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Conserved domains on  [gi|487748051|ref|WP_001830132|]
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MULTISPECIES: glycerophosphodiester phosphodiesterase [Staphylococcus]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 10171128)

glycerophosphodiester phosphodiesterase hydrolyzes deacylated phospholipids to glycerol 3-phosphate and the corresponding alcohols

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 50-304 1.58e-117

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: 338.46  E-value: 1.58e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTDI 129
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 NNQTPYRGHDKAKILSFEELLELYPNMYINVDLKDApdtyeGRIAPKVIYDNIIKHGAQHRVLVTSFHKKQIQRFTEYNQ 209
Cdd:cd08561   81 GGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDD-----GPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 210 aDIAIGASEGEVAEGFIKFNGMLGHTFKPQADTFQMPVAYKGISLTSKRFIQWLNLNNIVPGYYGVNSIDLMTDLYHKGV 289
Cdd:cd08561  156 -RVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                        250
                 ....*....|....*
gi 487748051 290 HTLVTDRPDLGQQFK 304
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 50-304 1.58e-117

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: 338.46  E-value: 1.58e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTDI 129
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 NNQTPYRGHDKAKILSFEELLELYPNMYINVDLKDApdtyeGRIAPKVIYDNIIKHGAQHRVLVTSFHKKQIQRFTEYNQ 209
Cdd:cd08561   81 GGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDD-----GPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 210 aDIAIGASEGEVAEGFIKFNGMLGHTFKPQADTFQMPVAYKGISLTSKRFIQWLNLNNIVPGYYGVNSIDLMTDLYHKGV 289
Cdd:cd08561  156 -RVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                        250
                 ....*....|....*
gi 487748051 290 HTLVTDRPDLGQQFK 304
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
46-303 4.59e-67

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 209.34  E-value: 4.59e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  46 QAPYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYH 125
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 126 ftdinnqtpyRGHDKAKILSFEELLELYP-NMYINVDLKDaPDTYEGRIAPKVIyDNIIKHGAQHRVLVTSFHKKQIQRF 204
Cdd:COG0584   81 ----------PDFAGERIPTLEEVLELVPgDVGLNIEIKS-PPAAEPDLAEAVA-ALLKRYGLEDRVIVSSFDPEALRRL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 205 TEYNqADIAIGASEGEVAEGFIKFNGMLGHTFkpqadtfqmpVAYkGISLTSKRFIQWLNLNNIVPGYYGVNSIDLMTDL 284
Cdd:COG0584  149 RELA-PDVPLGLLVEELPADPLELARALGADG----------VGP-DYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRL 216

                        250
                 ....*....|....*....
gi 487748051 285 YHKGVHTLVTDRPDLGQQF 303
Cdd:COG0584  217 LDLGVDGIITDRPDLLRAV 235
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 53-299 7.02e-32

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: 118.66  E-value: 7.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051   53 HRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGyhftdINNQ 132
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG-----AGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  133 TPYRgHDKAKILSFEELLELYPNMYINVDLK-----DAPDTYEGRIAPKVI-YDNII--KHGAQHRVLVTSFHKKQIQRF 204
Cdd:pfam03009  76 GPLS-GERVPFPTLEEVLEFDWDVGFNIEIKikpyvEAIAPEEGLIVKDLLlSVDEIlaKKADPRRVIFSSFNPDELKRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  205 TEYnqadiaigASEGEVAEGFIKFNGMLGHTFKPQADTFQMPVAYKGISLTSKR---FIQWLNLNNIVPGYYGVNSIDLM 281
Cdd:pfam03009 155 REL--------APKLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALVDEAlpdLVKRAHARGLVVHVWTVNNEDEM 226

                         250
                  ....*....|....*...
gi 487748051  282 TDLYHKGVHTLVTDRPDL 299
Cdd:pfam03009 227 KRLLELGVDGVITDRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 48-123 9.62e-23

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 94.62  E-value: 9.62e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAG 123
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAG 83
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 50-304 1.58e-117

