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Conserved domains on  [gi|71994759|ref|NP_001022321|]
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Putative glycerophosphocholine phosphodiesterase GPCPD1 homolog 2 [Caenorhabditis elegans]

Protein Classification

glycerophosphodiester phosphodiesterase family protein; PI-PLC domain-containing protein( domain architecture ID 10146619)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to GDPD domain region of GPCPD1/GDE5 that may be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity| PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol; similar to Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 402-704 3.89e-160

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: 466.39  E-value: 3.89e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 402 LEVGHRGAGNSYTKF-AMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRdglampppmtreqLD 480
Cdd:cd08607   1 LDVGHRGAGNSYTAAsAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSK-------------GD 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 481 SSNLDYHELPVKDLKLSQLKLLMLDHLSFPQKKEnvKKLVEAGEEEEDFKPFPTLLEALTKVDPDVGFNVEVKYPMMQNN 560
Cdd:cd08607  68 SDRDDLLEVPVKDLTYEQLKLLKLFHISALKVKE--YKSVEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKD 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 561 GEHECDH--YFERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTPFQDQRTSTSMTA 638
Cdd:cd08607 146 GSWESELftYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIA 225

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994759 639 VNFAAGADLLGVNFNSEDLLKDPMPVKKANEFGMVTFVWGEDLDKKENINYFkKELGVDGVIYDRI 704
Cdd:cd08607 226 VNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKL-KELGVDGLIYDRI 290
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 84-207 2.74e-48

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


:

Pssm-ID: 99888  Cd Length: 120  Bit Score: 166.34  E-value: 2.74e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759  84 VRVHFAVDVENLHAHQSVYVVGSNDVLGTWEATRAMPLVQDPDRFMRWKGSIVTD-VHQLKFRYFIGYNLMSDQGERLIV 162
Cdd:cd05814   1 CRVTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDDDCNLWKASIELPrGVDFQYRYFVAVVLNDSGPCQVIV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71994759 163 DKWEAFLHPRSTLCLaesrnDECRVDRVDLFGYYAGRKCVSDGWL 207
Cdd:cd05814  81 RKWETHLQPRSIKPL-----EEERLNDDDKFGIYDGVEQVDRGWL 120
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 402-704 3.89e-160

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: 466.39  E-value: 3.89e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 402 LEVGHRGAGNSYTKF-AMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRdglampppmtreqLD 480
Cdd:cd08607   1 LDVGHRGAGNSYTAAsAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSK-------------GD 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 481 SSNLDYHELPVKDLKLSQLKLLMLDHLSFPQKKEnvKKLVEAGEEEEDFKPFPTLLEALTKVDPDVGFNVEVKYPMMQNN 560
Cdd:cd08607  68 SDRDDLLEVPVKDLTYEQLKLLKLFHISALKVKE--YKSVEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKD 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 561 GEHECDH--YFERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTPFQDQRTSTSMTA 638
Cdd:cd08607 146 GSWESELftYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIA 225

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994759 639 VNFAAGADLLGVNFNSEDLLKDPMPVKKANEFGMVTFVWGEDLDKKENINYFkKELGVDGVIYDRI 704
Cdd:cd08607 226 VNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKL-KELGVDGLIYDRI 290
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 406-706 2.24e-64

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: 215.34  E-value: 2.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759   406 HRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRDglampppmtreqldssnld 485
Cdd:pfam03009   1 HRGASGSYP------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759   486 yhelPVKDLKLSQLKLLmldhlsfPQKKENVKKLVEAGeeeedfKPFPTLLEALtKVDPDVGFNVEVKYPMMQNNGEHEC 565
Cdd:pfam03009  56 ----YVRDLTLEELKRL-------DIGAGNSGPLSGER------VPFPTLEEVL-EFDWDVGFNIEIKIKPYVEAIAPEE 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759   566 -DHYFERNLFVDVILAdvmKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTPfqdqrtsTSMTAVNFAAG 644
Cdd:pfam03009 118 gLIVKDLLLSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRAYAEAD-------LLERAAAFAGA 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71994759   645 ADLLGVNFNSEDLLkdPMPVKKANEFGMVTFVWGEDldkKENINYFKKELGVDGVIYDRIGE 706
Cdd:pfam03009 188 PALLGEVALVDEAL--PDLVKRAHARGLVVHVWTVN---NEDEMKRLLELGVDGVITDRPDT 244
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 84-207 2.74e-48

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 166.34  E-value: 2.74e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759  84 VRVHFAVDVENLHAHQSVYVVGSNDVLGTWEATRAMPLVQDPDRFMRWKGSIVTD-VHQLKFRYFIGYNLMSDQGERLIV 162
Cdd:cd05814   1 CRVTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDDDCNLWKASIELPrGVDFQYRYFVAVVLNDSGPCQVIV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71994759 163 DKWEAFLHPRSTLCLaesrnDECRVDRVDLFGYYAGRKCVSDGWL 207
Cdd:cd05814  81 RKWETHLQPRSIKPL-----EEERLNDDDKFGIYDGVEQVDRGWL 120
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
404-706 9.79e-31

