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Conserved domains on  [gi|488192435|ref|WP_002263643|]
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glycerophosphodiester phosphodiesterase family protein [Streptococcus mutans]

Protein Classification

PI-PLC domain-containing protein( domain architecture ID 49489)

PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 23-169 2.36e-55

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


The actual alignment was detected with superfamily member cd08579:

Pssm-ID: 472694 [Multi-domain]  Cd Length: 220  Bit Score: 173.89  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  23 QITVSENGYSTKMTSFDDYLTKANQLEQKLLIEIKTSSQDSKKIMAHFLNKYAKPI---KHQIHSLDYHLIDKVKKYDKS 99
Cdd:cd08579   70 KLTIGENGHGAKIPSLDEYLALAKGLKQKLLIELKPHGHDSPDLVEKFVKLYKQNLienQHQVHSLDYRVIEKVKKLDPK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488192435 100 LVAYFILPY-KSIFSRTKANGYTMEYFSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDYL 169
Cdd:cd08579  150 IKTGYILPFnIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
 
Name Accession Description Interval E-value
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 23-169 2.36e-55

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial glycerophosphodiester phosphodiesterases. In addition to a C-terminal GDPD domain, most members in this family have an N-terminus that functions as a membrane anchor.


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 173.89  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  23 QITVSENGYSTKMTSFDDYLTKANQLEQKLLIEIKTSSQDSKKIMAHFLNKYAKPI---KHQIHSLDYHLIDKVKKYDKS 99
Cdd:cd08579   70 KLTIGENGHGAKIPSLDEYLALAKGLKQKLLIELKPHGHDSPDLVEKFVKLYKQNLienQHQVHSLDYRVIEKVKKLDPK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488192435 100 LVAYFILPY-KSIFSRTKANGYTMEYFSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDYL 169
Cdd:cd08579  150 IKTGYILPFnIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
22-168 1.47e-15

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 71.44  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  22 LQITVSENGYSTKMTSFDDYLTKAnQLEQKLLIEIKTSSQDSKKI---MAHFLNKYAKPIKHQIHSLDYHLIDKVKKYDK 98
Cdd:COG0584   75 LDAGSGPDFAGERIPTLEEVLELV-PGDVGLNIEIKSPPAAEPDLaeaVAALLKRYGLEDRVIVSSFDPEALRRLRELAP 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488192435  99 S-----LVAYFILPYKSIFSRTKANGYTMEYFSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:COG0584  154 DvplglLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDR 228
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 141-170 2.15e-06

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 42.49  E-value: 2.15e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 488192435  141 KIYAWTVNNESVMTGMILMGVNGIITDYLT 170
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDPE 30
 
Name Accession Description Interval E-value
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 23-169 2.36e-55

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial glycerophosphodiester phosphodiesterases. In addition to a C-terminal GDPD domain, most members in this family have an N-terminus that functions as a membrane anchor.


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 173.89  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  23 QITVSENGYSTKMTSFDDYLTKANQLEQKLLIEIKTSSQDSKKIMAHFLNKYAKPI---KHQIHSLDYHLIDKVKKYDKS 99
Cdd:cd08579   70 KLTIGENGHGAKIPSLDEYLALAKGLKQKLLIELKPHGHDSPDLVEKFVKLYKQNLienQHQVHSLDYRVIEKVKKLDPK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488192435 100 LVAYFILPY-KSIFSRTKANGYTMEYFSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDYL 169
Cdd:cd08579  150 IKTGYILPFnIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-168 1.13e-15

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 71.96  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  33 TKMTSFDDYLTKANQLEQKLLIEIKtSSQDSKKIMAHFLN--KYAKPIKHQIH--SLDYHLIDKVKKYDKSLVAYFILPY 108
Cdd:cd08582   84 EKVPTLEEYLAIVPKYGKKLFIEIK-HPRRGPEAEEELLKllKESGLLPEQIViiSFDAEALKRVRELAPTLETLWLRNY 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488192435 109 KS-------IFSRTKANGYTMEY-FSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:cd08582  163 KSpkedprpLAKSGGAAGLDLSYeKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNR 230
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
22-168 1.47e-15

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 71.44  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  22 LQITVSENGYSTKMTSFDDYLTKAnQLEQKLLIEIKTSSQDSKKI---MAHFLNKYAKPIKHQIHSLDYHLIDKVKKYDK 98
Cdd:COG0584   75 LDAGSGPDFAGERIPTLEEVLELV-PGDVGLNIEIKSPPAAEPDLaeaVAALLKRYGLEDRVIVSSFDPEALRRLRELAP 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488192435  99 S-----LVAYFILPYKSIFSRTKANGYTMEYFSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:COG0584  154 DvplglLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDR 228
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 37-168 9.23e-15

Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins; The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases.