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: 338.46  E-value: 1.58e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTDI 129
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 NNQTPYRGHDKAKILSFEELLELYPNMYINVDLKDApdtyeGRIAPKVIYDNIIKHGAQHRVLVTSFHKKQIQRFTEYNQ 209
Cdd:cd08561   81 GGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDD-----GPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 210 aDIAIGASEGEVAEGFIKFNGMLGHTFKPQADTFQMPVAYKGISLTSKRFIQWLNLNNIVPGYYGVNSIDLMTDLYHKGV 289
Cdd:cd08561  156 -RVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                        250
                 ....*....|....*
gi 487748051 290 HTLVTDRPDLGQQFK 304
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
46-303 4.59e-67

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 209.34  E-value: 4.59e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  46 QAPYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYH 125
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 126 ftdinnqtpyRGHDKAKILSFEELLELYP-NMYINVDLKDaPDTYEGRIAPKVIyDNIIKHGAQHRVLVTSFHKKQIQRF 204
Cdd:COG0584   81 ----------PDFAGERIPTLEEVLELVPgDVGLNIEIKS-PPAAEPDLAEAVA-ALLKRYGLEDRVIVSSFDPEALRRL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 205 TEYNqADIAIGASEGEVAEGFIKFNGMLGHTFkpqadtfqmpVAYkGISLTSKRFIQWLNLNNIVPGYYGVNSIDLMTDL 284
Cdd:COG0584  149 RELA-PDVPLGLLVEELPADPLELARALGADG----------VGP-DYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRL 216

                        250
                 ....*....|....*....
gi 487748051 285 YHKGVHTLVTDRPDLGQQF 303
Cdd:COG0584  217 LDLGVDGIITDRPDLLRAV 235
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 48-297 4.10e-50

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: 165.81  E-value: 4.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFT 127
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 128 dinnqtpyRGHDKAKILSFEELLELYP--NMYINVDLKDAPDTYEGrIAPKViYDNIIKHGAQHRVLVTSFHKKQIQRFT 205
Cdd:cd08563   81 --------EKFTGEKIPTLEEVLDLLKdkDLLLNIEIKTDVIHYPG-IEKKV-LELVKEYNLEDRVIFSSFNHESLKRLK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 206 EYN-QADIAIGASEGEV-AEGFIKFNGMLG-HtfkPQadtfqmpvaykgISLTSKRFIQWLNLNNIVPGYYGVNSIDLMT 282
Cdd:cd08563  151 KLDpKIKLALLYETGLQdPKDYAKKIGADSlH---PD------------FKLLTEEVVEELKKRGIPVRLWTVNEEEDMK 215

                        250
                 ....*....|....*
gi 487748051 283 DLYHKGVHTLVTDRP 297
Cdd:cd08563  216 RLKDLGVDGIITNYP 230
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-249 6.09e-46

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like 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 is not 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 mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4.


Pssm-ID: 176517 [Multi-domain]  Cd Length: 264  Bit Score: 156.22  E-value: 6.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFT 127
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 128 DINNQT--PYRGHDKaKILSFEELLELYPNMYINVDLKDAPDtyeGRIAPKVIyDNIIKHGAQHRVLVTSFHKKQIQRFT 205
Cdd:cd08575   81 FDGGKTgyPRGGGDG-RIPTLEEVFKAFPDTPINIDIKSPDA---EELIAAVL-DLLEKYKREDRTVWGSTNPEYLRALH 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 487748051 206 EYNQaDIAIGASegevAEGFIKFNGMLGHT----FKP-QADTFQMPVAY 249
Cdd:cd08575  156 PENP-NLFESFS----MTRCLLLYLALGYTgllpFVPiKESFFEIPRPV 199
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 50-208 2.09e-35

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family 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. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function.


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 127.80  E-value: 2.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGG-MAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAG---YH 125
Cdd:cd08566    2 VVAHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKdgdGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 126 FTDinnqtpyrghdkAKILSFEELLELYP-NMYINVDLKDAPdtyegriaPKVIYDNIIKHGAQHRVLVTSFHKKQIQRF 204
Cdd:cd08566   82 VTD------------EKVPTLEEALAWAKgKILLNLDLKDAD--------LDEVIALVKKHGALDQVIFKSYSEEQAKEL 141


                 ....
gi 487748051 205 TEYN 208
Cdd:cd08566  142 RALA 145
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 50-299 1.82e-32

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, 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.


