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Conserved domains on  [gi|1039732574|ref|XP_017169351|]
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sphingomyelin phosphodiesterase 2 isoform X1 [Mus musculus]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 662)

exonuclease/endonuclease/phosphatase (EEP) family protein may cleave phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 85-294 3.07e-21

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


The actual alignment was detected with superfamily member cd09079:

Pssm-ID: 469791 [Multi-domain]  Cd Length: 259  Bit Score: 92.33  E-value: 3.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  85 QELVFSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHhGDWFCGKSVGL----------LVLRLSGLVLNAYVTHLHA 154
Cdd:cd09079    62 EKLRELGATYYWTWILSHIGYDKYDEGLAILSKRPIAEV-EDFYVSKSQDYtdyksrkilgATIEINGQPIDVYSCHLGW 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 155 EYsrqkdiyfAHRVAQAWELAQFIHHTSKNADVVLLCGDLNMhPKDLGCCLLKEWTglHDAFVETEDFKGSDDGCTMVPK 234
Cdd:cd09079   141 WY--------DEEEPFAYEWSKLEKALAEAGRPVLLMGDFNN-PAGSRGEGYDLIS--SLGLQDTYDLAEEKDGGVTVEK 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039732574 235 NcyVSQQDlgPFPSGIRIDYVLY---KAVSEFHVCCetlkttTGCDPHSdkpFSDHEALMATL 294
Cdd:cd09079   210 A--IDGWR--GNKEAKRIDYIFVnrkVKVKSSRVIF------NGKNPPI---VSDHFGVEVEL 259
 
Name Accession Description Interval E-value
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
 85-294 3.07e-21

Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197313 [Multi-domain]  Cd Length: 259  Bit Score: 92.33  E-value: 3.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  85 QELVFSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHhGDWFCGKSVGL----------LVLRLSGLVLNAYVTHLHA 154
Cdd:cd09079    62 EKLRELGATYYWTWILSHIGYDKYDEGLAILSKRPIAEV-EDFYVSKSQDYtdyksrkilgATIEINGQPIDVYSCHLGW 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 155 EYsrqkdiyfAHRVAQAWELAQFIHHTSKNADVVLLCGDLNMhPKDLGCCLLKEWTglHDAFVETEDFKGSDDGCTMVPK 234
Cdd:cd09079   141 WY--------DEEEPFAYEWSKLEKALAEAGRPVLLMGDFNN-PAGSRGEGYDLIS--SLGLQDTYDLAEEKDGGVTVEK 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039732574 235 NcyVSQQDlgPFPSGIRIDYVLY---KAVSEFHVCCetlkttTGCDPHSdkpFSDHEALMATL 294
Cdd:cd09079   210 A--IDGWR--GNKEAKRIDYIFVnrkVKVKSSRVIF------NGKNPPI---VSDHFGVEVEL 259
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 97-196 3.78e-07

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 49.91  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  97 LCVFSKHPIQEIFQHVYSLNGYPymfhhgdwfcGKSVGLLVLRLSGLVLNAYVTHLHAEYsrqkdiyFAHRVAQAWELAQ 176
Cdd:COG3568    47 NAILSRYPIVSSGTFDLPDPGGE----------PRGALWADVDVPGKPLRVVNTHLDLRS-------AAARRRQARALAE 109

                          90       100
                  ....*....|....*....|
gi 1039732574 177 FIHHTSKNADVVlLCGDLNM 196
Cdd:COG3568   110 LLAELPAGAPVI-LAGDFND 128
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 89-196 4.84e-05

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 43.75  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  89 FSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHHGDWFCGKSVGLLVLRLSglvlnayvthlhaeysRQKDIYFAHRV 168
Cdd:pfam03372  64 GGGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLA----------------PHASPRLARDE 127

                          90       100
                  ....*....|....*....|....*...
gi 1039732574 169 AQAWELAQFIHHTSKNADVVLLCGDLNM 196
Cdd:pfam03372 128 QRADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
 85-294 3.07e-21

Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197313 [Multi-domain]  Cd Length: 259  Bit Score: 92.33  E-value: 3.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  85 QELVFSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHhGDWFCGKSVGL----------LVLRLSGLVLNAYVTHLHA 154
Cdd:cd09079    62 EKLRELGATYYWTWILSHIGYDKYDEGLAILSKRPIAEV-EDFYVSKSQDYtdyksrkilgATIEINGQPIDVYSCHLGW 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 155 EYsrqkdiyfAHRVAQAWELAQFIHHTSKNADVVLLCGDLNMhPKDLGCCLLKEWTglHDAFVETEDFKGSDDGCTMVPK 234
Cdd:cd09079   141 WY--------DEEEPFAYEWSKLEKALAEAGRPVLLMGDFNN-PAGSRGEGYDLIS--SLGLQDTYDLAEEKDGGVTVEK 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039732574 235 NcyVSQQDlgPFPSGIRIDYVLY---KAVSEFHVCCetlkttTGCDPHSdkpFSDHEALMATL 294
Cdd:cd09079   210 A--IDGWR--GNKEAKRIDYIFVnrkVKVKSSRVIF------NGKNPPI---VSDHFGVEVEL 259
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 93-294 2.01e-11

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 64.29  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  93 IGSGLCVFSKHPIQEIFQHVYSLNGYPymfhhgDWFCGKSVGLLVLRLSGLVlNAYV--THLHAEYSRQKDiyFAHRVAQ 170
Cdd:cd09078    81 VDGGVVILSRYPIVEKDQYIFPNGCGA------DCLAAKGVLYAKINKGGTK-VYHVfgTHLQASDGSCLD--RAVRQKQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 171 AWELAQFIH--HTSKNaDVVLLCGDLN---MHPKDLgccLLKEWTGLHDAFVETEDFKG----SDDGCTmvpkncYVSQQ 241
Cdd:cd09078   152 LDELRAFIEekNIPDN-EPVIIAGDFNvdkRSSRDE---YDDMLEQLHDYNAPEPITAGetplTWDPGT------NLLAK 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039732574 242 DLGPFPSGIRIDYVLY----KAVSEFHVCCETLKTTTGCDPHSDKP--FSDHEALMATL 294
Cdd:cd09078   222 YNYPGGGGERLDYILYsndhLQPSSWSNEVEVPKSPTWSVTNGYTFadLSDHYPVSATF 280
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 97-196 3.78e-07

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 49.91  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  97 LCVFSKHPIQEIFQHVYSLNGYPymfhhgdwfcGKSVGLLVLRLSGLVLNAYVTHLHAEYsrqkdiyFAHRVAQAWELAQ 176
Cdd:COG3568    47 NAILSRYPIVSSGTFDLPDPGGE----------PRGALWADVDVPGKPLRVVNTHLDLRS-------AAARRRQARALAE 109

                          90       100
                  ....*....|....*....|
gi 1039732574 177 FIHHTSKNADVVlLCGDLNM 196
Cdd:COG3568   110 LLAELPAGAPVI-LAGDFND 128
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 132-294 2.02e-06

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 48.75  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 132 SVGLLVLRLSGLVLNAYVTHL--HAEYSRQKdiyfahrvaQAWELAQFIHHTSKNADVVLlCGDLNMHPKDLGCCLLKEw 209
Cdd:cd09083   115 TWARFKDKKTGKEFYVFNTHLdhVGEEAREE---------SAKLILERIKEIAGDLPVIL-TGDFNAEPDSEPYKTLTS- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 210 TGLHDAFVETEDFKGSDDGcTMvpkncyvsqQDLGPFPSGIRIDYVLYKavSEFHVC-CETLKTTTGcdphsDKPFSDHE 288
Cdd:cd09083   184 GGLKDARDTAATTDGGPEG-TF---------HGFKGPPGGSRIDYIFVS--PGVKVLsYEILTDRYD-----GRYPSDHF 246


