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Conserved domains on  [gi|2225715120|ref|WP_245723941|]
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glycerophosphodiester phosphodiesterase family protein [Pedobacter steynii]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 39-300 4.17e-93

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


The actual alignment was detected with superfamily member cd08567:

Pssm-ID: 472694 [Multi-domain]  Cd Length: 263  Bit Score: 276.50  E-value: 4.17e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  39 EGHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISksdARKYAVFQMDYVAL 118
Cdd:cd08567     4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLP---YEGPALYELTLAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 119 KQFDLGSK-----YYEAFPQQKKMK-SYIPRLGELIDAVqqylKKAGKKQIFYNIETKCSPEGDGlLNPDPETFVQLLMD 192
Cdd:cd08567    81 KQLDVGEKrpgsdYAKLFPEQIPVPgTRIPTLEEVFALV----EKYGNQKVRFNIETKSDPDRDI-LHPPPEEFVDAVLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 193 VIEKKGIQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANK--KSFEENIADLGFNpfILSPMYQMVNAELIKKCHEQQIK 270
Cdd:cd08567   156 VIRKAGLEDRVVLQSFDWRTLQEVRRLAPDIPTVALTEETtlGNLPRAAKKLGAD--IWSPYFTLVTKELVDEAHALGLK 233

                         250       260       270
                  ....*....|....*....|....*....|
gi 2225715120 271 VIPWTVNTAKEITELKALNVDGIISDYPDL 300
Cdd:cd08567   234 VVPWTVNDPEDMARLIDLGVDGIITDYPDL 263
 
Name Accession Description Interval E-value
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 39-300 4.17e-93

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: 276.50  E-value: 4.17e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  39 EGHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISksdARKYAVFQMDYVAL 118
Cdd:cd08567     4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLP---YEGPALYELTLAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 119 KQFDLGSK-----YYEAFPQQKKMK-SYIPRLGELIDAVqqylKKAGKKQIFYNIETKCSPEGDGlLNPDPETFVQLLMD 192
Cdd:cd08567    81 KQLDVGEKrpgsdYAKLFPEQIPVPgTRIPTLEEVFALV----EKYGNQKVRFNIETKSDPDRDI-LHPPPEEFVDAVLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 193 VIEKKGIQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANK--KSFEENIADLGFNpfILSPMYQMVNAELIKKCHEQQIK 270
Cdd:cd08567   156 VIRKAGLEDRVVLQSFDWRTLQEVRRLAPDIPTVALTEETtlGNLPRAAKKLGAD--IWSPYFTLVTKELVDEAHALGLK 233

                         250       260       270
                  ....*....|....*....|....*....|
gi 2225715120 271 VIPWTVNTAKEITELKALNVDGIISDYPDL 300
Cdd:cd08567   234 VVPWTVNDPEDMARLIDLGVDGIITDYPDL 263
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
40-301 2.22e-67

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 210.11  E-value: 2.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPafmldpqgqeisKSDARKyAVFQMDYVALK 119
Cdd:COG0584     7 AHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDR------------TTNGTG-RVADLTLAELR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSkyYEAFPQQKkmksyIPRLGELIDAVqqylkkagKKQIFYNIETKCSPEgdgllnpDPETFVQLLMDVIEKKGI 199
Cdd:COG0584    74 QLDAGS--GPDFAGER-----IPTLEEVLELV--------PGDVGLNIEIKSPPA-------AEPDLAEAVAALLKRYGL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKSFEENIADlGFNPFILSPMYQMVNAELIKKCHEQQIKVIPWTVNTA 279
Cdd:COG0584   132 EDRVIVSSFDPEALRRLRELAPDVPLGLLVEELPADPLELAR-ALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDP 210

                         250       260
                  ....*....|....*....|..
gi 2225715120 280 KEITELKALNVDGIISDYPDLL 301
Cdd:COG0584   211 EEMRRLLDLGVDGIITDRPDLL 232
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 41-300 1.12e-28

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: 110.18  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFmldpqgqeisksDARKYaVFQMDYVALKQ 120
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTT------------DGAGY-VRDLTLEELKR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 121 FDLGSKYYEAFPQQkkmKSYIPRLGELIDAVQQYLKKAGKKQIFYN--IETKCSPEGDgllnpdpeTFVQLLMDVIEKKG 198
Cdd:pfam03009  68 LDIGAGNSGPLSGE---RVPFPTLEEVLEFDWDVGFNIEIKIKPYVeaIAPEEGLIVK--------DLLLSVDEILAKKA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 199 IQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANK-----KSFEENIADLGFNPFILSPM-YQMVNAELIKKCHEQQIKVI 272
Cdd:pfam03009 137 DPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRayaeaDLLERAAAFAGAPALLGEVAlVDEALPDLVKRAHARGLVVH 216

                         250       260
                  ....*....|....*....|....*...
gi 2225715120 273 PWTVNTAKEITELKALNVDGIISDYPDL 300
Cdd:pfam03009 217 VWTVNNEDEMKRLLELGVDGVITDRPDT 244
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 27-300 9.63e-09

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 55.83  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  27 MTTTAQFPAFSNE----GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISK 102
Cdd:PRK11143   14 LAGSAAAAADSAEkiviAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERFPDRAR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 103 SDARKYAV-FQMDYV-ALK---QFDL-GSKYYEAFPQQKKM-KSY--IPRLGELIDAVQQYLKKAGKKQIFYnIETKcSP 173
Cdd:PRK11143   94 KDGRYYAIdFTLDEIkSLKfteGFDIeNGKKVQVYPGRFPMgKSDfrVHTFEEEIEFIQGLNHSTGKNIGIY-PEIK-AP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 174 -----EGdgllnpdpETFVQLLMDVIEKKGIQQ---FVVIQSFDKRTLQVLHKK-YPQM----KTSYLVA---------- 230
Cdd:PRK11143  172 wfhhqEG--------KDIAAKVLEVLKKYGYTGkddKVYLQCFDANELKRIKNElEPKMgmdlKLVQLIAytdwnetqek 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 231 NKKSFEENIA-DLGFNPFILS----------PMYQMVNAE-----------LIKKCHEQQIKVIPWTVNT------AKEI 282
Cdd:PRK11143  244 QPDGKWVNYNyDWMFKPGAMKevakyadgigPDYHMLVDEtstpgnikltgMVKEAHQAKLVVHPYTVRAdqlpeyATDV 323