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 120.20  E-value: 1.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTDi 129
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFGE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 nnqtpyrghdkaKILSFEELLELY--PNMYINVDLK-DAPDTYEGRIAPKVIyDNIIKHGAQHRVLVTSFHKKQIQRFTE 206
Cdd:cd08565   80 ------------KIPTLEEVLALFapSGLELHVEIKtDADGTPYPGAAALAA-ATLRRHGLLERSVLTSFDPAVLTEVRK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 207 YNQADIA--IGASEGEVAEGFIKFNGMLGHTfkpqadTFQMPVAYKGISLTS---KRFIQWLNLnnivpGYYGVNSIDLM 281
Cdd:cd08565  147 HPGVRTLgsVDEDMLERLGGELPFLTATALK------AHIVAVEQSLLAATWelvRAAVPGLRL-----GVWTVNDDSLI 215

                        250
                 ....*....|....*...
gi 487748051 282 TDLYHKGVHTLVTDRPDL 299
Cdd:cd08565  216 RYWLACGVRQLTTDRPDL 233
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 50-196 3.80e-32

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase UgpQ and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), UgpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two distinct GP-GDEs. UgpQ gene from the E. coli ugp operon codes for a cytosolic phosphodiesterase GlpQ, which is the prototype of this family. Various glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), can only be hydrolyzed by UgpQ during transport at the inner side of the cytoplasmic membrane to alcohols and G3P, which is a source of phosphate. In contrast to Ca2+-dependent periplasmic phosphodiesterase GlpQ, cytosolic phosphodiesterase UgpQ requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity.


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 118.86  E-value: 3.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTDi 129
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSP- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 nnqtPYRGhdkAKILSFEELLEL--YPNMYINVDLKDAPDTyEGRIAPKVIYDnIIKHGAQH-RVLVTSF 196
Cdd:cd08562   80 ----EFAG---EPIPTLADVLELarELGLGLNLEIKPDPGD-EALTARVVAAA-LRELWPHAsKLLLSSF 140
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 53-299 7.02e-32

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: 118.66  E-value: 7.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051   53 HRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGyhftdINNQ 132
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG-----AGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  133 TPYRgHDKAKILSFEELLELYPNMYINVDLK-----DAPDTYEGRIAPKVI-YDNII--KHGAQHRVLVTSFHKKQIQRF 204
Cdd:pfam03009  76 GPLS-GERVPFPTLEEVLEFDWDVGFNIEIKikpyvEAIAPEEGLIVKDLLlSVDEIlaKKADPRRVIFSSFNPDELKRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  205 TEYnqadiaigASEGEVAEGFIKFNGMLGHTFKPQADTFQMPVAYKGISLTSKR---FIQWLNLNNIVPGYYGVNSIDLM 281
Cdd:pfam03009 155 REL--------APKLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALVDEAlpdLVKRAHARGLVVHVWTVNNEDEM 226

                         250
                  ....*....|....*...
gi 487748051  282 TDLYHKGVHTLVTDRPDL 299
Cdd:pfam03009 227 KRLLELGVDGVITDRPDT 244
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 48-210 2.35e-31

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 117.81  E-value: 2.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFT 127
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 128 DiNNQTPYRGHdKAKILSFEELLELYPNMYINVDLKDAPDTYEGRIAPKVIYDNiikhGAQHRVLVTSFHKKQIQRFTEY 207
Cdd:cd08580   81 P-EGGYPYRGK-PVGIPTLEQVLRAFPDTPFILDMKSLPADPQAKAVARVLERE----NAWSRVRIYSTNADYQDALAPY 154


                 ...
gi 487748051 208 NQA 210
Cdd:cd08580  155 PQA 157
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 50-299 1.16e-29

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: 112.79  E-value: 1.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYhftdi 129
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 nnqtpyrGHDKA----KILSFEELLELYP--NMYINVDLKDApdTYEGRIAPKVIydNIIK--HGAQHRVLVTSFHKKQI 201
Cdd:cd08582   76 -------WKGESykgeKVPTLEEYLAIVPkyGKKLFIEIKHP--RRGPEAEEELL--KLLKesGLLPEQIVIISFDAEAL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 202 QRFTEYnqadiaigASEGEVAegfikfngMLGHTFKPQADTFQMPVAYK--GISL-----TSKRFIQWLNLNNIVPGYYG 274
Cdd:cd08582  145 KRVREL--------APTLETL--------WLRNYKSPKEDPRPLAKSGGaaGLDLsyekkLNPAFIKALRDAGLKLNVWT 208