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 121.13  E-value: 9.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLvSVARRDGlampppmtreqldssn 483
Cdd:COG0584   6 IAHRGAS------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLD-RTTNGTG---------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 ldyhelPVKDLKLSQLKLlmLDHLSFPQkkenvkklvEAGEeeedfkPFPTLLEALTKVDPDVGFNVEVKYPmmqnngeh 563
Cdd:COG0584  63 ------RVADLTLAELRQ--LDAGSGPD---------FAGE------RIPTLEEVLELVPGDVGLNIEIKSP-------- 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 564 ecdhYFERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCvgetqrytpfqdQRTSTSMTAVNFAA 643
Cdd:COG0584 112 ----PAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV------------EELPADPLELARAL 175

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994759 644 GADLLGVNFnseDLLKDPMpVKKANEFGMVTFVWGedLDKKENINYFkKELGVDGVIYDRIGE 706
Cdd:COG0584 176 GADGVGPDY---DLLTPEL-VAAAHAAGLKVHVWT--VNDPEEMRRL-LDLGVDGIITDRPDL 231
CBM_2 smart01065
Starch binding domain;
84-175 6.26e-19

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 82.01  E-value: 6.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759     84 VRVHFAVDVENLHAHQSVYVVGSNDVLGTWEATRAMPLVQDPDRFMRWKGSIVTDVH--QLKFRYFIGYNLMsdqgerli 161
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAgtTIEYKYVKVDEDG-------- 72

                           90
                   ....*....|....
gi 71994759    162 VDKWEAFLHPRSTL 175
Cdd:smart01065  73 SVTWESGPNRRLTV 86
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 404-455 5.42e-06

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 48.40  E-value: 5.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71994759  404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:PRK09454  11 VAHRGGG------KLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHD 56
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 402-704 3.89e-160

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: 466.39  E-value: 3.89e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 402 LEVGHRGAGNSYTKF-AMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRdglampppmtreqLD 480
Cdd:cd08607   1 LDVGHRGAGNSYTAAsAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSK-------------GD 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 481 SSNLDYHELPVKDLKLSQLKLLMLDHLSFPQKKEnvKKLVEAGEEEEDFKPFPTLLEALTKVDPDVGFNVEVKYPMMQNN 560
Cdd:cd08607  68 SDRDDLLEVPVKDLTYEQLKLLKLFHISALKVKE--YKSVEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKD 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 561 GEHECDH--YFERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTPFQDQRTSTSMTA 638
Cdd:cd08607 146 GSWESELftYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIA 225

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994759 639 VNFAAGADLLGVNFNSEDLLKDPMPVKKANEFGMVTFVWGEDLDKKENINYFkKELGVDGVIYDRI 704
Cdd:cd08607 226 VNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKL-KELGVDGLIYDRI 290
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 402-704 3.47e-135

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: 402.43  E-value: 3.47e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 402 LEVGHRGAGNSYTKFAMA--RENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRDGlampppmtreql 479
Cdd:cd08572   1 LVIGHRGLGKNYASGSLAgiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTG------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 480 dSSNLDYHELPVKDLKLSQLKLLMLDHLSFPQKKENVKKLVE---AGEEEEDFKPFPTLLEALTKVDPDVGFNVEVKYPM 556
Cdd:cd08572  69 -SDEGELIEVPIHDLTLEQLKELGLQHISALKRKALTRKAKGpkpNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYPQ 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 557 MQNNGEHECDHYFERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRyTPFQDQRTSTSM 636
Cdd:cd08572 148 LLEDGEGELTPYFERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNGGTNE-VEHMDPRRRSLQ 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994759 637 TAVNFAAGADLLGVNFNSEDLLKDPMPVKKANEFGMVTFVWGEDLDKKENINYFkKELGVDGVIYDRI 704
Cdd:cd08572 227 AAVNFALAEGLLGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQ-KELGVDGVIYDRV 293
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 406-706 2.24e-64

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: 215.34  E-value: 2.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759   406 HRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRDglampppmtreqldssnld 485
Cdd:pfam03009   1 HRGASGSYP------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759   486 yhelPVKDLKLSQLKLLmldhlsfPQKKENVKKLVEAGeeeedfKPFPTLLEALtKVDPDVGFNVEVKYPMMQNNGEHEC 565
Cdd:pfam03009  56 ----YVRDLTLEELKRL-------DIGAGNSGPLSGER------VPFPTLEEVL-EFDWDVGFNIEIKIKPYVEAIAPEE 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759   566 -DHYFERNLFVDVILAdvmKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTPfqdqrtsTSMTAVNFAAG 644
Cdd:pfam03009 118 gLIVKDLLLSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRAYAEAD-------LLERAAAFAGA 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71994759   645 ADLLGVNFNSEDLLkdPMPVKKANEFGMVTFVWGEDldkKENINYFKKELGVDGVIYDRIGE 706
Cdd:pfam03009 188 PALLGEVALVDEAL--PDLVKRAHARGLVVHVWTVN---NEDEMKRLLELGVDGVITDRPDT 244
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 404-705 2.63e-53

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: 186.50  E-value: 2.63e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAG--NSYTKFAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFhvLVSVARRDglampppmtreqlds 481
Cdd:cd08606   5 IGHRGLGknTAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDF--LVSETGTD--------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 482 snldyheLPVKDLKLSQLKllmldHLSFPQKKENVKKLVEAGEEEEDF--KPFPTLLEALTKVDPDVGFNVEVKYPMMQN 559
Cdd:cd08606  68 -------VPIHDLTLEQFL-----HLSRMKYTVDFKKKGFKGNSRGHSiqAPFTTLEELLKKLPKSVGFNIELKYPMLHE 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 560 NGEHECDHY-FERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETqryTPFQDQRTSTSMTA 638
Cdd:cd08606 136 AEEEEVAPVaIELNAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGK---APDMDVRAASLQEA 212