                         330       340
                  ....*....|....*....|...
gi 2225715120 283 TEL-----KALNVDGIISDYPDL 300
Cdd:PRK11143  324 NQLydilyNQAGVDGVFTDFPDK 346
 
Name Accession Description Interval E-value
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 39-300 4.17e-93

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: 276.50  E-value: 4.17e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  39 EGHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISksdARKYAVFQMDYVAL 118
Cdd:cd08567     4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLP---YEGPALYELTLAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 119 KQFDLGSK-----YYEAFPQQKKMK-SYIPRLGELIDAVqqylKKAGKKQIFYNIETKCSPEGDGlLNPDPETFVQLLMD 192
Cdd:cd08567    81 KQLDVGEKrpgsdYAKLFPEQIPVPgTRIPTLEEVFALV----EKYGNQKVRFNIETKSDPDRDI-LHPPPEEFVDAVLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 193 VIEKKGIQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANK--KSFEENIADLGFNpfILSPMYQMVNAELIKKCHEQQIK 270
Cdd:cd08567   156 VIRKAGLEDRVVLQSFDWRTLQEVRRLAPDIPTVALTEETtlGNLPRAAKKLGAD--IWSPYFTLVTKELVDEAHALGLK 233

                         250       260       270
                  ....*....|....*....|....*....|
gi 2225715120 271 VIPWTVNTAKEITELKALNVDGIISDYPDL 300
Cdd:cd08567   234 VVPWTVNDPEDMARLIDLGVDGIITDYPDL 263
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
40-301 2.22e-67

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 210.11  E-value: 2.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPafmldpqgqeisKSDARKyAVFQMDYVALK 119
Cdd:COG0584     7 AHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDR------------TTNGTG-RVADLTLAELR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSkyYEAFPQQKkmksyIPRLGELIDAVqqylkkagKKQIFYNIETKCSPEgdgllnpDPETFVQLLMDVIEKKGI 199
Cdd:COG0584    74 QLDAGS--GPDFAGER-----IPTLEEVLELV--------PGDVGLNIEIKSPPA-------AEPDLAEAVAALLKRYGL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKSFEENIADlGFNPFILSPMYQMVNAELIKKCHEQQIKVIPWTVNTA 279
Cdd:COG0584   132 EDRVIVSSFDPEALRRLRELAPDVPLGLLVEELPADPLELAR-ALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDP 210

                         250       260
                  ....*....|....*....|..
gi 2225715120 280 KEITELKALNVDGIISDYPDLL 301
Cdd:COG0584   211 EEMRRLLDLGVDGIITDRPDLL 232
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 40-301 1.78e-44

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: 151.64  E-value: 1.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDylspafMLDPqgqeisKSDARKyAVFQMDYVALK 119
Cdd:cd08561     3 AHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDE------TLDR------TTDGTG-PVADLTLAELR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLG---SKYYEAFPQQKKMKSYIPRLGELIDAvqqylkkagkkqiF----YNIETKcspegdgllnPDPETFVQLLMD 192
Cdd:cd08561    70 RLDAGyhfTDDGGRTYPYRGQGIRIPTLEELFEA-------------FpdvrLNIEIK----------DDGPAAAAALAD 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 193 VIEKKGIQQFVVIQSFDKRTLQVLHKKYPQMKTS--------YLVANK---KSFEENIADlgfnpFILSPMYQM----VN 257
Cdd:cd08561   127 LIERYGAQDRVLVASFSDRVLRRFRRLCPRVATSagegevaaFVLASRlglGSLYSPPYD-----ALQIPVRYGgvplVT 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2225715120 258 AELIKKCHEQQIKVIPWTVNTAKEITELKALNVDGIISDYPDLL 301
Cdd:cd08561   202 PRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGVDGIITDRPDLL 245
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 40-297 1.50e-41

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: 142.02  E-value: 1.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDdylspafmldpqgqeisksdarkyavfqmdyvalk 119
Cdd:cd08556     3 AHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD----------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 qfdlgskyyeafpqqkkmksyIPRLGELIDAVqqylkkagKKQIFYNIETKCSPEGDGLlnpdpetfVQLLMDVIEKKGI 199
Cdd:cd08556    48 ---------------------IPTLEEVLELV--------KGGVGLNIELKEPTRYPGL--------EAKVAELLREYGL 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKS-FEENIADLGFNPFILSPMYQMVNAELIKKCHEQQIKVIPWTVNT 278
Cdd:cd08556    91 EERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLdPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVND 170

                         250
                  ....*....|....*....
gi 2225715120 279 AKEITELKALNVDGIISDY 297
Cdd:cd08556   171 PEDARRLLALGVDGIITDD 189
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 40-298 1.44e-40

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: 140.77  E-value: 1.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSpafmldpqgqeiSKSDARKYaVFQMDYVALK 119
Cdd:cd08563     5 AHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVD------------RTTNGKGY-VKDLTLEELK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSKYYEAFPQQKkmksyIPRLGELIDAVQqylkkagKKQIFYNIETKcspeGDGLLNPDPEtfvQLLMDVIEKKGI 199
Cdd:cd08563    72 KLDAGSWFDEKFTGEK-----IPTLEEVLDLLK-------DKDLLLNIEIK----TDVIHYPGIE---KKVLELVKEYNL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKSFEENIAdLGFNPFILSPMYQMVNAELIKKCHEQQIKVIPWTVNTA 279
Cdd:cd08563   133 EDRVIFSSFNHESLKRLKKLDPKIKLALLYETGLQDPKDYA-KKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEE 211

