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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGD-IESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYE 343
Cdd:cd08566     4 AHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTN---------------GKGKVSDLTLA 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391421944 344 QLCQLRLRTGNGeysaadsEITEYIIPTLKEAFMVCNERSLLVLDRVTTShWDKIYEIIKETKAY-RCFTYS 414
Cdd:cd08566    69 EIRKLRLKDGDG-------EVTDEKVPTLEEALAWAKGKILLNLDLKDAD-LDEVIALVKKHGALdQVIFKS 132

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGD-IESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYE 343
Cdd:cd08566     4 AHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTN---------------GKGKVSDLTLA 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391421944 344 QLCQLRLRTGNGeysaadsEITEYIIPTLKEAFMVCNERSLLVLDRVTTShWDKIYEIIKETKAY-RCFTYS 414
Cdd:cd08566    69 EIRKLRLKDGDG-------EVTDEKVPTLEEALAWAKGKILLNLDLKDAD-LDEVIALVKKHGALdQVIFKS 132

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 266 HRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYEQL 345
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTD---------------GAGYVRDLTLEEL 65

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1391421944 346 cqLRLRTGNGEYSAADSEIteYIIPTLKEAFMVC 379
Cdd:pfam03009  66 --KRLDIGAGNSGPLSGER--VPFPTLEEVLEFD 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGD-IESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYE 343
Cdd:cd08566     4 AHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTN---------------GKGKVSDLTLA 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391421944 344 QLCQLRLRTGNGeysaadsEITEYIIPTLKEAFMVCNERSLLVLDRVTTShWDKIYEIIKETKAY-RCFTYS 414
Cdd:cd08566    69 EIRKLRLKDGDG-------EVTDEKVPTLEEALAWAKGKILLNLDLKDAD-LDEVIALVKKHGALdQVIFKS 132

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 266 HRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYEQL 345
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTD---------------GAGYVRDLTLEEL 65

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1391421944 346 cqLRLRTGNGEYSAADSEIteYIIPTLKEAFMVC 379
Cdd:pfam03009  66 --KRLDIGAGNSGPLSGER--VPFPTLEEVLEFD 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYEQ 344
Cdd:cd08573     3 GHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTD---------------GTGLVAELTWEE 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 345 LCQLRLRTGNGEYSAADSEiteyIIPTLKEAFMVCNERSLLVLDRVtTSHWDKIYEIIKE 404
Cdd:cd08573    68 LRKLNAAAKHRLSSRFPGE----KIPTLEEAVKECLENNLRMIFDV-KSNSSKLVDALKN 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDlsvttdwaLKRgetLNGIklpmSSSISAWTYEQ 344
Cdd:cd08579     3 AHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDAN--------LKR---LAGV----NKKVWDLTLEE 67

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1391421944 345 LCQLRLRT-GNGEYsaadseiteyiIPTLKEAFMVCN 380
Cdd:cd08579    68 LKKLTIGEnGHGAK-----------IPSLDEYLALAK 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHgedlsvttDWALKRgeTLNGiklpmSSSISAWTYEQ 344
Cdd:cd08582     3 AHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVH--------DPTLKR--TSGG-----DGAVSDLTLAE 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391421944 345 LCQLRLRTGNGEYSAADSeiteyiIPTLKEAFMVCNErsllvldrvttshWDKiyEIIKETKAYRC 410
Cdd:cd08582    68 LRKLDIGSWKGESYKGEK------VPTLEEYLAIVPK-------------YGK--KLFIEIKHPRR 112

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1391421944 263 CYAHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMH 308
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIH 46

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDWALKRGETLNGiKLPMsssisawtyeQ 344
Cdd:cd08612    31 SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYA-DLPP----------Y 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1391421944 345 LCQLRLRTGNGEYSAADSEITEyiIPTLKEAF 376
Cdd:cd08612   100 LEKLEVTFSPGDYCVPKGSDRR--IPLLEEVF 129

