLSNNDNPQV---------------YQPAREFLHSFEAMKVNSKPRILLTHVPLYRPPNTSCGP---LREKKTPLPYGY 195

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6969227  291 HLSYNTTMKIfELIPSIK------LVLSGHDHMGCDYEHP-------NGAIEHTLPS---AMG 337
Cdd:cd08163 196 GYQYQNVLEP-SLSESILkainpvAAFSGDDHDYCEVVHEyqfdgkeGSAREITVKSismAMG 257
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
86-356 6.36e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 53.16  E-value: 6.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   86 LRHLV-HMNQfwGQPDAMILLGDLVsfQHLDNEEFNKRAKRLKKItgaknfwqvgnsslpartfengNIPVWTIAGNHDI 164
Cdd:COG1409  23 LAAALaDINA--PRPDFVVVTGDLT--DDGEPEEYAAAREILARL----------------------GVPVYVVPGNHDI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  165 gygcesSDAQISKWEQAMGPVNWVS---HFNVSkfPVRVIGINSLSLDDVqfYDANPSDIINsksfsslgilALSKEARD 241
Cdd:COG1409  77 ------RAAMAEAYREYFGDLPPGGlyySFDYG--GVRFIGLDSNVPGRS--SGELGPEQLA----------WLEEELAA 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227  242 AwqflfdialePSIPTILFTHVPLYkPANVCVDEPRIVRQLDFRvksqnhlsynttmKIFELIPsIKLVLSGHDHMGcDY 321
Cdd:COG1409 137 A----------PAKPVIVFLHHPPY-STGSGSDRIGLRNAEELL-------------ALLARYG-VDLVLSGHVHRY-ER 190

                       250       260       270
                ....*....|....*....|....*....|....*
gi 6969227  322 EHPNGAIEHTLPSAMGYFGGNIGFVKLIATNDVLT 356
Cdd:COG1409 191 TRRDGVPYIVAGSTGGQVRLPPGYRVIEVDGDGLT 225
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 56-138 1.92e-03

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: 39.34  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6969227   56 VADPQIEGNhkiEANGFFKGTLDLWGNDLFLRHlVHMNQFWG-QPDAMILLGDLVSFQHLDNE-EFNKRAKRLKKITGAK 133
Cdd:cd08166   3 VADPQILGY---ENEKFGLGEISRWDSDRYLAK-TYERALWYfKPDIVIFLGDLFDEGIIANDdEYYSYVQRFIGIFPLK 78


                ....*
gi 6969227  134 NFWQV 138
Cdd:cd08166  79 RGKNA 83
 
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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