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994759 639 VNFAAGADLLGVNFNSEDLLKDPMPVKKANEFGMVTFVWGEDLDKKENINyFKKELGVDGVIYDRIG 705
Cdd:cd08606 213 IRFAKQWNLLGLVSAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAK-TQVKAGVDAVIVDSVL 278
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 404-704 1.97e-51

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: 181.07  E-value: 1.97e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAG-----NSYTKFAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVsvarRDGLAMPPPMtreq 478
Cdd:cd08605   3 IGHRGLGmnrasHQPSVGPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVV----ERGGEVESSR---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 479 ldssnldyhelpVKDLKLSQLKLLMLDHLSFPQKKENVKKLVEAGEEE------EDfkPFPTLLEALTKVDPDVGFNVEV 552
Cdd:cd08605  75 ------------IRDLTLAELKALGPQAESTKTSTVALYRKAKDPEPEpwimdvED--SIPTLEEVFSEVPPSLGFNIEL 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 553 KYpmmqNNGEHECDHYFERNLfvDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTpfqDQRT 632
Cdd:cd08605 141 KF----GDDNKTEAEELVREL--RAILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHN---DPRR 211

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71994759 633 STSMTAVNFAAGADLLGVNFNSEDLLKDPMPVKKANEFGMVTFVWGEDLDKKENInYFKKELGVDGVIYDRI 704
Cdd:cd08605 212 NSIEAAIQVALEGGLQGIVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAV-ERQADLGVDGVIVDHV 282
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 84-207 2.74e-48

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 166.34  E-value: 2.74e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759  84 VRVHFAVDVENLHAHQSVYVVGSNDVLGTWEATRAMPLVQDPDRFMRWKGSIVTD-VHQLKFRYFIGYNLMSDQGERLIV 162
Cdd:cd05814   1 CRVTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDDDCNLWKASIELPrGVDFQYRYFVAVVLNDSGPCQVIV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71994759 163 DKWEAFLHPRSTLCLaesrnDECRVDRVDLFGYYAGRKCVSDGWL 207
Cdd:cd05814  81 RKWETHLQPRSIKPL-----EEERLNDDDKFGIYDGVEQVDRGWL 120
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
404-706 9.79e-31

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 121.13  E-value: 9.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLvSVARRDGlampppmtreqldssn 483
Cdd:COG0584   6 IAHRGAS------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLD-RTTNGTG---------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 ldyhelPVKDLKLSQLKLlmLDHLSFPQkkenvkklvEAGEeeedfkPFPTLLEALTKVDPDVGFNVEVKYPmmqnngeh 563
Cdd:COG0584  63 ------RVADLTLAELRQ--LDAGSGPD---------FAGE------RIPTLEEVLELVPGDVGLNIEIKSP-------- 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 564 ecdhYFERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCvgetqrytpfqdQRTSTSMTAVNFAA 643
Cdd:COG0584 112 ----PAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV------------EELPADPLELARAL 175

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994759 644 GADLLGVNFnseDLLKDPMpVKKANEFGMVTFVWGedLDKKENINYFkKELGVDGVIYDRIGE 706
Cdd:COG0584 176 GADGVGPDY---DLLTPEL-VAAAHAAGLKVHVWT--VNDPEEMRRL-LDLGVDGIITDRPDL 231
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 404-703 8.07e-25

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: 102.34  E-value: 8.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfhvlvsvarrdglampppmtreqldssn 483
Cdd:cd08556   2 IAHRGAS------GEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 ldyhelpvkdlklsqlkllmldhlsfpqkkenvkklveageeeedfkpFPTLLEALTKVDPDVGFNVEVKYPMMQNNgeh 563
Cdd:cd08556  48 ------------------------------------------------IPTLEEVLELVKGGVGLNIELKEPTRYPG--- 76

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 564 ecdhyfernlFVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLcvgetqrYTPFQDQRTSTSMTAvnfAA 643
Cdd:cd08556  77 ----------LEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLL-------VDKPPLDPLLAELAR---AL 136

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 644 GADLLGVNFnseDLLKDPMpVKKANEFGMVTFVWGedLDKKENINYFkKELGVDGVIYDR 703
Cdd:cd08556 137 GADAVNPHY---KLLTPEL-VRAAHAAGLKVYVWT--VNDPEDARRL-LALGVDGIITDD 189
CBM_2 smart01065
Starch binding domain;
84-175 6.26e-19

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 82.01  E-value: 6.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759     84 VRVHFAVDVENLHAHQSVYVVGSNDVLGTWEATRAMPLVQDPDRFMRWKGSIVTDVH--QLKFRYFIGYNLMsdqgerli 161
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAgtTIEYKYVKVDEDG-------- 72

                           90
                   ....*....|....
gi 71994759    162 VDKWEAFLHPRSTL 175
Cdd:smart01065  73 SVTWESGPNRRLTV 86
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 405-703 5.24e-16