                        250       260
                 ....*....|....*....|....*
gi 487748051 275 VNSIDLMTDLYHKGVHTLVTDRPDL 299
Cdd:cd08582  209 VDDAEDAKRLIELGVDSITTNRPGR 233
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 50-296 1.66e-29

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: 110.82  E-value: 1.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDalvdrttngsgkvsehtlaelkrldagyhftdi 129
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 nnqtpyrghdkakILSFEELLELYPN-MYINVDLKDaPDTYEGrIAPKVIyDNIIKHGAQHRVLVTSFHKKQIQRFTEYN 208
Cdd:cd08556   48 -------------IPTLEEVLELVKGgVGLNIELKE-PTRYPG-LEAKVA-ELLREYGLEERVVVSSFDHEALRALKELD 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 209 QaDIAIGAsegeVAEGFIKFNGMLGHTFKPQADTFQMPVAykgisLTSKRFIQWLNLNNIVPGYYGVNSIDLMTDLYHKG 288
Cdd:cd08556  112 P-EVPTGL----LVDKPPLDPLLAELARALGADAVNPHYK-----LLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALG 181


                 ....*...
gi 487748051 289 VHTLVTDR 296
Cdd:cd08556  182 VDGIITDD 189
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 50-203 3.95e-27

Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 106.63  E-value: 3.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGS--GKVSEHTLAELKRLDAGYHFt 127
Cdd:cd08601    3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAGSWF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 128 diNNQTPYRGHD---KAKILSFEELLELY---PNMYInvDLKDaPDTYEGrIAPKViYDNIIKHGAQH------RVLVTS 195
Cdd:cd08601   82 --NKAYPEYAREsysGLKVPTLEEVIERYggrANYYI--ETKS-PDLYPG-MEEKL-LATLDKYGLLTdnlkngQVIIQS 154


                 ....*...
gi 487748051 196 FHKKQIQR 203
Cdd:cd08601  155 FSKESLKK 162
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 50-226 9.96e-27

Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermotoga maritime glycerophosphodiester phosphodiesterase (TmGDE, 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. TmGDE exists as a monomer that might be the biologically relevant form.


Pssm-ID: 176511 [Multi-domain]  Cd Length: 226  Bit Score: 104.69  E-value: 9.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGyhftdi 129
Cdd:cd08568    2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 nnqtpyrghdKAKILSFEELLELYPNMYI-NVDLKDaPDtyegriAPKVIYDNIIKHGAQHRVLVTSFHKKQIQRFTEYN 208
Cdd:cd08568   76 ----------GELIPTLEEVFRALPNDAIiNVEIKD-ID------AVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLD 138

                        170
                 ....*....|....*...
gi 487748051 209 QaDIAIGASEGEVAEGFI 226
Cdd:cd08568  139 P-DAKVGLLIGEEEEGFS 155
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 52-208 5.36e-25

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: 101.52  E-value: 5.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  52 AHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAEL----KRLD---AGY 124
Cdd:cd08612   31 SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylEKLEvtfSPG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 125 HFTDINNQTPyrghdkaKILSFEELLELYPNMYINVDLKdapdtYEGRIAPKVIYDNIIKHGAQHRVLVTSFHKKQIQRF 204
Cdd:cd08612  111 DYCVPKGSDR-------RIPLLEEVFEAFPDTPINIDIK-----VENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKC 178


                 ....
gi 487748051 205 TEYN 208
Cdd:cd08612  179 HKEN 182
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 48-153 8.00e-25

Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in bacterial and eukaryotic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ. GP-GDEs are involved in glycerol metabolism and catalyze the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. In E. coli, there are two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the glp operon codes for a periplasmic phosphodiesterase GlpQ. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for GlpQ enzymatic activity. This subfamily also includes some GP-GDEs in higher plants and their eukaryotic homologs, which show very high sequence similarities with bacterial periplasmic GP-GDEs.


