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Conserved domains on  [gi|1907206193|ref|XP_036017993|]
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glycerophosphoinositol inositolphosphodiesterase GDPD2 isoform X1 [Mus musculus]

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 ...
 198-500 0e+00

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 cd08609:

Pssm-ID: 472694 [Multi-domain]  Cd Length: 315  Bit Score: 537.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 198 VTLVIYLMPLLfISSPCIMKLRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLS 277
Cdd:cd08609     1 VSAAVYLAPLA-ICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 278 RTTNVASVFPERISAHSSDFSWAELQRLNAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDL 357
Cdd:cd08609    80 RTTNVKDVFPGRDAAGSNNFTWTELKTLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 358 RRPPRNHTYYDTFVNQTLEAVLSANVSQAMVLWLPDEDRANVQQRAPRMRQIYGHQGGNWTERPQFLNLPYQDLPALDIK 437
Cdd:cd08609   160 RNENNSHVFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQVYGRQKEMLMDGGNFMNLPYQDLSALEIK 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907206193 438 ALHQDNISVNLFVVNKPWLFSLLWCAGVDSVTTNACQLLQQMQNPLWLLPPQKYLMIWVITDC 500
Cdd:cd08609   240 ELRKDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKDMSKPIWLLEPNTYLGIWIATDC 302
 
Name Accession Description Interval E-value
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 198-500 0e+00

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: 537.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 198 VTLVIYLMPLLfISSPCIMKLRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLS 277
Cdd:cd08609     1 VSAAVYLAPLA-ICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 278 RTTNVASVFPERISAHSSDFSWAELQRLNAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDL 357
Cdd:cd08609    80 RTTNVKDVFPGRDAAGSNNFTWTELKTLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 358 RRPPRNHTYYDTFVNQTLEAVLSANVSQAMVLWLPDEDRANVQQRAPRMRQIYGHQGGNWTERPQFLNLPYQDLPALDIK 437
Cdd:cd08609   160 RNENNSHVFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQVYGRQKEMLMDGGNFMNLPYQDLSALEIK 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907206193 438 ALHQDNISVNLFVVNKPWLFSLLWCAGVDSVTTNACQLLQQMQNPLWLLPPQKYLMIWVITDC 500
Cdd:cd08609   240 ELRKDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKDMSKPIWLLEPNTYLGIWIATDC 302
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
223-478 1.64e-42

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 151.95  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 223 PKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVAsvfpERIsahsSDFSWAEL 302
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGT----GRV----ADLTLAEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 303 QRLNAGtwflerqpfwgakklsgsDRKEAENQTIPALEELLkEAAALNLSIMFDLRRPPrnhTYYDTFVNQTLEAVLSAN 382
Cdd:COG0584    73 RQLDAG------------------SGPDFAGERIPTLEEVL-ELVPGDVGLNIEIKSPP---AAEPDLAEAVAALLKRYG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 383 VSQAMVLWLPDEDR-ANVQQRAPRMR--QIYGHQGGNWTE-----RPQFLNLPYQDLPALDIKALHQDNISVNLFVVNKP 454
Cdd:COG0584   131 LEDRVIVSSFDPEAlRRLRELAPDVPlgLLVEELPADPLElaralGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDP 210

                         250       260
                  ....*....|....*....|....
gi 1907206193 455 WLFSLLWCAGVDSVTTNACQLLQQ 478
Cdd:COG0584   211 EEMRRLLDLGVDGIITDRPDLLRA 234
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 230-471 4.25e-25

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: 104.02  E-value: 4.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 230 HRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVfperisahSSDFSWAELQRLNAGT 309
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY--------VRDLTLEELKRLDIGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 310 WFL-----ERQPF----------WGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDLRRPPRNhtYYDTFVNQT 374
Cdd:pfam03009  73 GNSgplsgERVPFptleevlefdWDVGFNIEIKIKPYVEAIAPEEGLIVKDLLLSVDEILAKKADPRRV--IFSSFNPDE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 375 LEAV-LSANVSQAMVLW-LPDEDRANVQQRAPRMRQIYGHQGGNWterpqflnLPYQDLPALdIKALHQDNISVNLFVVN 452
Cdd:pfam03009 151 LKRLrELAPKLPLVFLSsGRAYAEADLLERAAAFAGAPALLGEVA--------LVDEALPDL-VKRAHARGLVVHVWTVN 221