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: 78.89  E-value: 5.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 405 GHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLVSVARRDGLAMPPPmtrEQLDSSNL 484
Cdd:cd08567   5 GHRGAR------GLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLPY---EGPALYEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 485 DYHElpVKDLKLSQLKLLMLDHLSFP-QKKENVKKLveageeeedfkpfPTLLEALTKVDPDVG----FNVEVKYPMMQn 559
Cdd:cd08567  76 TLAE--IKQLDVGEKRPGSDYAKLFPeQIPVPGTRI-------------PTLEEVFALVEKYGNqkvrFNIETKSDPDR- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 560 ngehecDHYF-ERNLFVDVILADVMKHAGNRRIMFSSFDPDICSMVatkQNKYPVLflcvgetqRYTPFQDQRTSTSMTA 638
Cdd:cd08567 140 ------DILHpPPEEFVDAVLAVIRKAGLEDRVVLQSFDWRTLQEV---RRLAPDI--------PTVALTEETTLGNLPR 202

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994759 639 VNFAAGADLLGVNFNsedlLKDPMPVKKANEFGMVTFVWGedLDKKENINYFkKELGVDGVIYDR 703
Cdd:cd08567 203 AAKKLGADIWSPYFT----LVTKELVDEAHALGLKVVPWT--VNDPEDMARL-IDLGVDGIITDY 260
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 404-703 1.41e-14

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: 73.89  E-value: 1.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAgnSYTkfamARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLvsvarrdglampppMTreqldsSN 483
Cdd:cd08582   2 IAHRGA--SAE----APENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLK--------------RT------SG 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 LDyheLPVKDLKLSQLKLLMLDhlsfpqkkeNVKKLVEAGEeeedfkPFPTLLEALTKV-DPDVGFNVEVKYPmmQNNGE 562
Cdd:cd08582  56 GD---GAVSDLTLAELRKLDIG---------SWKGESYKGE------KVPTLEEYLAIVpKYGKKLFIEIKHP--RRGPE 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 563 HEcdhyferNLFVDVILADVMKHAgnrRIMFSSFDPDICSMVATKQNKYPVLFLCvgetqrytPFQDQRTSTSMTAVN-F 641
Cdd:cd08582 116 AE-------EELLKLLKESGLLPE---QIVIISFDAEALKRVRELAPTLETLWLR--------NYKSPKEDPRPLAKSgG 177

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71994759 642 AAGADLLGVNFNSEDLlkdpmpVKKANEFGMVTFVWgeDLDKKENINYFkKELGVDGVIYDR 703
Cdd:cd08582 178 AAGLDLSYEKKLNPAF------IKALRDAGLKLNVW--TVDDAEDAKRL-IELGVDSITTNR 230
GDPD_NUC-2_fungi cd08578
Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and ...
 391-701 3.49e-14

Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and similar proteins; This subfamily corresponds to a putative glycerophosphodiester phosphodiesterase domain (GDPD) present in Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81. Some uncharacterized NUC-2 sequence homologs are also included in this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in Neurospora crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein PHO81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both NUC-2 and PHO81 have multi-domain architecture, including an SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal GDPD domain with unknown function. Although the putative GDPD domain displays sequence homology to that of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), the residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in members of this family, which suggests the function of putative GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs.


Pssm-ID: 176520  Cd Length: 300  Bit Score: 73.90  E-value: 3.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 391 TYcrhWKKRNALEVGHRGAGNSYTkfamarenTIHSLNtaakngADYVEFDVQLTKDRIAVIYHDFHVLVSVARrdglam 470
Cdd:cd08578   2 TY---WKSTSGSDTQANKDGNSFV--------TASSLS------GEYLRVKVCVLKDGTPVVAPEWFVPVGGIK------ 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 471 pppmtreqldssnldyheLPVKDLKLSQLKLLMLdhlsfpqkkENVKKLVEAGEEEEDFKP-----FPTLLEALTKVDPD 545
Cdd:cd08578  59 ------------------LLVSDLTAEQLESILD---------YSLDDLNSEISDMVDLKRllssrVVSLETLLELLPPS 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 546 VGFNVEVKYPMmqnngEHECDHYFER-------NLFVDVILADVMKHA-------GN-RRIMFSSFDPDICSMVATKQNK 610
Cdd:cd08578 112 IQLDIQVLFPT-----AAEIASIPVKgsplvdlNKFIDTVLLVVFDHArylrhtpGStRSIVFSSCNPEVCTILNWKQPN 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 611 YPVLF-----------LCVGETQRYTP---------FQDQRTSTSMTAVNFAAGADLLGVNFnSEDLLKdPMP-----VK 665
Cdd:cd08578 187 FPVFFamnglvrnndtLSFDTPHHLDSlavdpqklnEADPRSRSIKEAVRFAKNNNLLGLIL-PYSLLN-IVPqlvesIK 264

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 71994759 666 KAnefGMVTFVWGEDLDKKENInyfKKELGVDGVIY 701
Cdd:cd08578 265 SR---GLLLIASGEPESLIEVA---EAGDGINGVVT 294
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 404-704 1.66e-13

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: 71.35  E-value: 1.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGNSytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHdfhvlvsvARRDGLAmppPMTREQLDSSN 483
Cdd:cd08564   7 VGHRGAGCS----TLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFH--------GTEDDTN---PDTSIQLDDSG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 LDYhelpVKDLKLSQLKLLmldHLSFPQKKEnvkklvEAGEEEEDFKPFPTLLEALTKVDPDVGFNVEVKYPmmqNNGEH 563
Cdd:cd08564  72 FKN----INDLSLDEITRL---HFKQLFDEK------PCGADEIKGEKIPTLEDVLVTFKDKLKYNIELKGR---EVGLG 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 564 EcdhyfernlfvdVILADVMKHAGNRRIMFSSFD----PDICSMVATKQNKYPVLFLcvgetqrytpFQDQRTSTSMTAV 639
Cdd:cd08564 136 E------------RVLNLVEKYGMILQVHFSSFLhydrLDLLKALRPNKLNVPIALL----------FNEVKSPSPLDFL 193