                         250
                  ....*....|....*....
gi 2225715120 280 KEITELKALNVDGIISDYP 298
Cdd:cd08563   212 EDMKRLKDLGVDGIITNYP 230
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 36-301 2.82e-37

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: 133.21  E-value: 2.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  36 FSNEGHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLspafmldpqgqEISKSDARKYAVFQMDY 115
Cdd:cd08601     1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETL-----------DRTTNIERPGPVKDYTL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 116 VALKQFDLGSKYYEAFPQQKKmKSY----IPRLGELIDAvqqYLKKAGkkqifYNIETKcSPEgdglLNPDPEtfvQLLM 191
Cdd:cd08601    70 AEIKQLDAGSWFNKAYPEYAR-ESYsglkVPTLEEVIER---YGGRAN-----YYIETK-SPD----LYPGME---EKLL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 192 DVIEKKGIQQF------VVIQSFDKRTLQVLHKKYPQMKTSYLVANKKSFEENIADLGF---NPFILSPMYQMVNAELIK 262
Cdd:cd08601   133 ATLDKYGLLTDnlkngqVIIQSFSKESLKKLHQLNPNIPLVQLLWYGEGAETYDKWLDEikeYAIGIGPSIADADPWMVH 212

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2225715120 263 KCHEQQIKVIPWTVNTAKEITELKALNVDGIISDYPDLL 301
Cdd:cd08601   213 LIHKKGLLVHPYTVNEKADMIRLINWGVDGMFTNYPDRL 251
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 40-298 1.85e-36

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: 129.97  E-value: 1.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLspafmldpqgQEISKSDARkyaVFQMDYVALK 119
Cdd:cd08579     3 AHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANL----------KRLAGVNKK---VWDLTLEELK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSKYYEAfpqqkkmksYIPRLgelidavQQYLKKAGKKQIFYNIETKCSPEgdgllnpDPETFVQLLMDVIEKKGI 199
Cdd:cd08579    70 KLTIGENGHGA---------KIPSL-------DEYLALAKGLKQKLLIELKPHGH-------DSPDLVEKFVKLYKQNLI 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLVA-NKKSFEENIADlgfnpfILSPMYQMVNAELIKKCHEQQIKVIPWTVNT 278
Cdd:cd08579   127 ENQHQVHSLDYRVIEKVKKLDPKIKTGYILPfNIGNLPKTNVD------FYSIEYSTLNKEFIRQAHQNGKKVYVWTVND 200

                         250       260
                  ....*....|....*....|
gi 2225715120 279 AKEITELKALNVDGIISDYP 298
Cdd:cd08579   201 PDDMQRYLAMGVDGIITDYP 220
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 41-300 4.82e-34

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: 123.96  E-value: 4.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLspafmldpqgQEISKSDArkyAVFQMDYVALKQ 120
Cdd:cd08582     4 HRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTL----------KRTSGGDG---AVSDLTLAELRK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 121 FDLGSKYYEAFPQQKkmksyIPRLGELIDAVqqylKKAGKKQIfynIETKCSPEGDGLlnpdpetfVQLLMDVIEKKGI- 199
Cdd:cd08582    71 LDIGSWKGESYKGEK-----VPTLEEYLAIV----PKYGKKLF---IEIKHPRRGPEA--------EEELLKLLKESGLl 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 -QQFVVIqSFDKRTLQVLHKKYPQMKTSYLVANK--KSFEENIADLGFNPFILSPMYQMVNAELIKKCHEQQIKVIPWTV 276
Cdd:cd08582   131 pEQIVII-SFDAEALKRVRELAPTLETLWLRNYKspKEDPRPLAKSGGAAGLDLSYEKKLNPAFIKALRDAGLKLNVWTV 209

                         250       260
                  ....*....|....*....|....
gi 2225715120 277 NTAKEITELKALNVDGIISDYPDL 300
Cdd:cd08582   210 DDAEDAKRLIELGVDSITTNRPGR 233
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 40-298 2.57e-30

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: 115.83  E-value: 2.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLS----PAFMLDPQGQEIsksdaRKYAVFQMDY 115
Cdd:cd08559     5 AHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDrttnVAEHFPFRGRKD-----TGYFVIDFTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 116 VALKQFDLGSKYYEAFPQQKKM---KSYIPRLGELIDAVQQYLKKAGKKqIFYNIETKcSPEGDGLLNPDPETfvqLLMD 192
Cdd:cd08559    80 AELKTLRAGSWFNQRYPERAPSyygGFKIPTLEEVIELAQGLNKSTGRN-VGIYPETK-HPTFHKQEGPDIEE---KLLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 193 VIEKKGIQ---QFVVIQSFDKRTLQVLHKKYPQMKTSYLVA--------NKKSFEENIADLGFNPF-----ILSPMYQMV 256
Cdd:cd08559   155 VLKKYGYTgknDPVFIQSFEPESLKRLRNETPDIPLVQLIDygdwaetdKKYTYAWLTTDAGLKEIakyadGIGPWKSLI 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225715120 257 NAE----------LIKKCHEQQIKVIPWTVNT----------AKEITELKALNVDGIISDYP 298
Cdd:cd08559   235 IPEdsngllvptdLVKDAHKAGLLVHPYTFRNenlflapdfkQDMDALYNAAGVDGVFTDFP 296
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 41-300 1.12e-28

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: 110.18  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFmldpqgqeisksDARKYaVFQMDYVALKQ 120
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTT------------DGAGY-VRDLTLEELKR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 121 FDLGSKYYEAFPQQkkmKSYIPRLGELIDAVQQYLKKAGKKQIFYN--IETKCSPEGDgllnpdpeTFVQLLMDVIEKKG 198
Cdd:pfam03009  68 LDIGAGNSGPLSGE---RVPFPTLEEVLEFDWDVGFNIEIKIKPYVeaIAPEEGLIVK--------DLLLSVDEILAKKA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 199 IQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANK-----KSFEENIADLGFNPFILSPM-YQMVNAELIKKCHEQQIKVI 272
Cdd:pfam03009 137 DPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRayaeaDLLERAAAFAGAPALLGEVAlVDEALPDLVKRAHARGLVVH 216