                         250
                  ....*....|....*....
gi 1907206193 453 KPWLFSLLWCAGVDSVTTN 471
Cdd:pfam03009 222 NEDEMKRLLELGVDGVITD 240
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 223-311 5.55e-21

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 92.31  E-value: 5.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 223 PKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAEL 302
Cdd:PRK09454    6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNG--------WGVAGELTWQDL 77


                  ....*....
gi 1907206193 303 QRLNAGTWF 311
Cdd:PRK09454   78 AQLDAGSWF 86
 
Name Accession Description Interval E-value
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 198-500 0e+00

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: 537.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 198 VTLVIYLMPLLfISSPCIMKLRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLS 277
Cdd:cd08609     1 VSAAVYLAPLA-ICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 278 RTTNVASVFPERISAHSSDFSWAELQRLNAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDL 357
Cdd:cd08609    80 RTTNVKDVFPGRDAAGSNNFTWTELKTLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 358 RRPPRNHTYYDTFVNQTLEAVLSANVSQAMVLWLPDEDRANVQQRAPRMRQIYGHQGGNWTERPQFLNLPYQDLPALDIK 437
Cdd:cd08609   160 RNENNSHVFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQVYGRQKEMLMDGGNFMNLPYQDLSALEIK 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907206193 438 ALHQDNISVNLFVVNKPWLFSLLWCAGVDSVTTNACQLLQQMQNPLWLLPPQKYLMIWVITDC 500
Cdd:cd08609   240 ELRKDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKDMSKPIWLLEPNTYLGIWIATDC 302
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 224-472 1.02e-146

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: 421.72  E-value: 1.02e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 224 KPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFPERISAHSSDFSWAELQ 303
Cdd:cd08574     1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHERASMFTWTDLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 304 RLNAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDLRRPPRNHTYYDTFVNQTLEAVLSANV 383
Cdd:cd08574    81 QLNAGQWFLKDDPFWTASSLSESDREEAGNQSIPSLAELLRLAKKHNKSVIFDLRRPPPNHPYYQSYVNITLDTILASGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 384 SQAMVLWLPDEDRANVQQRAPRMRQIYGHQGGNWTER---PQFLNLPYQDLPALDIKALHQDNISVNLFVVNKPWLFSLL 460
Cdd:cd08574   161 PQHQVFWLPDEYRALVRKVAPGFQQVSGRKLPVESLRengISRLNLEYSQLSAQEIREYSKANISVNLYVVNEPWLYSLL 240

                         250
                  ....*....|..
gi 1907206193 461 WCAGVDSVTTNA 472
Cdd:cd08574   241 WCSGVQSVTTNA 252
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 224-499 9.74e-109

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


Pssm-ID: 176550  Cd Length: 351  Bit Score: 328.34  E-value: 9.74e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 224 KPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFPERISAHSSDFSWAELQ 303
Cdd:cd08608     1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 304 RLNAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDLRRPPRNHTYYDTFVNQTLEAVLSANV 383
Cdd:cd08608    81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKRYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 384 SQAMVLWLPDEDRANVQQRAPRMRQIYG--------HQGGnwterPQFLNLPYQDLPALDIKALHQDNISVNLFVVNKPW 455
Cdd:cd08608   161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGeklpvaslRERG-----ITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPW 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907206193 456 LFSLLWCAGVDSVTTNACQLLQQMQNPLWLLPPQKYLMIWVITD 499
Cdd:cd08608   236 LYSLLWCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSD 279
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 202-501 1.06e-101