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994759 640 NFAAGADLLGVNFNSEDLLKDpmPVKKANEFGMVTFVW--GEDLDKKENIN-YFkkELGVDGVIYDRI 704
Cdd:cd08564 194 EQAKYYNATWVNFSYDFWTEE--FVKKAHENGLKVMTYfdEPVNDNEEDYKvYL--ELGVDCICPNDP 257
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 404-703 3.13e-13

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: 69.50  E-value: 3.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRG-AGNsytkfamARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVlvsvarrdglampppmtreqldsS 482
Cdd:cd08579   2 IAHRGvSSN-------GVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANL-----------------------K 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 483 NLDYHELPVKDLKLSQLKLLmldhlsfpqkkenvkKLVEAGEEEedfkPFPTLLEALTKV-DPDVGFNVEVKYpmmqnNG 561
Cdd:cd08579  52 RLAGVNKKVWDLTLEELKKL---------------TIGENGHGA----KIPSLDEYLALAkGLKQKLLIELKP-----HG 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 562 EHECDhyFERNlFVDVILADVMKHagnrRIMFSSFDPDIcsmVATKQNKYPVLFlcVGetqrY-TPFqdQRTSTSMTAVN 640
Cdd:cd08579 108 HDSPD--LVEK-FVKLYKQNLIEN----QHQVHSLDYRV---IEKVKKLDPKIK--TG----YiLPF--NIGNLPKTNVD 169

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994759 641 FaagadllgvnFNSEDLLKDPMPVKKANEFGMVTFVWgeDLDKKENINYFKKeLGVDGVIYDR 703
Cdd:cd08579 170 F----------YSIEYSTLNKEFIRQAHQNGKKVYVW--TVNDPDDMQRYLA-MGVDGIITDY 219
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 404-703 4.55e-13

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: 70.77  E-value: 4.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfHVLVSVArrDGLAMPPPMTReqldsSN 483
Cdd:cd08559   4 IAHRGAS------GYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHD-PTLDRTT--NVAEHFPFRGR-----KD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 LDYhelPVKDLKLSQLKLLMLDHLSFPQKKENvkklveAGEEEEDFKpFPTLLEALTKVDP-------DVGFNVEVKYPm 556
Cdd:cd08559  70 TGY---FVIDFTLAELKTLRAGSWFNQRYPER------APSYYGGFK-IPTLEEVIELAQGlnkstgrNVGIYPETKHP- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 557 mqnngehecdhYFERNLFVDV--ILADVMKHAG----NRRIMFSSFDPDICSMVATKQNKYPVLFLcVGETQRYTPFQDQ 630
Cdd:cd08559 139 -----------TFHKQEGPDIeeKLLEVLKKYGytgkNDPVFIQSFEPESLKRLRNETPDIPLVQL-IDYGDWAETDKKY 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 631 RTSTSMTAVNF---AAGADLLG------VNFNSEDLLKDPMPVKKANEFGMV----TF-------VWGEDLDKKENINYf 690
Cdd:cd08559 207 TYAWLTTDAGLkeiAKYADGIGpwksliIPEDSNGLLVPTDLVKDAHKAGLLvhpyTFrnenlflAPDFKQDMDALYNA- 285

                       330
                ....*....|...
gi 71994759 691 kkeLGVDGVIYDR 703
Cdd:cd08559 286 ---AGVDGVFTDF 295
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 404-455 2.12e-12

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: 68.05  E-value: 2.12e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71994759 404 VGHRGAGNSytkfamARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:cd08573   2 IGHRGAGHD------APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHD 47
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 406-600 3.70e-12

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: 67.24  E-value: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 406 HRGagnsytkfaMAR---ENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLvsvaRRDGLAMpppmtreqldss 482
Cdd:cd08575   6 HRG---------GAAefpENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLD----RLTGGSG------------ 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 483 nldyhelPVKDLKLSQLKLLmldhlsfpQKKENVKKLVEAGEEEEDFKP--FPTLLEALTKVdPDVGFNVEVKYPmmqNN 560
Cdd:cd08575  61 -------LVSDLTYAELPPL--------DAGYGYTFDGGKTGYPRGGGDgrIPTLEEVFKAF-PDTPINIDIKSP---DA 121

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 71994759 561 GEhecdhyfernlFVDVILADVMKHAGNRRIMFSSFDPDI 600
Cdd:cd08575 122 EE-----------LIAAVLDLLEKYKREDRTVWGSTNPEY 150
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 404-703 1.54e-11

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: 65.42  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAgnSYtkfaMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfhvlvsvarrdglampppmtrEQLD-SS 482
Cdd:cd08601   4 IAHRGA--SG----YAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHD---------------------ETLDrTT 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 483 NLDYHElPVKDLKLSQLKllMLDHLS-----FPQ--KKENVKKLVeageeeedfkpfPTLLEALTKVDPDVGFNVEVK-- 553
Cdd:cd08601  57 NIERPG-PVKDYTLAEIK--QLDAGSwfnkaYPEyaRESYSGLKV------------PTLEEVIERYGGRANYYIETKsp 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 554 --YPMMQNNGEHECDHYFernlfvdvILADVMKhagNRRIMFSSFDPDICSMVATKQNKYPVLFLC-VGETQRYTpfqDQ 630
Cdd:cd08601 122 dlYPGMEEKLLATLDKYG--------LLTDNLK---NGQVIIQSFSKESLKKLHQLNPNIPLVQLLwYGEGAETY---DK 187