Pssm-ID: 176502 [Multi-domain]  Cd Length: 296  Bit Score: 101.20  E-value: 8.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTN------------GSGKVSEHTLA 115
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 487748051 116 ELKRLDAGYHFtdiNNQTPYRGHD---KAKILSFEELLELY 153
Cdd:cd08559   81 ELKTLRAGSWF---NQRYPERAPSyygGFKIPTLEEVIELA 118
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 48-123 9.62e-23

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 94.62  E-value: 9.62e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAG 123
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAG 83
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 50-197 1.48e-22

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 94.25  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTDI 129
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748051 130 NNqtpyrgHDKAKILSFEE----LLELypNMYINVDLKDAPDTyegriAPKVIYDNIIKH-GAQHRVLVTSFH 197
Cdd:cd08573   81 SR------FPGEKIPTLEEavkeCLEN--NLRMIFDVKSNSSK-----LVDALKNLFKKYpGLYDKAIVCSFN 140
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 50-297 5.42e-21

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: 89.20  E-value: 5.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKV-SEHTLAELKRLdagyhftd 128
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIiDDSTWDELSHL-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 129 innQTpyRGHDKAKILSFEELLEL-----YPNMYINVDLKDAPDTyegRIAPKVIyDNIIK-----HGAQHRVLVTSFHK 198
Cdd:cd08570   73 ---RT--IEEPHQPMPTLKDVLEWlveheLPDVKLMLDIKRDNDP---EILFKLI-AEMLAvkpdlDFWRERIILGLWHL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 199 KqiqrFTEYNQAD------IAIGASEgEVAEGFIKFNGMLghtfkpqadtfqmpvayKGISLT--------SKRFIQWLN 264
Cdd:cd08570  144 D----FLKYGKEVlpgfpvFHIGFSL-DYARHFLNYSEKL-----------------VGISMHfvslwgpfGQAFLPELK 201

                        250       260       270
                 ....*....|....*....|....*....|...
gi 487748051 265 LNNIVPGYYGVNSIDLMTDLYHKGVHTLVTDRP 297
Cdd:cd08570  202 KNGKKVFVWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 50-299 1.58e-20

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: 88.91  E-value: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALV--DRTTNGSGK--------VSEHTLAELKR 119
Cdd:cd08567    3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAwlpyegpaLYELTLAEIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 120 LDAGY---------HFTDinnQTPYRGhdkAKILSFEELLEL-----YPNMYINVDLKDAPDtYEGRIAP-----KVIYD 180
Cdd:cd08567   83 LDVGEkrpgsdyakLFPE---QIPVPG---TRIPTLEEVFALvekygNQKVRFNIETKSDPD-RDILHPPpeefvDAVLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 181 NIIKHGAQHRVLVTSFHKKQIQRFTEYNqADIAIGA-SEGEVAEGFIKFNGMLG-HTFKPQADtfqmpvaykgisLTSKR 258
Cdd:cd08567  156 VIRKAGLEDRVVLQSFDWRTLQEVRRLA-PDIPTVAlTEETTLGNLPRAAKKLGaDIWSPYFT------------LVTKE 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 487748051 259 FIQW---LNLNNIVpgyYGVNSIDLMTDLYHKGVHTLVTDRPDL 299
Cdd:cd08567  223 LVDEahaLGLKVVP---WTVNDPEDMARLIDLGVDGIITDYPDL 263
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 44-172 5.59e-20

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 88.19  E-value: 5.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  44 SGQAPYIFAHRGgMA-----------------MRP------EQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVD 100
Cdd:cd08613   20 PGGKPKLLAHRG-LAqtfdregvendtctaerIDPpthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLD 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748051 101 RTTNGSGKVSEHTLAELKRLDAGYHFTDINNQT-PYRGHDKAKILSFEELLELYPNMYINVDLKDApDTYEGR 172
Cdd:cd08613   99 CRTDGSGVTRDHTMAELKTLDIGYGYTADGGKTfPFRGKGVGMMPTLDEVFAAFPDRRFLINFKSD-DAAEGE 170
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 50-297 6.76e-20

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: 86.06  E-value: 6.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYHFTdi 129
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGENGH-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 130 nnqtpyrghdKAKILSFEELLELYPNMYI--NVDLKDAPdTYEGRIAPKVIyDNIIKHGAQHRVLVTSFHKKQIQRFTEY 207
Cdd:cd08579   79 ----------GAKIPSLDEYLALAKGLKQklLIELKPHG-HDSPDLVEKFV-KLYKQNLIENQHQVHSLDYRVIEKVKKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 208 NqADIAIGAsegevaegFIKFN-GMLGHTFkpqADTFQMPVaykgiSLTSKRFIQWLNLNN-IVpgY-YGVNSIDLMTDL 284
Cdd:cd08579  147 D-PKIKTGY--------ILPFNiGNLPKTN---VDFYSIEY-----STLNKEFIRQAHQNGkKV--YvWTVNDPDDMQRY 207