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: 309.11  E-value: 1.06e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 202 IYLMPLlFISSPCIMKLRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTN 281
Cdd:cd08610     1 LYLIPL-GIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 282 VASVFPERISAHSSDFSWAELQRLNAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDLRRPP 361
Cdd:cd08610    80 IGEVQPESACENPAFFNWDFLSTLNAGKWFVKPRPFYNMKPLSEADKERARNQSIPKLSNFLRLAEKENKLVIFDLYRPP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 362 RNHTYYDTFVNQTLEAVL-SANVSQAMVLWLPDEDRANVQQRAPRMRQIYGHQGGN---WTERPQFLNLPYQDLPALDIK 437
Cdd:cd08610   160 PKHPYRHTWIRRVLEVILnEVGIEQHLVLWLPAHDRQYVQSVAPGFKQHVGRKVPIetlLKNNISILNLAYKKLFSNDIR 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907206193 438 ALHQDNISVNLFVVNKPWLFSLLWCAGVDSVTTNACQLLQQMQNPLWLLPPQKYLMIWVITDCA 501
Cdd:cd08610   240 DYKAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQLDHPHFFMTPKFYVFMWLLADII 303
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
223-478 1.64e-42

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 151.95  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 223 PKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVAsvfpERIsahsSDFSWAEL 302
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGT----GRV----ADLTLAEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 303 QRLNAGtwflerqpfwgakklsgsDRKEAENQTIPALEELLkEAAALNLSIMFDLRRPPrnhTYYDTFVNQTLEAVLSAN 382
Cdd:COG0584    73 RQLDAG------------------SGPDFAGERIPTLEEVL-ELVPGDVGLNIEIKSPP---AAEPDLAEAVAALLKRYG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 383 VSQAMVLWLPDEDR-ANVQQRAPRMR--QIYGHQGGNWTE-----RPQFLNLPYQDLPALDIKALHQDNISVNLFVVNKP 454
Cdd:COG0584   131 LEDRVIVSSFDPEAlRRLRELAPDVPlgLLVEELPADPLElaralGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDP 210

                         250       260
                  ....*....|....*....|....
gi 1907206193 455 WLFSLLWCAGVDSVTTNACQLLQQ 478
Cdd:COG0584   211 EEMRRLLDLGVDGIITDRPDLLRA 234
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 227-470 4.97e-34

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: 128.49  E-value: 4.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNvasvfperISAHSSDFSWAELQRLN 306
Cdd:cd08562     1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN--------GSGAVTELTWAELAQLD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 307 AGTWFLERqpFWGAKklsgsdrkeaenqtIPALEELLKEAAALNLSIMFDLRRPPRNHTYYDTFVNQTLeAVLSANVSQA 386
Cdd:cd08562    73 AGSWFSPE--FAGEP--------------IPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAAL-RELWPHASKL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 387 MV-------LWLpdedranVQQRAPRMRQ--IYGHQGGNWTER-----PQFLNLPYQDLPALDIKALHQDNISVNLFVVN 452
Cdd:cd08562   136 LLssfsleaLRA-------ARRAAPELPLglLFDTLPADWLELlaalgAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVN 208

                         250
                  ....*....|....*...
gi 1907206193 453 KPWLFSLLWCAGVDSVTT 470
Cdd:cd08562   209 DPARAAELLEWGVDAIFT 226
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 227-407 6.21e-26

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: 106.23  E-value: 6.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPM-LAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNvasvfperISAHSSDFSWAELQRL 305
Cdd:cd08566     2 VVAHRGGWGaGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTN--------GKGKVSDLTLAEIRKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 306 NAGTWFLERQpfwgakklsgsdrkeaeNQTIPALEELLkEAAALNLSIMFDLRrpprnhtyyDTFVNQTLEAVLSANVSQ 385
Cdd:cd08566    74 RLKDGDGEVT-----------------DEKVPTLEEAL-AWAKGKILLNLDLK---------DADLDEVIALVKKHGALD 126

                         170       180
                  ....*....|....*....|...
gi 1907206193 386 AMVLWLPD-EDRANVQQRAPRMR 407
Cdd:cd08566   127 QVIFKSYSeEQAKELRALAPEVM 149
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 225-352 9.22e-26

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: 107.36  E-value: 9.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFPERISAH----SSDFSWA 300
Cdd:cd08559     1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKDtgyfVIDFTLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907206193 301 ELQRLNAGTWFLERQPFwgakklsgSDRKEAENQTIPALEELLKEAAALNLS 352
Cdd:cd08559    81 ELKTLRAGSWFNQRYPE--------RAPSYYGGFKIPTLEEVIELAQGLNKS 124
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 230-471 4.25e-25