                         250       260
                  ....*....|....*....|....*...
gi 2225715120 273 PWTVNTAKEITELKALNVDGIISDYPDL 300
Cdd:pfam03009 217 VWTVNNEDEMKRLLELGVDGVITDRPDT 244
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 40-298 2.06e-27

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: 106.54  E-value: 2.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLspafmldpqgqeiSKSDARKYAVFQMDYVALK 119
Cdd:cd08562     3 AHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTL-------------DRTTNGSGAVTELTWAELA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSKYYEAFPqqkkmksyiprlGELIDAVQQYLKKAGKKQIFYNIETKCSPEGDGLLNPDPETFVQLLMDVIEKkgi 199
Cdd:cd08562    70 QLDAGSWFSPEFA------------GEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAALRELWPHASK--- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 qqfVVIQSFDKRTLQVLHKKYPQMKTSYLvankksFEENIAD-----LGFNPFILSPMYQMVNAELIKKCHEQQIKVIPW 274
Cdd:cd08562   135 ---LLLSSFSLEALRAARRAAPELPLGLL------FDTLPADwlellAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVY 205

                         250       260
                  ....*....|....*....|....
gi 2225715120 275 TVNTAKEITELKALNVDGIISDYP 298
Cdd:cd08562   206 TVNDPARAAELLEWGVDAIFTDRP 229
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-301 4.60e-25

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: 101.14  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSpaFMLDPQGqeisksdarkyAVFQMDYVALKQ 120
Cdd:cd08575     6 HRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLD--RLTGGSG-----------LVSDLTYAELPP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 121 FDLGSKYYeaFPQQKKMKSY------IPRLGELIDAVqqylkkagkKQIFYNIETKcspegdgllNPDPETFVQLLMDVI 194
Cdd:cd08575    73 LDAGYGYT--FDGGKTGYPRgggdgrIPTLEEVFKAF---------PDTPINIDIK---------SPDAEELIAAVLDLL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 195 EKKGIQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKSFEENIADLGFNPFI-------------------------L 249
Cdd:cd08575   133 EKYKREDRTVWGSTNPEYLRALHPENPNLFESFSMTRCLLLYLALGYTGLLPFVpikesffeiprpvivletftlgegaS 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2225715120 250 SPMYQMVNAELIKKCHEQQIKVIPWTVNTAKEITELKALNVDGIISDYPDLL 301
Cdd:cd08575   213 IVAALLWWPNLFDHLRKRGIQVYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 40-298 1.07e-23

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: 96.52  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFmlDPQGQEISKSDARKYAVFQMdyvaLK 119
Cdd:cd08570     3 GHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCF--GKDGLIIDDSTWDELSHLRT----IE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QfdlgskyyeafPQQKkmksyIPRLGELIDavqqYLKKAGKKQIFYNIETKcspegdgLLNPdPETFVQLLMDVIEKK-- 197
Cdd:cd08570    77 E-----------PHQP-----MPTLKDVLE----WLVEHELPDVKLMLDIK-------RDND-PEILFKLIAEMLAVKpd 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 198 --GIQQFVVIQSFDKRTLQVLHKKYPQMKTSY----LVANKKSFEENIADLGFNPFILSPMYQMVnAELIKKCHEQQIKV 271
Cdd:cd08570   129 ldFWRERIILGLWHLDFLKYGKEVLPGFPVFHigfsLDYARHFLNYSEKLVGISMHFVSLWGPFG-QAFLPELKKNGKKV 207

                         250       260
                  ....*....|....*....|....*..
gi 2225715120 272 IPWTVNTAKEITELKALNVDGIISDYP 298
Cdd:cd08570   208 FVWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 40-298 2.35e-23

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: 95.44  E-value: 2.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDpqgqeisksdarkYAVFQMDYVALK 119
Cdd:cd08568     4 GHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVD-------------LKVKELTYKELK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSKyyeafpqqkkmksYIPRLGELIDAVqqylkkagKKQIFYNIETKcspegdgllnpDPETfVQLLMDVIEKKGI 199
Cdd:cd08568    71 KLHPGGE-------------LIPTLEEVFRAL--------PNDAIINVEIK-----------DIDA-VEPVLEIVEKFNA 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKS-FEENIADLGFNPFILSPMYQMVNA-------ELIKKCHEQQIKV 271
Cdd:cd08568   118 LDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEgFSIPELHEKLKLYSLHVPIDAIGYigfekfvELLRLLRKLGLKI 197

                         250       260
                  ....*....|....*....|....*..
gi 2225715120 272 IPWTVNTAKEITELKALnVDGIISDYP 298
Cdd:cd08568   198 VLWTVNDPELVPKLKGL-VDGVITDDV 223
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-301 9.20e-22

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: 92.66  E-value: 9.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLspafmLDPQGQEISKSDarkyavfqMDYVALK- 119
Cdd:cd08612    32 HRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENL-----LRSCGVDKLVSD--------LNYADLPp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 -------QFDLGSKYYEAFPQQKkmksyIPRLGELIDAVqqylkkagkKQIFYNIETKcspegdgllNPDPEtFVQLLMD 192
Cdd:cd08612    99 yleklevTFSPGDYCVPKGSDRR-----IPLLEEVFEAF---------PDTPINIDIK---------VENDE-LIKKVSD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 193 VIEKKGIQQFVVIQSFDKRTLQVLHKKYPQMKTS-------------------YLVANKKSFE------ENIADLGFNPF 247
Cdd:cd08612   155 LVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFfslkrvllllllyytgllpFIPIKESFLEipmpsiFLKTYFPKSMS 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 248 ILSP-MYQMVNAELIKKC---HEQQ--IKVIPWTVNTAKEITELKALNVDGIISDYPDLL 301
Cdd:cd08612   235 RLNRfVLFLIDWLLMRPSlfrHLQKrgIQVYGWVLNDEEEFERAFELGADGVMTDYPTKL 294
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 41-298 7.75e-19