Pssm-ID: 176499 [Multi-domain]  Cd Length: 189  Bit Score: 68.44  E-value: 9.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  37 SFDDYLTKANQlEQKLLIEIKTSSQDSK--KIMAHFLNKYAKPIKHQIHSLDYHLIDKVKKYDKSLVAYFILPYKSIF-- 112
Cdd:cd08556   50 TLEEVLELVKG-GVGLNIELKEPTRYPGleAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDpl 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488192435 113 -----SRTKANGYTMEYFSLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:cd08556  129 laelaRALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 54-168 6.97e-12

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 61.42  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  54 IEIKTSSQDSKKI---MAHFLNKYAKPIKHQIHSLDYHLIDKVKKYDKS-----LVAYFILPYKSIFSRTKANGYTMEYF 125
Cdd:cd08563  107 IEIKTDVIHYPGIekkVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKiklalLYETGLQDPKDYAKKIGADSLHPDFK 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488192435 126 SLDQNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:cd08563  187 LLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNY 229
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 141-170 2.15e-06

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 42.49  E-value: 2.15e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 488192435  141 KIYAWTVNNESVMTGMILMGVNGIITDYLT 170
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDPE 30
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 141-168 2.71e-06

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 45.85  E-value: 2.71e-06
                          10        20
                  ....*....|....*....|....*...
gi 488192435  141 KIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:pfam03009 214 VVHVWTVNNEDEMKRLLELGVDGVITDR 241
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 131-168 2.94e-06

Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic phosphodiesterases UgpQ2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized cytoplasmic phosphodiesterases which predominantly exist in bacteria. The prototype of this family is a putative cytoplasmic phosphodiesterase encoded by gene ulpQ2 (SCO1419) in the Streptomyces coelicolor genome. It is distantly related to the Escherichia coli cytoplasmic phosphodiesterases UgpQ that catalyzes the hydrolysis of glycerophosphodiesters at the inner side of the cytoplasmic membrane to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176504 [Multi-domain]  Cd Length: 249  Bit Score: 45.71  E-value: 2.94e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488192435 131 FMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:cd08561  204 FVRAAHAAGLEVHVWTVNDPAEMRRLLDLGVDGIITDR 241
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 141-168 4.24e-06

Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and similar proteins. The prototype of this CD is a putative GP-GDE from Silicibacter pomeroyi (SpGDE). It shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176510 [Multi-domain]  Cd Length: 263  Bit Score: 45.38  E-value: 4.24e-06
                         10        20
                 ....*....|....*....|....*...
gi 488192435 141 KIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:cd08567  233 KVVPWTVNDPEDMARLIDLGVDGIITDY 260
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 129-168 1.40e-05

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase.


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 43.75  E-value: 1.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488192435 129 QNFMTKLLTNHKKIYAWTVNNESVMTGMILMGVNGIITDY 168
Cdd:cd08570  194 QAFLPELKKNGKKVFVWTVNTEEDMRYAIRLGVDGVITDD 233
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 54-170 8.35e-04

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family.


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 38.74  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488192435  54 IEIKTSSQDSKKIMAHFLNKYAKPIKHQIHSLDYHLIDKVKKYDKS-------------LVAYFI--------------L 106
Cdd:cd08612  139 IDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNiplffslkrvlllLLLYYTgllpfipikesfleI 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488192435 107 PYKSIFSRTK-ANGYTMEY----FSLDQNFMTKLLTNHKK-----IYAWTVNNESVMTGMILMGVNGIITDYLT 170
Cdd:cd08612  219 PMPSIFLKTYfPKSMSRLNrfvlFLIDWLLMRPSLFRHLQkrgiqVYGWVLNDEEEFERAFELGADGVMTDYPT 292
 
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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