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: 104.02  E-value: 4.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 230 HRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVfperisahSSDFSWAELQRLNAGT 309
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY--------VRDLTLEELKRLDIGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 310 WFL-----ERQPF----------WGAKKLSGSDRKEAENQTIPALEELLKEAAALNLSIMFDLRRPPRNhtYYDTFVNQT 374
Cdd:pfam03009  73 GNSgplsgERVPFptleevlefdWDVGFNIEIKIKPYVEAIAPEEGLIVKDLLLSVDEILAKKADPRRV--IFSSFNPDE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 375 LEAV-LSANVSQAMVLW-LPDEDRANVQQRAPRMRQIYGHQGGNWterpqflnLPYQDLPALdIKALHQDNISVNLFVVN 452
Cdd:pfam03009 151 LKRLrELAPKLPLVFLSsGRAYAEADLLERAAAFAGAPALLGEVA--------LVDEALPDL-VKRAHARGLVVHVWTVN 221

                         250
                  ....*....|....*....
gi 1907206193 453 KPWLFSLLWCAGVDSVTTN 471
Cdd:pfam03009 222 NEDEMKRLLELGVDGVITD 240
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 229-478 3.09e-24

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: 101.57  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 229 GHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNvasvFPERIsahsSDFSWAELQRLNAG 308
Cdd:cd08561     3 AHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTD----GTGPV----ADLTLAELRRLDAG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 309 TWFlerqpfwgaKKLSGSDRK-EAENQTIPALEELLKeaAALNLSIMFDLRRPPRNH--TYYDtFVNQT--LEAVLSANV 383
Cdd:cd08561    75 YHF---------TDDGGRTYPyRGQGIRIPTLEELFE--AFPDVRLNIEIKDDGPAAaaALAD-LIERYgaQDRVLVASF 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 384 SqamvlwlpDEDRANVQQRAPRMRQIYG----------HQGG-NWTERP--QFLNLPYQ------DLPALdIKALHQDNI 444
Cdd:cd08561   143 S--------DRVLRRFRRLCPRVATSAGegevaafvlaSRLGlGSLYSPpyDALQIPVRyggvplVTPRF-VRAAHAAGL 213

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907206193 445 SVNLFVVNKPWLFSLLWCAGVDSVTTNACQLLQQ 478
Cdd:cd08561   214 EVHVWTVNDPAEMRRLLDLGVDGIITDRPDLLLE 247
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 227-471 3.97e-24

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: 99.65  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDerlsrttnvasvfperisahssdfswaelqrln 306
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 307 agtwflerqpfwgakklsgsdrkeaenqtIPALEELLkEAAALNLSIMFDLRRPPRnhtyYDTFVNQTLEAVLSAN-VSQ 385
Cdd:cd08556    48 -----------------------------IPTLEEVL-ELVKGGVGLNIELKEPTR----YPGLEAKVAELLREYGlEER 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 386 AMVLWLPDEDRANVQQRAPRMR--QIYGHQGGNWTE-------RPQFLNLPYQDLPALDIKALHQDNISVNLFVVNKPWL 456
Cdd:cd08556    94 VVVSSFDHEALRALKELDPEVPtgLLVDKPPLDPLLaelaralGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPED 173

                         250
                  ....*....|....*
gi 1907206193 457 FSLLWCAGVDSVTTN 471
Cdd:cd08556   174 ARRLLALGVDGIITD 188
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-357 7.94e-24

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: 100.80  E-value: 7.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfPERIsahsSDFSWAELQRLN 306
Cdd:cd08573     1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDG----TGLV----AELTWEELRKLN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907206193 307 AgtwflerqpfwgAKKLSGSDRKEAENqtIPALEELLKEAAALNLSIMFDL 357
Cdd:cd08573    73 A------------AAKHRLSSRFPGEK--IPTLEEAVKECLENNLRMIFDV 109
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 223-311 5.55e-21

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 92.31  E-value: 5.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 223 PKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAEL 302
Cdd:PRK09454    6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNG--------WGVAGELTWQDL 77


                  ....*....
gi 1907206193 303 QRLNAGTWF 311
Cdd:PRK09454   78 AQLDAGSWF 86
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 225-343 5.14e-20