                        250
                 ....*....|...
gi 487748051 285 YHKGVHTLVTDRP 297
Cdd:cd08579  208 LAMGVDGIITDYP 220
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 51-228 5.61e-18

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 with Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 81.21  E-value: 5.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  51 FAHRG--GMAMR-PEQTQLAFDNAVEYGLdGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLdagyHFT 127
Cdd:cd08585    7 IAHRGlhDRDAGiPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL----RLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 128 DINNQTPyrghdkakilSFEELLELYPN--MYInVDLKdAPDTYEGRIAPKVIydNIIKH--GAqhrVLVTSFHKKQIQR 203
Cdd:cd08585   82 GTDEHIP----------TLDEVLELVAGrvPLL-IELK-SCGGGDGGLERRVL--AALKDykGP---AAIMSFDPRVVRW 144

                        170       180
                 ....*....|....*....|....*.
gi 487748051 204 FTEyNQADIAIG-ASEGEVAEGFIKF 228
Cdd:cd08585  145 FRK-LAPGIPRGqLSEGSNDEADPAF 169
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 48-197 6.33e-16

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase (GsGDE, EC 3.1.4.46) and its uncharacterized eukaryotic 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.


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 75.97  E-value: 6.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRG-GMAMR-PEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFH--------DALVDRTTNGSGKVSEHTLAEL 117
Cdd:cd08564    4 PIIVGHRGaGCSTLyPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDEI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 118 KRLDAGYHFtdINNQTPYRGHDKAKILSFEELLELY-PNMYINVDLKdapdtyegriAPKV-----IYDNIIKHGAQHRV 191
Cdd:cd08564   84 TRLHFKQLF--DEKPCGADEIKGEKIPTLEDVLVTFkDKLKYNIELK----------GREVglgerVLNLVEKYGMILQV 151


                 ....*.
gi 487748051 192 LVTSFH 197
Cdd:cd08564  152 HFSSFL 157
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 50-197 1.06e-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: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 74.68  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTLAELKRLDAGYhftdi 129
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAE----- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487748051 130 nNQTPYRGHDKAKILSFEELLEL---YPNMYINVDLKdaPDTYeGRIAPKVIYDNIIKHG---AQHRVLVtSFH 197
Cdd:cd08581   76 -PARFGSRFAGEPLPSLAAVVQWlaqHPQVTLFVEIK--TESL-DRFGLERVVDKVLRALpavAAQRVLI-SFD 144
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 47-166 1.73e-15

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2, GDE3, GDE6-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase domain-containing protein subtype 5 (GDE2), subtype 2 (GDE3), subtype 1 (GDE6), and their eukaryotic homologs. Mammalian GDE2, GDE3, and GDE6 show very high sequence similarity to each other and have been classified into the same family. Although they are all transmembrane proteins, based on different pattern of tissue distribution, these enzymes might display diverse cellular functions. Mammalian GDE2 is primarily expressed in mature neurons. It selectively hydrolyzes glycerophosphocholine (GPC) and mainly functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE3 is specifically expressed in bone tissues and spleen. It selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol and functions as an inducer of osteoblast differentiation. Mammalian GDE6 is predominantly expressed in the spermatocytes of testis, and its specific physiological function has not been elucidated yet.


Pssm-ID: 176516 [Multi-domain]  Cd Length: 252  Bit Score: 74.65  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  47 APYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGS----GKVSEH----TLAELK 118
Cdd:cd08574    1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVAdvfpERAHERasmfTWTDLQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 487748051 119 RLDAG---------YHFTDINNQTPYRGHDKaKILSFEELLEL--YPNMYINVDLKDAP 166
Cdd:cd08574   81 QLNAGqwflkddpfWTASSLSESDREEAGNQ-SIPSLAELLRLakKHNKSVIFDLRRPP 138
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 48-206 7.72e-15

Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively.