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: 83.51  E-value: 7.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGG-RGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSpafmldpqgqeisksdaR----KYAVFQMDY 115
Cdd:cd08566     5 HRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLD-----------------RttngKGKVSDLTL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 116 VALKQFDLGSKYYEAFPQQkkmksyIPRLGELIDavqqylkkAGKKQIFYNIETKcspegdgllnpdpETFVQLLMDVIE 195
Cdd:cd08566    68 AEIRKLRLKDGDGEVTDEK------VPTLEEALA--------WAKGKILLNLDLK-------------DADLDEVIALVK 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 196 KKGIQQFVVIQSFDKRTLQVLHKKYPQMKTSYLVANKKSFEENIADLGFN----PFILSPMYQMVNAELIKKCHEQQIKV 271
Cdd:cd08566   121 KHGALDQVIFKSYSEEQAKELRALAPEVMLMPIVRDAEDLDEEEARAIDAlnllAFEITFDDLDLPPLFDELLRALGIRV 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2225715120 272 IpwtVNT----------------AKEITELKALNVDGIISDYP 298
Cdd:cd08566   201 W---VNTlgdddtagldralsdpREVWGELVDAGVDVIQTDRP 240
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 39-301 2.41e-17

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: 79.82  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  39 EGHRGG--RGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTH--DDYLSPAFMLDPQGQEISKSDarkyavfQMD 114
Cdd:cd08564     7 VGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgtEDDTNPDTSIQLDDSGFKNIN-------DLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 115 YVALKqfdlgsKYYEAFPQQKKMKSYIPRLGELIDAVQQYLKKAGKKqIFYNIETKCSPEGDGllnpdpetfvQLLMDVI 194
Cdd:cd08564    80 LDEIT------RLHFKQLFDEKPCGADEIKGEKIPTLEDVLVTFKDK-LKYNIELKGREVGLG----------ERVLNLV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 195 EKKGIQQFVVIQSFDKRT----LQVLHKKYPQMKTSYLVANKKS-----FEENIADLGFNPFILSpmYQMVNAELIKKCH 265
Cdd:cd08564   143 EKYGMILQVHFSSFLHYDrldlLKALRPNKLNVPIALLFNEVKSpspldFLEQAKYYNATWVNFS--YDFWTEEFVKKAH 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2225715120 266 EQQIKVI---PWTVNTAKEITELK-ALNVDGIISDYPDLL 301
Cdd:cd08564   221 ENGLKVMtyfDEPVNDNEEDYKVYlELGVDCICPNDPVLL 260
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 40-300 2.96e-16

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: 76.29  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAfmLDPQGqeisksdarkyAVFQMDYVALK 119
Cdd:cd08565     3 GHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRT--THGTG-----------AVRDLTLAERK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSKYYEAfpqqkkmksyIPRLGELIDAVQQylkkagkKQIFYNIETKcsPEGDGLlnpDPETFVQLLMDVIEKKGI 199
Cdd:cd08565    70 ALRLRDSFGEK----------IPTLEEVLALFAP-------SGLELHVEIK--TDADGT---PYPGAAALAAATLRRHGL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKkYPQMKTSYLVaNKKSFEENIADLGFNPFILSPMY--------QMVNAELIKKCHEQQiKV 271
Cdd:cd08565   128 LERSVLTSFDPAVLTEVRK-HPGVRTLGSV-DEDMLERLGGELPFLTATALKAHivaveqslLAATWELVRAAVPGL-RL 204

                         250       260
                  ....*....|....*....|....*....
gi 2225715120 272 IPWTVNTAKEITELKALNVDGIISDYPDL 300
Cdd:cd08565   205 GVWTVNDDSLIRYWLACGVRQLTTDRPDL 233
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 40-297 1.13e-15

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: 73.62  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSpafmldpqgqeisksdaRKYAVFQmdyvalk 119
Cdd:cd08555     3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLD-----------------RTTAGIL------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 qfdlgskyyeafpqqkkmksyIPRLGELIDAVQQYLKKAGKKQIFyNIETKCSPegdgllnpdpetfvqllmdviekkgi 199
Cdd:cd08555    59 ---------------------PPTLEEVLELIADYLKNPDYTIIL-SLEIKQDS-------------------------- 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 qqfVVIQSFDKRTLQVLHKKYPQMKTSYLVAnkKSFEENIADLgfnpFILSPMYQmVNAELIKKCHEQQIKVIPWTVNTA 279
Cdd:cd08555    91 ---PEYDEFLAKVLKELRVYFDYDLRGKVVL--SSFNALGVDY----YNFSSKLI-KDTELIASANKLGLLSRIWTVNDN 160

                         250
                  ....*....|....*....
gi 2225715120 280 KE-ITELKALNVDGIISDY 297
Cdd:cd08555   161 NEiINKFLNLGVDGLITDF 179
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 41-299 5.16e-15

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: 73.96  E-value: 5.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISKSDARKYAV-FQMDyvALK 119
Cdd:cd08600     6 HRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRYYVIdFTLD--ELK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSKYY-------EAFPQQKKMKSY---IPRLGELIDAVQQYLKKAGKKQIFYnIETKcSP-----EGDgllnpDPE 184
Cdd:cd08600    84 SLSVTERFDiengkkvQVYPNRFPLWKSdfkIHTLEEEIELIQGLNKSTGKNVGIY-PEIK-APwfhhqEGK-----DIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 185 TfvqLLMDVIEKKGIQQ---FVVIQSFDKRTLQVLHKK-YPQMKTSY----LVANKKSFEENIADLG----------FNP 246
Cdd:cd08600   157 A---ATLEVLKKYGYTSkndKVYLQTFDPNELKRIKNElLPKMGMDLklvqLIAYTDWGETQEKDPGgwvnydydwmFTK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 247 FILS----------PMYQM-----------VNAELIKKCHEQQIKVIPWTVNT------AKEITEL-----KALNVDGII 294
Cdd:cd08600   234 GGLKeiakyadgvgPWYSMiieeksskgniVLTDLVKDAHEAGLEVHPYTVRKdalpeyAKDADQLldallNKAGVDGVF 313