                  ....*.
gi 1039732574 289 ALMATL 294
Cdd:cd09083   247 PVVADL 252
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 150-294 2.66e-06

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 48.49  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 150 THL-----HAEYsrqkdiyfahRVAQAWELAQFIHHTSKNADVVLlCGDLNMHPKDLGCCLLKEwtGLHDAFVETEDFKg 224
Cdd:cd09080   116 THLeslksHSSE----------RTAQLEEIAKKLKKPPGAANVIL-GGDFNLRDKEDDTGGLPN--GFVDAWEELGPPG- 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039732574 225 sDDGCTM-VPKNCYVSQQDLGPFpsgIRIDYVLYK----AVSEFHvccetLKTTTGCDPHSDKPF-SDHEALMATL 294
Cdd:cd09080   182 -EPGYTWdTQKNPMLRKGEAGPR---KRFDRVLLRgsdlKPKSIE-----LIGTEPIPGDEEGLFpSDHFGLLAEL 248
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 89-196 4.84e-05

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 43.75  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  89 FSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHHGDWFCGKSVGLLVLRLSglvlnayvthlhaeysRQKDIYFAHRV 168
Cdd:pfam03372  64 GGGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLA----------------PHASPRLARDE 127

                          90       100
                  ....*....|....*....|....*...
gi 1039732574 169 AQAWELAQFIHHTSKNADVVLLCGDLNM 196
Cdd:pfam03372 128 QRADLLLLLLALLAPRSEPVILAGDFNA 155
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 90-294 1.92e-03

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 39.59  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  90 SGMIGSGLCVFSKHPI---QEIFQHVYSLNGYpymfhhgdwFC-----GKSVGLLVLRLSGLVLNAYVTHLHAEYSRQK- 160
Cdd:cd09084    65 SDSGGTGLAIFSKYPIlnsGSIDFPNTNNNAI---------FAdirvgGDTIRVYNVHLESFRITPSDKELYKEEKKAKe 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 161 ---DIY------FAHRVAQAWELAQFIHHTSKNadvVLLCGDLNMHPKDLGCCLLKEwtGLHDAFVEtedfKGSDDGctm 231
Cdd:cd09084   136 lsrNLLrklaeaFKRRAAQADLLAADIAASPYP---VIVCGDFNDTPASYVYRTLKK--GLTDAFVE----AGSGFG--- 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039732574 232 vpkncyVSQQDLGPFpsgIRIDYVLYKAVSEFHvCCETLktttgcdphsDKPFSDHEALMATL 294
Cdd:cd09084   204 ------YTFNGLFFP---LRIDYILTSKGFKVL-RYRVD----------PGKYSDHYPIVATL 246
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 93-294 2.47e-03

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 39.39  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574  93 IGSGLCVFSKHPIQEIFQhVYSLNGYPYMFHHGdwfcgksvGLLVLRLSGLVLNAYV--THLHAEYSRQKDiyfahRVAQ 170
Cdd:cd08372    65 GYEGVAILSKTPKFKIVE-KHQYKFGEGDSGER--------RAVVVKFDVHDKELCVvnAHLQAGGTRADV-----RDAQ 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732574 171 AWELAQFI-HHTSKNADVVLLCGDLNMHPKDLGCCLLKEW-TGLHD-AFVETEDFKGSDDGCTMVPKNCYVsqqdlgpfp 247
Cdd:cd08372   131 LKEVLEFLkRLRQPNSAPVVICGDFNVRPSEVDSENPSSMlRLFVAlNLVDSFETLPHAYTFDTYMHNVKS--------- 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039732574 248 sgiRIDYVLYKAvSEFHVCCETLKTTtgcDPHSDKPFSDHEALMATL 294
Cdd:cd08372   202 ---RLDYIFVSK-SLLPSVKSSKILS---DAARARIPSDHYPIEVTL 241
 
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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