Pssm-ID: 176544 [Multi-domain]  Cd Length: 309  Bit Score: 73.49  E-value: 7.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNgsgkVSEH--------------- 112
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTD----VADHpefadrkttktvdgv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 113 ----------TLAELKRLDAGYHFTDINNQtpYRGhdKAKILSFEELLELypnmyinvdLKDAPDTYEGRIApkvIYDNi 182
Cdd:cd08602   77 nvtgwftedfTLAELKTLRARQRLPYRDQS--YDG--QFPIPTFEEIIAL---------AKAASAATGRTVG---IYPE- 139

                        170       180
                 ....*....|....*....|....
gi 487748051 183 IKHGaqhrvlvtSFHKKQIQRFTE 206
Cdd:cd08602  140 IKHP--------TYFNAPLGLPME 155
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 50-152 2.16e-13

Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), GlpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ, which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein, protein D (HPD), from Haemophilus influenza Type b and nontypeable strains, which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria.


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 69.34  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  50 IFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTN------------GSGKVSEHTLAEL 117
Cdd:cd08600    3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNvaekfpdrkrkdGRYYVIDFTLDEL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 487748051 118 KRLDAGYHFTDINN----QTPYR---GHDKAKILSFEELLEL 152
Cdd:cd08600   83 KSLSVTERFDIENGkkvqVYPNRfplWKSDFKIHTLEEEIEL 124
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 32-169 4.16e-13

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE3 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE3 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 2 (GDPD2), Osteoblast differentiation promoting factor) and their metazoan homologs. Mammalian GDE3 is a transmembrane protein specifically expressed in bone tissues and spleen. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE3 has been characterized as glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol. Mammalian GDE3 functions as an inducer of osteoblast differentiation. It also plays a critical role for actin cytoskeletal modulation. The catalytic activity of GDPD domain is essential for mammalian GDE3 cellular function.


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 68.41  E-value: 4.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  32 SPQQLksiPPffsgqAPYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKV-- 109
Cdd:cd08609   19 EENNL---PP-----KPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFpg 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487748051 110 ------SEHTLAELKRLDAGYHFTDinnQTPY-----------RGHDKAKILSFEELLELYP--NMYINVDLKDAPDTY 169
Cdd:cd08609   91 rdaagsNNFTWTELKTLNAGSWFLE---RRPFwtlsslseedrREADNQTVPSLSELLDLAKkhNVSIMFDLRNENNSH 166
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 45-104 2.80e-11

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation.


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 63.35  E-value: 2.80e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  45 GQAPYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTN 104
Cdd:cd08610   20 GPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 48-152 7.79e-09

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 56.22  E-value: 7.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  48 PYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGK------------VSEHTLA 115
Cdd:PRK11143  27 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERfpdrarkdgryyAIDFTLD 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 487748051 116 ELKRLDAGYHF-TDINNQT---PYR---GHDKAKILSFEELLEL 152
Cdd:PRK11143 107 EIKSLKFTEGFdIENGKKVqvyPGRfpmGKSDFRVHTFEEEIEF 150
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 52-147 1.80e-08

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.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 53.21  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  52 AHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSgkvSEHTLAELKRLDAGYHFTDinn 131
Cdd:cd08555    3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGI---LPPTLEEVLELIADYLKNP--- 76

                         90
                 ....*....|....*.
gi 487748051 132 qtpyrghDKAKILSFE 147
Cdd:cd08555   77 -------DYTIILSLE 85
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 47-210 4.88e-08

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 53.69  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  47 APYIFAHRGGMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEHTL--------AELK 118
Cdd:cd08608    1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYedasmfnwTDLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 119 RLDAGYHFTDIN--------NQTPYRGHDKAKILSFEELLEL--------------------YPNMYINVDLKD------ 164
Cdd:cd08608   81 RLNAGQWFLKDDpfwtaqslSPSDRKEAGNQSVCSLAELLELakrynasvllnlrrpppnhpYHQSWINLTLKTilasgi 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487748051 165 -------APDTYEG---RIAPkviydnIIKHGAQHRVLVTSFHKKQIQRFT-EYNQA 210
Cdd:cd08608  161 pqeqvmwTPDWQRKlvrKVAP------GFQQTSGEKLPVASLRERGITRLNlRYTQA 211
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 53-197 6.15e-08