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: 89.68  E-value: 5.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVAsvFPERIsahsSDFSWAELQR 304
Cdd:cd08601     1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIE--RPGPV----KDYTLAEIKQ 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907206193 305 LNAGTWFLERQPFWGakklsgsdRKEAENQTIPALEELL 343
Cdd:cd08601    75 LDAGSWFNKAYPEYA--------RESYSGLKVPTLEEVI 105
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 229-471 5.91e-19

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: 86.07  E-value: 5.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 229 GHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFperisahsSDFSWAELQRLNAG 308
Cdd:cd08563     5 AHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYV--------KDLTLEELKKLDAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 309 TWFLERQPFwgakklsgsdrkeaenQTIPALEELLKEAAA----LNLSI-------------MFDL--RRPPRNHTYYDT 369
Cdd:cd08563    77 SWFDEKFTG----------------EKIPTLEEVLDLLKDkdllLNIEIktdvihypgiekkVLELvkEYNLEDRVIFSS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 370 FVNQTLEAVLSANvSQAMVLWLPDEdraNVQQRAPRMRQIyghqggnwteRPQFLNLPYQDLPALDIKALHQDNISVNLF 449
Cdd:cd08563   141 FNHESLKRLKKLD-PKIKLALLYET---GLQDPKDYAKKI----------GADSLHPDFKLLTEEVVEELKKRGIPVRLW 206

                         250       260
                  ....*....|....*....|..
gi 1907206193 450 VVNKPWLFSLLWCAGVDSVTTN 471
Cdd:cd08563   207 TVNEEEDMKRLKDLGVDGIITN 228
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 227-472 3.45e-18

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 83.90  E-value: 3.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAELQRLN 306
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG--------DGAVSDLTLAELRKLD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 307 AGTWflerqpfwgakklsgsDRKEAENQTIPALEELLKEAAALNLSIMFDLRRPPRNHTYYDTFVNQTLEAVL------- 379
Cdd:cd08582    73 IGSW----------------KGESYKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLlpeqivi 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 380 ---SANVSQAM--------VLWL-PDEDRANVQQRAPRMRQIYG---HqgGNWTERPQFlnlpyqdlpaldIKALHQDNI 444
Cdd:cd08582   137 isfDAEALKRVrelaptleTLWLrNYKSPKEDPRPLAKSGGAAGldlS--YEKKLNPAF------------IKALRDAGL 202

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907206193 445 SVNLFVVNKPWlfSLLWCA--GVDSVTTNA 472
Cdd:cd08582   203 KLNVWTVDDAE--DAKRLIelGVDSITTNR 230
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 225-345 9.43e-18

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: 83.04  E-value: 9.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAELQR 304
Cdd:cd08575     1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGG--------SGLVSDLTYAELPP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907206193 305 LNAGtWFLERQPFWGAKKLSGSDRKeaenqtIPALEELLKE 345
Cdd:cd08575    73 LDAG-YGYTFDGGKTGYPRGGGDGR------IPTLEEVFKA 106
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 227-344 3.34e-16

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: 77.76  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFPERisahssDFSWAELQRLN 306
Cdd:cd08581     1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHEL------EDAELDSLRVA 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907206193 307 AGTWFLERQPfwgakklsgsdrkeaeNQTIPALEELLK 344
Cdd:cd08581    75 EPARFGSRFA----------------GEPLPSLAAVVQ 96
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 225-361 7.69e-15

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: 74.67  E-value: 7.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAELQR 304
Cdd:cd08580     1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNG--------SGAVSAYTAAQLAT 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907206193 305 LNAGtWFLERQpfwGAKKLSGSdrkeaeNQTIPALEELLKeaAALNLSIMFDLRRPP 361
Cdd:cd08580    73 LNAG-YNFKPE---GGYPYRGK------PVGIPTLEQVLR--AFPDTPFILDMKSLP 117
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 227-470 6.74e-14