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994759 631 RtstsmtaVNFAA-GADLLGVNFNsedlLKDPMPVKKANEFGMVT--FVWGEDLDKKENINYfkkelGVDGVIYDR 703
Cdd:cd08601 188 W-------LDEIKeYAIGIGPSIA----DADPWMVHLIHKKGLLVhpYTVNEKADMIRLINW-----GVDGMFTNY 247
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 405-702 2.07e-11

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: 64.24  E-value: 2.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 405 GHRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfhvlvSVARRDGlampppmtreqldssNL 484
Cdd:cd08568   4 GHRGYRAKYP------ENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHD-----ENLKRVG---------------GV 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 485 DYHelpVKDLKLSQLKLLMLDHlsfpqkkenvkklveageeeedfKPFPTLLEALTKVDPDVGFNVEVKypmmqnngehe 564
Cdd:cd08568  58 DLK---VKELTYKELKKLHPGG-----------------------ELIPTLEEVFRALPNDAIINVEIK----------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 565 cdhyfERNLfVDVILADVMKHAGNRRIMFSSFDPDICSMVATKQNKYPVLFLCVGETQRYTPFQDQRtSTSMTAVNFAag 644
Cdd:cd08568 101 -----DIDA-VEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEGFSIPELHE-KLKLYSLHVP-- 171

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71994759 645 ADLLGVnFNSEDLLKdpmPVKKANEFGMVTFVWgeDLDKKENINYFKKElgVDGVIYD 702
Cdd:cd08568 172 IDAIGY-IGFEKFVE---LLRLLRKLGLKIVLW--TVNDPELVPKLKGL--VDGVITD 221
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 405-702 4.78e-11

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: 63.34  E-value: 4.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 405 GHRGAgnSYTkfamARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFhvlvSVAR---RDGLampppmtreqlds 481
Cdd:cd08563   5 AHRGY--SGT----APENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDE----TVDRttnGKGY------------- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 482 snldyhelpVKDLKLSQLKllMLDHLSFpqKKENVKKlveageeeedfKPFPTLLEALTKVDP-DVGFNVEVK-----YP 555
Cdd:cd08563  62 ---------VKDLTLEELK--KLDAGSW--FDEKFTG-----------EKIPTLEEVLDLLKDkDLLLNIEIKtdvihYP 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 556 mmqnNGEHEcdhyfernlfvdvILADVMKHAGNRRIMFSSFDPDicSMVATKQ----NKYPVLFLcvgetqryTPFQDqr 631
Cdd:cd08563 118 ----GIEKK-------------VLELVKEYNLEDRVIFSSFNHE--SLKRLKKldpkIKLALLYE--------TGLQD-- 168

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71994759 632 tstsmtAVNFAAGADLLGVNFNSEDLLKDpmPVKKANEFGMVTFVWgeDLDKKENINYFKKeLGVDGVIYD 702
Cdd:cd08563 169 ------PKDYAKKIGADSLHPDFKLLTEE--VVEELKKRGIPVRLW--TVNEEEDMKRLKD-LGVDGIITN 228
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 405-703 4.97e-11

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: 63.82  E-value: 4.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 405 GHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfHVLVSVARRDGLamPPPMTREQLDSSNL 484
Cdd:cd08561   3 AHRGGA------GLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHD-ETLDRTTDGTGP--VADLTLAELRRLDA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 485 DYHELPvkdlklsqlkllmLDHLSFPQKKENVKklveageeeedfkpfPTLLEALTKVDPDVGFNVEVKypmmqnngehe 564
Cdd:cd08561  74 GYHFTD-------------DGGRTYPYRGQGIR---------------IPTLEELFEAFPDVRLNIEIK----------- 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 565 cdhyfERNLFVDVILADVMKHAGNR-RIMFSSFDPD-------ICSMVATkqnkypvlFLCVGETQRYtpfqdqrtstsM 636
Cdd:cd08561 115 -----DDGPAAAAALADLIERYGAQdRVLVASFSDRvlrrfrrLCPRVAT--------SAGEGEVAAF-----------V 170

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994759 637 TAVN------FAAGADLLGVNFNSEDL-LKDPMPVKKANEFGMVTFVWGEDlDKKENINYFkkELGVDGVIYDR 703
Cdd:cd08561 171 LASRlglgslYSPPYDALQIPVRYGGVpLVTPRFVRAAHAAGLEVHVWTVN-DPAEMRRLL--DLGVDGIITDR 241
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 404-613 5.74e-11

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: 63.12  E-value: 5.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfHVLVSVARRDGLAmpPPMTREQLDSSN 483
Cdd:cd08581   2 VAHRGYPARYP------ENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHD-DTLLRLTGVEGLL--HELEDAELDSLR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 LDYHELPVKdlklsqlkllmldhlSFPQkkenvkklveageeeedfKPFPTL---LEALTKvDPDVGFNVEVKypmmqnn 560
Cdd:cd08581  73 VAEPARFGS---------------RFAG------------------EPLPSLaavVQWLAQ-HPQVTLFVEIK------- 111