                  ....*
gi 2225715120 295 SDYPD 299
Cdd:cd08600   314 TDFPD 318
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 40-298 1.67e-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: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 71.21  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLspafmLDPQGQEIsksdarkyAVFQMDYVALK 119
Cdd:cd08581     3 AHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTL-----LRLTGVEG--------LLHELEDAELD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDL--GSKYYEAFPQQKkmksyIPRLgeliDAVQQYLKKAGKKQIFYNIETKCSPegdgllNPDPETFVQLLMDVIEKK 197
Cdd:cd08581    70 SLRVaePARFGSRFAGEP-----LPSL----AAVVQWLAQHPQVTLFVEIKTESLD------RFGLERVVDKVLRALPAV 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 198 GIQqfVVIQSFDKRTLQVLhKKYPQMKTSYLV-----ANKKSFEENIADLGFNPFILSPMyqmvnaelIKKCHEQQIKVI 272
Cdd:cd08581   135 AAQ--RVLISFDYDLLALA-KQQGGPRTGWVLpdwddASLAEADELQPDYLFCDKNLLPD--------TGDLWAGTWKWV 203

                         250       260
                  ....*....|....*....|....*.
gi 2225715120 273 PWTVNTAKEITELKALNVDGIISDYP 298
Cdd:cd08581   204 IYEVNEPAEALALAARGVALIETDNI 229
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-278 1.99e-11

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: 62.71  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISKSDArkyAVFQMDyvALK 119
Cdd:cd08574     6 GHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHERA---SMFTWT--DLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGS------KYYEAFP-----QQKKMKSYIPRLGELIDAVqqylKKAGKKQIFyniETKCSPEGdgllNPDPETFVQ 188
Cdd:cd08574    81 QLNAGQwflkddPFWTASSlsesdREEAGNQSIPSLAELLRLA----KKHNKSVIF---DLRRPPPN----HPYYQSYVN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 189 LLMDVIEKKGIQQFVVIQSFDKRTLQVlHKKYPQMKTSYlvANKKSFEEniaDLGFNPFILSPMYQMVNAELIKKCHEQQ 268
Cdd:cd08574   150 ITLDTILASGIPQHQVFWLPDEYRALV-RKVAPGFQQVS--GRKLPVES---LRENGISRLNLEYSQLSAQEIREYSKAN 223

                         250
                  ....*....|
gi 2225715120 269 IKVIPWTVNT 278
Cdd:cd08574   224 ISVNLYVVNE 233
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-297 4.15e-10

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: 59.60  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRG--------GRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSpafMLDPQGQEISKSDARKYAVF 111
Cdd:cd08572     4 GHRGlgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIS---VSEKSKTGSDEGELIEVPIH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 112 QMDYVALKQ-------FDLGSKYYEA---FPQQKKMKSY---IPRLGELIDAVQQYLkkaGkkqifYNIETK--CSPE-G 175
Cdd:cd08572    81 DLTLEQLKElglqhisALKRKALTRKakgPKPNPWGMDEhdpFPTLQEVLEQVPKDL---G-----FNIEIKypQLLEdG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 176 DGLLNPDPE--TFVQLLMDVIEKKGIQQFVVIQSFDK------RTLQvlhKKYPQM---------------KTSYL-VAN 231
Cdd:cd08572   153 EGELTPYFErnAFVDTILAVVFEHAGGRRIIFSSFDPdicimlRLKQ---NKYPVLfltnggtnevehmdpRRRSLqAAV 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225715120 232 KKSFEENIADLGFNPFILSPmyqmvNAELIKKCHEQQIKVIPW--TVNTAKEITELKALNVDGIISDY 297
Cdd:cd08572   230 NFALAEGLLGVVLHAEDLLK-----NPSLISLVKALGLVLFTYgdDNNDPENVKKQKELGVDGVIYDR 292
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 40-298 5.58e-10

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: 59.23  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLS--------PAFMLDPQGQEISKSDARKYAVF 111
Cdd:cd08602     5 AHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSgttdvadhPEFADRKTTKTVDGVNVTGWFTE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 112 QMDYVALKQfdLGSKyyEAFPQQKkmKSY-----IPRLGELIDAVQQYLKKAGKKQIFYnIETKCSP---EGDGLlnpdp 183
Cdd:cd08602    85 DFTLAELKT--LRAR--QRLPYRD--QSYdgqfpIPTFEEIIALAKAASAATGRTVGIY-PEIKHPTyfnAPLGL----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 184 eTFVQLLMDVIEK---KGIQQFVVIQSFDKRTLQVLHKK-----------YPQMKTSYLVANKKSFEENIADLGFN---- 245
Cdd:cd08602   153 -PMEDKLLETLKKygyTGKKAPVFIQSFEVTNLKYLRNKtdlplvqliddATIPPQDTPEGDSRTYADLTTDAGLKeiat 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225715120 246 ---------PFILSPMYQMVNAE---LIKKCHEQQIKVIPWTV-------------NTAKEITELKALNVDGIISDYP 298
Cdd:cd08602   232 yadgigpwkDLIIPSDANGRLGTptdLVEDAHAAGLQVHPYTFrnentflppdffgDPYAEYRAFLDAGVDGLFTDFP 309
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 41-294 1.80e-09

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: 56.95  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRG----GRGLmPENTIPAMYHAIDLGmTTLEMDTHITKDQEVVVTHDDYLspafmldpqgQEISKSDARkyaVFQMDYV 116
Cdd:cd08585     9 HRGlhdrDAGI-PENSLSAFRAAAEAG-YGIELDVQLTADGEVVVFHDDNL----------KRLTGVEGR---VEELTAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 117 ALKQFDLGSKyyeafpqqkkmKSYIPRLGELIDAVqqylkkAGKKQIFynIETKcSPEGdgllnpDPETFVQLLMDVIek 196
Cdd:cd08585    74 ELRALRLLGT-----------DEHIPTLDEVLELV------AGRVPLL--IELK-SCGG------GDGGLERRVLAAL-- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 197 KGIQQFVVIQSFDKRTLQVLHKKYPQM---KTSY-----------LVANKKSFEENIADlgfNPFILSPMYQMVNAELIK 262
Cdd:cd08585   126 KDYKGPAAIMSFDPRVVRWFRKLAPGIprgQLSEgsndeadpafwNEALLSALFSNLLT---RPDFIAYHLDDLPNPFVT 202