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: 71.96  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTT--NVASVFPERISAHSSDFSWAELQR 304
Cdd:cd08567     3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDItrDPDGAWLPYEGPALYELTLAEIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 305 LNAGtwflERQPFWGAKKLsGSDRKEAENQTIPALEELLKEAAA-------LNLSIMFDLRRpPRNHTYYDTFVNQTLEA 377
Cdd:cd08567    83 LDVG----EKRPGSDYAKL-FPEQIPVPGTRIPTLEEVFALVEKygnqkvrFNIETKSDPDR-DILHPPPEEFVDAVLAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 378 VLSANVSQAMVLwLPDEDRA--NVQQRAPRMRQIYghqggnWTERPQFLNLP--------------YQDLPALDIKALHQ 441
Cdd:cd08567   157 IRKAGLEDRVVL-QSFDWRTlqEVRRLAPDIPTVA------LTEETTLGNLPraakklgadiwspyFTLVTKELVDEAHA 229

                         250       260
                  ....*....|....*....|....*....
gi 1907206193 442 DNISVNLFVVNKPWLFSLLWCAGVDSVTT 470
Cdd:cd08567   230 LGLKVVPWTVNDPEDMARLIDLGVDGIIT 258
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 227-471 1.18e-13

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


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 70.27  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAELQRLN 306
Cdd:cd08579     1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGV--------NKKVWDLTLEELKKLT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 307 AGTWflerqpFWGAKklsgsdrkeaenqtIPALEELLKEAAALNLSIMFDLRRPPRNhtyYDTFVNQTLEAVLSANVS-Q 385
Cdd:cd08579    73 IGEN------GHGAK--------------IPSLDEYLALAKGLKQKLLIELKPHGHD---SPDLVEKFVKLYKQNLIEnQ 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 386 AMVLWLPDEDRANVQQRAPRMRQ---IYGHQGGNWTERPQFLNLPYQDLPALDIKALHQDNISVNLFVVNKPWLFSLLWC 462
Cdd:cd08579   130 HQVHSLDYRVIEKVKKLDPKIKTgyiLPFNIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLA 209


                  ....*....
gi 1907206193 463 AGVDSVTTN 471
Cdd:cd08579   210 MGVDGIITD 218
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 228-305 8.01e-13

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


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 69.34  E-value: 8.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 228 VGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFPERISAHSS----DFSWAELQ 303
Cdd:cd08600     4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRyyviDFTLDELK 83


                  ..
gi 1907206193 304 RL 305
Cdd:cd08600    84 SL 85
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 228-356 4.44e-12

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: 66.09  E-value: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 228 VGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfPERISAHSsdfSWAELQRLNA 307
Cdd:cd08570     2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGK----DGLIIDDS---TWDELSHLRT 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907206193 308 gtwflerqpfwgakklsgsdrKEAENQTIPALEELLKEAAA-------LNLSIMFD 356
Cdd:cd08570    75 ---------------------IEEPHQPMPTLKDVLEWLVEhelpdvkLMLDIKRD 109
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 225-348 5.13e-12

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: 66.94  E-value: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASV--FPERISAH--------- 293
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHpeFADRKTTKtvdgvnvtg 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907206193 294 --SSDFSWAELQRLNAgtwfleRQpfwgakklsgsdRKEAENQ------TIPALEELLKEAAA 348
Cdd:cd08602    81 wfTEDFTLAELKTLRA------RQ------------RLPYRDQsydgqfPIPTFEEIIALAKA 125
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-379 5.98e-12

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: 66.53  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPM--------LAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHD----ERLSRTTNVASVFPERISAHs 294
Cdd:cd08572     2 VIGHRGLGKnyasgslaGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDftisVSEKSKTGSDEGELIEVPIH- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 295 sDFSWAELQRL--NAGTWFLERQPFWGAKKLSGSDRKEAENQTIPALEELLKEAAA---LNLSIMFDLRRPPRNHTYYDT 369
Cdd:cd08572    81 -DLTLEQLKELglQHISALKRKALTRKAKGPKPNPWGMDEHDPFPTLQEVLEQVPKdlgFNIEIKYPQLLEDGEGELTPY 159

                         170
                  ....*....|.
gi 1907206193 370 F-VNQTLEAVL 379
Cdd:cd08572   160 FeRNAFVDTIL 170
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 229-353 7.83e-12