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71994759 561 geHECDHYFERNLFVDVILADVMKHAGNRRIMfsSFDPDICSmVATKQNKYPV 613
Cdd:cd08581 112 --TESLDRFGLERVVDKVLRALPAVAAQRVLI--SFDYDLLA-LAKQQGGPRT 159
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 404-455 2.23e-10

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: 61.65  E-value: 2.23e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71994759 404 VGHRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:cd08565   2 AGHRGGRNLWP------ENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHD 47
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 404-455 5.54e-10

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: 60.31  E-value: 5.54e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:cd08562   2 IAHRGAS------SLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHD 47
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 404-455 1.47e-09

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: 59.16  E-value: 1.47e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71994759 404 VGHRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:cd08570   2 IGHRGYKAKYP------ENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHD 47
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 404-677 6.63e-08

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: 54.25  E-value: 6.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAgnsYTKFAMARENTIHSLNTAAKngADY-VEFDVQLTKDRIAVIYHDfhvlvsvarrDGLAMpppMTREQLDSS 482
Cdd:cd08585   7 IAHRGL---HDRDAGIPENSLSAFRAAAE--AGYgIELDVQLTADGEVVVFHD----------DNLKR---LTGVEGRVE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 483 NLDYHElpvkdlkLSQLKLLmldhlsfpqkkenvkklveaGEEEedfkPFPTLLEALTKVDPDVGFNVEVKypmmqnnGE 562
Cdd:cd08585  69 ELTAAE-------LRALRLL--------------------GTDE----HIPTLDEVLELVAGRVPLLIELK-------SC 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 563 HECDHYFERnlfvdVILADVMKHAGNRRIMfsSFDPDicSMVATKQNKYPVLflcVGET-QRYTPFQDQRTSTSMTAV-- 639
Cdd:cd08585 111 GGGDGGLER-----RVLAALKDYKGPAAIM--SFDPR--VVRWFRKLAPGIP---RGQLsEGSNDEADPAFWNEALLSal 178

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71994759 640 --NFAAGADLLGVNFnseDLLKDPMPVKKANEFGMVTFVW 677
Cdd:cd08585 179 fsNLLTRPDFIAYHL---DDLPNPFVTLARALLGMPVIVW 215
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 392-601 1.88e-07

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: 53.37  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 392 YCRHwkkrnaleVGHRG-AGNSYtkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLvsvaRrdglam 470
Cdd:cd08612  26 PCRH--------ISHRGgSGENL-------ENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLL----R------ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 471 pppMTREQLDSSNLDYHELPVKDLKLSqlkllmldhLSFPQKKENVKKlveageeEEDfKPFPtLLEALTKVDPDVGFNV 550
Cdd:cd08612  81 ---SCGVDKLVSDLNYADLPPYLEKLE---------VTFSPGDYCVPK-------GSD-RRIP-LLEEVFEAFPDTPINI 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71994759 551 EVKYPmmqnngehecdhyfeRNLFVDVILADVMKHAGNRRIMFSSFDPDIC 601
Cdd:cd08612 140 DIKVE---------------NDELIKKVSDLVRKYKREDITVWGSFNDEIV 175
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 404-703 2.18e-07

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: 51.67  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGNSYtkfamaRENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfhvlvsvarrdglampPPMTREQLDSSN 483
Cdd:cd08555   2 LSHRGYSQNG------QENTLEAFYRALDAGARGLELDVRLTKDGELVVYHG----------------PTLDRTTAGILP 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 LDYHElpvkdlklsqlkllmldhlsfpqkkenvkklveageeeedfkPFPTLLEALTKVDPDVGFNVEVKYPMMQNNGeh 563
Cdd:cd08555  60 PTLEE------------------------------------------VLELIADYLKNPDYTIILSLEIKQDSPEYDE-- 95

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 564 ecdhyfernlFVDVILADVMKHAGNR---RIMFSSFDpdicsmvatkqnkypvlflcvgetqrytpfqdqrtstsmtavn 640
Cdd:cd08555  96 ----------FLAKVLKELRVYFDYDlrgKVVLSSFN------------------------------------------- 122

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71994759 641 fAAGADLLgvNFnSEDLLKDPMPVKKANEFGMVTFVWGEDlDKKENINYFKKeLGVDGVIYDR 703
Cdd:cd08555 123 -ALGVDYY--NF-SSKLIKDTELIASANKLGLLSRIWTVN-DNNEIINKFLN-LGVDGLITDF 179
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 404-612 2.44e-07

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: 52.69  E-value: 2.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGNsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFhvlvSVARrdglampppMTreqldssn 483
Cdd:cd08566   3 VAHRGGWG-----AGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDD----TLDR---------TT-------- 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 lDYHElPVKDLKLSQLKLLmldhlsfpqkkenvkKLVEAGEEEEDFKPfPTLLEALTKVDPDVGFNVEVKYPMMQNngeh 563
Cdd:cd08566  57 -NGKG-KVSDLTLAEIRKL---------------RLKDGDGEVTDEKV-PTLEEALAWAKGKILLNLDLKDADLDE---- 114

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71994759 564 ecdhyfernlfvdviLADVMKHAGN-RRIMFSSFDPDICSMVATKQNKYP 612
Cdd:cd08566 115 ---------------VIALVKKHGAlDQVIFKSYSEEQAKELRALAPEVM 149
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 85-148 6.11e-07