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2225715120 263 KCHE-QQIKVIPWTVNTAKEITELKAlNVDGII 294
Cdd:cd08585   203 LARAlLGMPVIVWTVRTEEDIARLKQ-YADNII 234
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-277 2.35e-09

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: 57.24  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLD---PQGQEISKSDarkyavfqMDYV 116
Cdd:cd08609    31 GHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKdvfPGRDAAGSNN--------FTWT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 117 ALKQFDLGSKYYEAFP-----------QQKKMKSYIPRLGELIDAVqqylkKAGKKQIFYNIEtkcsPEGDGllNPDPET 185
Cdd:cd08609   103 ELKTLNAGSWFLERRPfwtlsslseedRREADNQTVPSLSELLDLA-----KKHNVSIMFDLR----NENNS--HVFYSS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 186 FVQLLMDVIEKKGIQQFVVIQSFDKRTLQVLhKKYPQMKTSYlvaNKKsfEENIADlgfNPFILSPMYQMVNAELIKKCH 265
Cdd:cd08609   172 FVFYTLETILKLGIPPDKVWWLPDEYRHDVM-KMEPGFKQVY---GRQ--KEMLMD---GGNFMNLPYQDLSALEIKELR 242

                         250
                  ....*....|..
gi 2225715120 266 EQQIKVIPWTVN 277
Cdd:cd08609   243 KDNVSVNLWVVN 254
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-298 3.05e-09

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: 56.50  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDylspafmldpqgqEISKSDARKYAVFQMDYVALK 119
Cdd:cd08573     3 GHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDD-------------TVDRTTDGTGLVAELTWEELR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 120 QFDLGSK--YYEAFPQQKkmksyIPRLGElidAVQQYLKKagKKQIFYNIETkcspegdgllnpDPETFVQLLMDVIEK- 196
Cdd:cd08573    70 KLNAAAKhrLSSRFPGEK-----IPTLEE---AVKECLEN--NLRMIFDVKS------------NSSKLVDALKNLFKKy 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 197 KGIQQFVVIQSFDKRTLQVLHKKYPQMKT-----SYLVANkKSFEENIAdlgFNPFILSPMYQM---------------- 255
Cdd:cd08573   128 PGLYDKAIVCSFNPIVIYKVRKADPKILTgltwrPWFLSY-TDDEGGPR---RKSGWKHFLYSMldvilewslhswlpyf 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2225715120 256 ------------VNAELIKKCHEQQIKVIPWTVNTAKEITEL-KALNVDgIISDYP 298
Cdd:cd08573   204 lgvsallihkddISSAYVRYWRARGIRVIAWTVNTPTEKQYFaKTLNVP-YITDSL 258
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 27-300 9.63e-09

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 55.83  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  27 MTTTAQFPAFSNE----GHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLDPQGQEISK 102
Cdd:PRK11143   14 LAGSAAAAADSAEkiviAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERFPDRAR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 103 SDARKYAV-FQMDYV-ALK---QFDL-GSKYYEAFPQQKKM-KSY--IPRLGELIDAVQQYLKKAGKKQIFYnIETKcSP 173
Cdd:PRK11143   94 KDGRYYAIdFTLDEIkSLKfteGFDIeNGKKVQVYPGRFPMgKSDfrVHTFEEEIEFIQGLNHSTGKNIGIY-PEIK-AP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 174 -----EGdgllnpdpETFVQLLMDVIEKKGIQQ---FVVIQSFDKRTLQVLHKK-YPQM----KTSYLVA---------- 230
Cdd:PRK11143  172 wfhhqEG--------KDIAAKVLEVLKKYGYTGkddKVYLQCFDANELKRIKNElEPKMgmdlKLVQLIAytdwnetqek 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 231 NKKSFEENIA-DLGFNPFILS----------PMYQMVNAE-----------LIKKCHEQQIKVIPWTVNT------AKEI 282
Cdd:PRK11143  244 QPDGKWVNYNyDWMFKPGAMKevakyadgigPDYHMLVDEtstpgnikltgMVKEAHQAKLVVHPYTVRAdqlpeyATDV 323

                         330       340
                  ....*....|....*....|...
gi 2225715120 283 TEL-----KALNVDGIISDYPDL 300
Cdd:PRK11143  324 NQLydilyNQAGVDGVFTDFPDK 346
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 41-303 2.08e-08

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 53.79  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDylspafMLDpqgqeiSKSDARKyAVFQMDYVALKQ 120
Cdd:PRK09454   13 HRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDD------TLE------RTSNGWG-VAGELTWQDLAQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 121 FDLGSKYYEAFPQQKkmksyIPRLgeliDAVQQYLKKAGkkqIFYNIETKCSPegdGLlnpDPETFVQLLMDVIEK-KGI 199
Cdd:PRK09454   80 LDAGSWFSAAFAGEP-----LPTL----SQVAARCRAHG---MAANIEIKPTT---GR---EAETGRVVALAARALwAGA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 200 QQFVVIQSFDKRTLQVLHKKYPQMKTSYLvankksFEENIAD-------LGFNPFILSpmYQMVNAELIKKCHEQQIKVI 272
Cdd:PRK09454  142 AVPPLLSSFSEDALEAARQAAPELPRGLL------LDEWPDDwleltrrLGCVSLHLN--HKLLDEARVAALKAAGLRIL 213

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2225715120 273 PWTVNTAKEITELKALNVDGIISDYPDLLGH 303
Cdd:PRK09454  214 VYTVNDPARARELLRWGVDCICTDRIDLIGP 244
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 40-296 1.93e-06