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDWALK---RGETLNGIKlpmsssISAWT 341
Cdd:cd08559     5 AHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHfpfRGRKDTGYF------VIDFT 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1391421944 342 YEQLCQLRLRTGNGEYSA--ADSEITEYIIPTLKE 374
Cdd:cd08559    79 LAELKTLRAGSWFNQRYPerAPSYYGGFKIPTLEE 113

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 266 HRGDIESY--------PENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDWALKRGEtlngiKLPMSSSI 337
Cdd:cd08572     5 HRGLGKNYasgslagiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDE-----GELIEVPI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391421944 338 SAWTYEQLCQLRLRTGNGEYSAADSEITEY------------IIPTLKEAF 376
Cdd:cd08572    80 HDLTLEQLKELGLQHISALKRKALTRKAKGpkpnpwgmdehdPFPTLQEVL 130

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 260 RPMCYAHRGDIES--YPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHG--EDLSVTTDWALKRGETLNGIKLpmss 335
Cdd:cd08564     3 RPIIVGHRGAGCStlYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGteDDTNPDTSIQLDDSGFKNINDL---- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1391421944 336 sisawTYEQLCQLRLRTGNGEYSAADSEITEYIIPTLKEAFMVCNE 381
Cdd:cd08564    79 -----SLDEITRLHFKQLFDEKPCGADEIKGEKIPTLEDVLVTFKD 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalkrgetlngiklpMSSSISAWTYEQ 344
Cdd:cd08565     3 GHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTH---------------GTGAVRDLTLAE 67

                          90       100       110
                  ....*....|....*....|....*....|
gi 1391421944 345 LCQLRLRTGNGEYsaadseiteyiIPTLKE 374
Cdd:cd08565    68 RKALRLRDSFGEK-----------IPTLEE 86

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 266 HRGDIESY-------PENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTDwalKRGETLNGIKLPMssSIS 338
Cdd:cd08607     5 HRGAGNSYtaasavvRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLK---SKGDSDRDDLLEV--PVK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1391421944 339 AWTYEQLCQLRL----RTGNGEYSAADSEITEY---IIPTLKEAF 376
Cdd:cd08607    80 DLTYEQLKLLKLfhisALKVKEYKSVEEDEDPPehqPFPTLSDVL 124

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 265 AHRGDIE-----------SYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVttdwalKRGETLNgiklpm 333
Cdd:cd08605     4 GHRGLGMnrashqpsvgpGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVV------ERGGEVE------ 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391421944 334 SSSISAWTYEQLCQLRLRTGNGEYS-------AADSEITEYI------IPTLKEAF 376
Cdd:cd08605    72 SSRIRDLTLAELKALGPQAESTKTStvalyrkAKDPEPEPWImdvedsIPTLEEVF 127

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391421944 259 ARPmcYAHRG------DIesyPENSIEAVISAVKKGADmIELDVCMTRDKVLVLMHgedlsvttDWALKRgetLNGIKLP 332
Cdd:cd08585     4 DRP--IAHRGlhdrdaGI---PENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFH--------DDNLKR---LTGVEGR 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391421944 333 MSSSisawTYEQLCQLRLRtGNGEYsaadseiteyiIPTLKEAFMVCNERSLLVLD 388
Cdd:cd08585    67 VEEL----TAAELRALRLL-GTDEH-----------IPTLDEVLELVAGRVPLLIE 106

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTD 317
Cdd:cd08555     3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA 55

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1391421944 265 AHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTD 317
Cdd:PRK09454   12 AHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN 64

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1391421944 260 RPMCYAHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTD 317
Cdd:cd08610    22 KPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79

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.

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gi 1391421944 260 RPMCYAHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTD 317
Cdd:cd08574     1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTN 58

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.

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gi 1391421944 261 PMCYAHRGDIESYPENSIEAVISAVKKGADMIELDVCMTRDKVLVLMHGEDLSVTTD 317
Cdd:cd08604     1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTT 57