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 48.09  E-value: 6.11e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994759  85 RVHFAVDVENLHAHQSVYVVGSNDVLGTWEATRAMPLVqdPDRFMRWKGSIV--TDVHQLKFRYFI 148
Cdd:cd05816   1 VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKALKLS--DVGFPIWEADIDisKDSFPFEYKYII 64
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 404-702 1.04e-06

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: 51.24  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGNSYTkfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfHVLVSV----------ARRDGlamppp 473
Cdd:cd08600   4 IAHRGASGYLP------EHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHD-HYLDNVtnvaekfpdrKRKDG------ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 474 mtreqldssnlDYHelpVKDLKLSQLKLLML---------DHLS-----FPQKKENVKklVEAGEEEEDFkpfptlLEAL 539
Cdd:cd08600  71 -----------RYY---VIDFTLDELKSLSVterfdiengKKVQvypnrFPLWKSDFK--IHTLEEEIEL------IQGL 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 540 TKV-DPDVGFNVEVKYPMM-QNNGEHecdhyfernlfVDVILADVMKHAG----NRRIMFSSFDPDICSMVATKQN-KYP 612
Cdd:cd08600 129 NKStGKNVGIYPEIKAPWFhHQEGKD-----------IAAATLEVLKKYGytskNDKVYLQTFDPNELKRIKNELLpKMG 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 613 VLFLCV--------GETQRYTPFQDQ-------RTSTSMTAVnfAAGAD--------LLGVNFNSEDLLKDPMpVKKANE 669
Cdd:cd08600 198 MDLKLVqliaytdwGETQEKDPGGWVnydydwmFTKGGLKEI--AKYADgvgpwysmIIEEKSSKGNIVLTDL-VKDAHE 274

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 71994759 670 FGMV----TF------VWGEDLDKKENINYFKkeLGVDGVIYD 702
Cdd:cd08600 275 AGLEvhpyTVrkdalpEYAKDADQLLDALLNK--AGVDGVFTD 315
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 421-455 1.05e-06

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: 51.21  E-value: 1.05e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 71994759 421 ENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:cd08613  60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHD 94
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 404-454 2.30e-06

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: 50.02  E-value: 2.30e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYH 454
Cdd:cd08580   4 VAHRGGT------ADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYR 48
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 404-455 5.42e-06

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 48.40  E-value: 5.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71994759  404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:PRK09454  11 VAHRGGG------KLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHD 56
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 404-563 1.62e-05

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: 47.61  E-value: 1.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFHVLvsvaRRDGLAMPPPmTREQLDSSN 483
Cdd:cd08609  30 VGHRGAP------MLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLL----RTTNVKDVFP-GRDAAGSNN 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759 484 LDYHELpvKDLKLSQlklLMLDHLSFPqkkeNVKKLVEAGEEEEDFKPFPTLLEALtkvDPDVGFNVEVKYPMMQNNGEH 563
Cdd:cd08609  99 FTWTEL--KTLNAGS---WFLERRPFW----TLSSLSEEDRREADNQTVPSLSELL---DLAKKHNVSIMFDLRNENNSH 166
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 85-166 1.88e-05

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 43.83  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759  85 RVHFAVDVEnLHAHQSVYVVGSNDVLGTWEATRAMPLvQDPDRFMRWKGSIVTDVHQ---LKFRYFIgynlmSDQGERLI 161
Cdd:cd05467   1 QVRFQVRCT-TQFGQSVYVVGSHPELGNWDPAKALRL-NTSNSYPLWTGEIPLPAPEgqvIEYKYVI-----VDDDGNVQ 73


                ....*
gi 71994759 162 vdkWE 166
Cdd:cd05467  74 ---WE 75
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 404-457 3.55e-04

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: 43.06  E-value: 3.55e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71994759 404 VGHRGAgnsytkfAM-ARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDFH 457
Cdd:cd08574   5 IGHRGA-------PMlAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRT 52
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 393-467 8.08e-04

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 42.35  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994759  393 CRHWKKRNA--LEVGHRGAgNSYTKfamarENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDfHVLVSV-------- 462
Cdd:PRK11143  17 SAAAAADSAekIVIAHRGA-SGYLP-----EHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHD-HYLDRVtdvaerfp 89


                 ....*..
gi 71994759  463 --ARRDG 467
Cdd:PRK11143  90 drARKDG 96
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 397-469 8.80e-04

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show 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: 176503  Cd Length: 356  Bit Score: 42.41  E-value: 8.80e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71994759 397 KKRNALEVGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYH---DFHVLVSVARRDGLA 469
Cdd:cd08560  13 FRKTDFSIGHRGAP------LQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHsqcDLHTTTNILAIPELA 82
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 99-135 3.16e-03

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 37.77  E-value: 3.16e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 71994759  99 QSVYVVGSNDVLGTWEATRAMPLvqDPDRFMRWKGSI 135
Cdd:cd05810  16 QSVYVVGNVPQLGNWSPADAVKL--DPTAYPTWSGSI 50
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 404-456 7.14e-03

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: 39.47  E-value: 7.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHDF 456
Cdd:cd08610  26 IGHRGAP------MLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDF 72
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 404-455 7.21e-03

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: 39.20  E-value: 7.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71994759 404 VGHRGAGnsytkfAMARENTIHSLNTAAKNGADYVEFDVQLTKDRIAVIYHD 455
Cdd:cd08602   4 IAHRGAS------GYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHE 49
 
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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