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


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 48.44  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRG-------GRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDdyLSPAFMLDPQGQEiSKSDARKYAVFQ 112
Cdd:cd08607     4 GHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHD--FTLRVSLKSKGDS-DRDDLLEVPVKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 113 MDYVALKQFDLgskYYEAFPQQKKMKSYI-----------PRLGELIDAVqqyLKKAGkkqifYNIETKC-------SPE 174
Cdd:cd08607    81 LTYEQLKLLKL---FHISALKVKEYKSVEededppehqpfPTLSDVLESV---PEDVG-----FNIEIKWpqqqkdgSWE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 175 GDGLLNPDPETFVQLLMDVIEKKGIQQFVVIQSFDK------RTLQ----VL------HKKYPQM-----KTSYLVANKK 233
Cdd:cd08607   150 SELFTYFDRNLFVDIILKIVLEHAGKRRIIFSSFDAdictmlRFKQnkypVLfltqgkTQRYPEFmdlrtRTFEIAVNFA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225715120 234 SFEENiadLGFNP---FILSpmyqmvNAELIKKCHEQQIKVIPW--TVNTAKEITELKALNVDGIISD 296
Cdd:cd08607   230 QAEEL---LGVNLhseDLLK------DPSQIELAKSLGLVVFCWgdDLNDPENRKKLKELGVDGLIYD 288
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 50-84 1.34e-05

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: 45.81  E-value: 1.34e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2225715120  50 ENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHD 84
Cdd:cd08613    60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHD 94
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 51-297 1.89e-05

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


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 44.98  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  51 NTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSpafMLDPQGQEISKSDARkyavfqmdyVALKQFdLGSKYYEa 130
Cdd:cd08583    16 NSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWDES---LLKQLGLPTSKNTKP---------LSYEEF-KSKKIYG- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 131 fpQQKKMKsyiprlgelIDAVQQYLKKagKKQIFYNIETKcspegDGLLNPDPETFVQLLMDVIEKKG-IQQFVVIQSFD 209
Cdd:cd08583    82 --KYTPMD---------FKDVIDLLKK--YPDVYIVTDTK-----QDDDNDIKKLYEYIVKEAKEVDPdLLDRVIPQIYN 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 210 KRTLQVLHKKYPQMKTSYLVANKKSFEEN-IADL---GFNPFILSPMYQmVNAELIKKCHEQQIKVIPWTVNTAKEITEL 285
Cdd:cd08583   144 EEMYEAIMSIYPFKSVIYTLYRQDSIRLDeIIAFcyeNGIKAVTISKNY-VNDKLIEKLNKAGIYVYVYTINDLKDAQEY 222

                         250
                  ....*....|..
gi 2225715120 286 KALNVDGIISDY 297
Cdd:cd08583   223 KKLGVYGIYTDF 234
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-277 4.51e-05

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: 44.48  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  25 QRMTTTAQFPAFSneGHRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPAFMLdpqGQEISKSD 104
Cdd:cd08610    14 REKETLGPKPTII--GHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI---GEVQPESA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 105 ARKYAVFQMDyvALKQFDLGSKYYEAFP-----------QQKKMKSYIPRLGELidavqqyLKKAGKKQIFYNIETKCSP 173
Cdd:cd08610    89 CENPAFFNWD--FLSTLNAGKWFVKPRPfynmkplseadKERARNQSIPKLSNF-------LRLAEKENKLVIFDLYRPP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 174 EGdgllNPDPETFVQLLMDVI-EKKGIQQFVV--IQSFDKRTLQVLHKKYPQMktsylVANKKSFEENIADlgfNPFILS 250
Cdd:cd08610   160 PK----HPYRHTWIRRVLEVIlNEVGIEQHLVlwLPAHDRQYVQSVAPGFKQH-----VGRKVPIETLLKN---NISILN 227

                         250       260
                  ....*....|....*....|....*..
gi 2225715120 251 PMYQMVNAELIKKCHEQQIKVIPWTVN 277
Cdd:cd08610   228 LAYKKLFSNDIRDYKAANIHTNVYVIN 254
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 41-225 7.67e-04

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: 40.39  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  41 HRGGRGLMPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDDYLSPafMLDPQGQeISKSDARKYAvfQMDyvALKQ 120
Cdd:cd08580     6 HRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKS--LTNGSGA-VSAYTAAQLA--TLN--AGYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 121 F-DLGSKYYeafpQQKKMKsyIPRLgelidavQQYLKKAGKKQIFYNIETkcspegdgllnPDPETFVQLLMDVIEKKGI 199
Cdd:cd08580    79 FkPEGGYPY----RGKPVG--IPTL-------EQVLRAFPDTPFILDMKS-----------LPADPQAKAVARVLERENA 134

                         170       180
                  ....*....|....*....|....*.
gi 2225715120 200 QQFVVIQSFDKRTLQVLhKKYPQMKT 225
Cdd:cd08580   135 WSRVRIYSTNADYQDAL-APYPQARL 159
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 40-223 2.74e-03

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: 38.58  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120  40 GHRG-GRGL-------MPENTIPAMYHAIDLGMTTLEMDTHITKDQEVVVTHDdylspaFMLDPQGQEIsksdarkyavf 111
Cdd:cd08606     6 GHRGlGKNTaerkslqLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHD------FLVSETGTDV----------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225715120 112 QMDYVALKQFdLGS---KYYEAFpqqkKMKSYIPR-LGELIDAVQQYLKKAGKK---QIFYNIETK------CSPEGDGL 178
Cdd:cd08606    69 PIHDLTLEQF-LHLsrmKYTVDF----KKKGFKGNsRGHSIQAPFTTLEELLKKlpkSVGFNIELKypmlheAEEEEVAP 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2225715120 179 LNPDPETFVQLLMDVIEKKGIQQFVVIQSFDKRTLQVLHKK---YPQM 223
Cdd:cd08606   144 VAIELNAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKqpgYPVL 191
 
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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