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176514 [Multi-domain]  Cd Length: 293  Bit Score: 53.05  E-value: 6.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  53 HRG-GM-------AMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNGSGKVSEH----------TL 114
Cdd:cd08572    5 HRGlGKnyasgslAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDEGelievpihdlTL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 115 AELKRLDaGYHFTDINNQTPYRGHDKAKIL-----------SFEELLE-LYPNMYINVDLKdAPDTYEGRIAPKVIYDN- 181
Cdd:cd08572   85 EQLKELG-LQHISALKRKALTRKAKGPKPNpwgmdehdpfpTLQEVLEqVPKDLGFNIEIK-YPQLLEDGEGELTPYFEr 162

                        170       180
                 ....*....|....*....|....*.
gi 487748051 182 ----------IIKHGAQHRVLVTSFH 197
Cdd:cd08572  163 nafvdtilavVFEHAGGRRIIFSSFD 188
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 53-196 1.04e-06

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism.


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 49.21  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  53 HRG-------GMAMRPEQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHD----ALVDRTTNGSGK------VSEHTLA 115
Cdd:cd08607    5 HRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDftlrVSLKSKGDSDRDdllevpVKDLTYE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 116 ELKRLDAgYHFTDINNQTPYRGHDKAKIL------SFEELLE-LYPNMYINVDLK------------DAPDTYEGRIAPK 176
Cdd:cd08607   85 QLKLLKL-FHISALKVKEYKSVEEDEDPPehqpfpTLSDVLEsVPEDVGFNIEIKwpqqqkdgswesELFTYFDRNLFVD 163

                        170       180
                 ....*....|....*....|
gi 487748051 177 VIYDNIIKHGAQHRVLVTSF 196
Cdd:cd08607  164 IILKIVLEHAGKRRIIFSSF 183
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 67-295 1.17e-06

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 48.84  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  67 AFDNAVEYGLDGFETDVRLTKDEQLIVFH-------DALVDRTTNGSGKVSEHtlaELKRldagyhftdinnqTPYrgHD 139
Cdd:cd08583   20 AFEHNYKKGYRVFEVDLSLTSDGVLVARHswdesllKQLGLPTSKNTKPLSYE---EFKS-------------KKI--YG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 140 KAKILSFEELLEL---YPNMYINVDLKDAPDTyegriAPKVIYDNIIKhGAQH-------RVLVtsfhkkQIqrfteYNQ 209
Cdd:cd08583   82 KYTPMDFKDVIDLlkkYPDVYIVTDTKQDDDN-----DIKKLYEYIVK-EAKEvdpdlldRVIP------QI-----YNE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 210 ADIAIGASegevaegFIKFNGMLGHTFKPQADTFQMPVAY---KGISLT-------SKRFIQWLNLNNIVPGYYGVNSID 279
Cdd:cd08583  145 EMYEAIMS-------IYPFKSVIYTLYRQDSIRLDEIIAFcyeNGIKAVtisknyvNDKLIEKLNKAGIYVYVYTINDLK 217

                        250
                 ....*....|....*.
gi 487748051 280 LMTDLYHKGVHTLVTD 295
Cdd:cd08583  218 DAQEYKKLGVYGIYTD 233
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 52-120 1.62e-04

Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs.


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 42.40  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  52 AHRG-GMAMRP----------EQTQLAFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTTNG---SGKVSEHTLAEL 117
Cdd:cd08605    4 GHRGlGMNRAShqpsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGeveSSRIRDLTLAEL 83


                 ...
gi 487748051 118 KRL 120
Cdd:cd08605   84 KAL 86
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 47-197 6.74e-04

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), 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 YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 40.51  E-value: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051  47 APYIFAHRGGMAMRPEQTQL--------AFDNAVEYGLDGFETDVRLTKDEQLIVFHDALVDRTtngSGKVSEHTLAELK 118
Cdd:cd08606    1 SVQVIGHRGLGKNTAERKSLqlgentveSFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSET---GTDVPIHDLTLEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748051 119 RLDAGY-----HFTDINNQTPYRGHD-KAKILSFEELL-ELYPNMYINVDLKD-----------APDTYEGRIAPKVIYD 180
Cdd:cd08606   78 FLHLSRmkytvDFKKKGFKGNSRGHSiQAPFTTLEELLkKLPKSVGFNIELKYpmlheaeeeevAPVAIELNAFVDTVLE 157

                        170
                 ....*....|....*..
gi 487748051 181 NIIKHGAQHRVLVTSFH 197
Cdd:cd08606  158 KVFDYGAGRNIIFSSFT 174
 
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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