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: 65.01  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 229 GHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVasvfperiSAHSSDFSWAELQRLNAG 308
Cdd:cd08568     4 GHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGV--------DLKVKELTYKELKKLHPG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907206193 309 twflerqpfwgakklsgsdrkeaeNQTIPALEELLK---EAAALNLSI 353
Cdd:cd08568    76 ------------------------GELIPTLEEVFRalpNDAIINVEI 99
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 228-409 1.37e-11

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: 64.35  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 228 VGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFperisahsSDFSWAELQRLNA 307
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAV--------RDLTLAERKALRL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 308 GTWFLErqpfwgakklsgsdrkeaenqTIPALEELLKEAAALNLSIMFDLrRPPRNHTYYDTFVNQTLE----------A 377
Cdd:cd08565    74 RDSFGE---------------------KIPTLEEVLALFAPSGLELHVEI-KTDADGTPYPGAAALAAAtlrrhgllerS 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907206193 378 VLSA----------NVSQAMVLWLPDEDRANVQQRAPRMRQI 409
Cdd:cd08565   132 VLTSfdpavltevrKHPGVRTLGSVDEDMLERLGGELPFLTA 173
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 207-305 6.61e-11

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 63.92  E-value: 6.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 207 LLFISSPCIMKLRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVF 286
Cdd:PRK11143    9 LLAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERF 88

                          90       100
                  ....*....|....*....|...
gi 1907206193 287 PERISA----HSSDFSWAELQRL 305
Cdd:PRK11143   89 PDRARKdgryYAIDFTLDEIKSL 111
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 225-307 1.25e-10

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


Pssm-ID: 176513  Cd Length: 302  Bit Score: 62.69  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASVFPERISAHSS--------- 295
Cdd:cd08571     1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVegqstsgif 80

                          90
                  ....*....|....
gi 1907206193 296 --DFSWAELQRLNA 307
Cdd:cd08571    81 sfDLTWAEIQTLKP 94
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 223-345 1.61e-09

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: 58.64  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 223 PKPGLVGHRGA--PMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMH--DERLSRTTNVASVfpERISAHSSDFS 298
Cdd:cd08564     2 VRPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgtEDDTNPDTSIQLD--DSGFKNINDLS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907206193 299 WAELQRLNAGTWFLERQPFwgakklsgsdRKEAENQTIPALEELLKE 345
Cdd:cd08564    80 LDEITRLHFKQLFDEKPCG----------ADEIKGEKIPTLEDVLVT 116
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 228-442 2.18e-07

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: 51.94  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 228 VGHRG---APMLAPENTLMSLRKTAECGAAvFETDVMVSSDGVPFLMHDERLSRTTNVASVFperisahsSDFSWAELQR 304
Cdd:cd08585     7 IAHRGlhdRDAGIPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRV--------EELTAAELRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 305 LnagtwflerqpfwgakKLSGSDrkeaenQTIPALEELLkEAAALNLSIMFDLRRPPRNHTYYDTFVNQTLE------AV 378
Cdd:cd08585    78 L----------------RLLGTD------EHIPTLDEVL-ELVAGRVPLLIELKSCGGGDGGLERRVLAALKdykgpaAI 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907206193 379 LSANVSQamVLWLPDeDRANV----------QQRAPRMRQIYG--HQGGNWTERPQFLNLPYQDLPALDIKALHQD 442
Cdd:cd08585   135 MSFDPRV--VRWFRK-LAPGIprgqlsegsnDEADPAFWNEALlsALFSNLLTRPDFIAYHLDDLPNPFVTLARAL 207
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 202-345 4.36e-07

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


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 51.83  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 202 IYLM-PLLFISSPCIM-KLRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRT 279
Cdd:cd08612     2 GYIAtSYFLLRNPTLLhKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907206193 280 TNVAsvfperisAHSSDFSWAELQRlnagtwFLERQP------FWGAKKlsGSDRKeaenqtIPALEELLKE 345
Cdd:cd08612    82 CGVD--------KLVSDLNYADLPP------YLEKLEvtfspgDYCVPK--GSDRR------IPLLEEVFEA 131
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 227-305 5.80e-07

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


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 51.26  E-value: 5.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 227 LVGHRGAPM-LAP----------ENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLsrttnVASVFPERISAHSS 295
Cdd:cd08605     2 VIGHRGLGMnRAShqpsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFI-----VVERGGEVESSRIR 76

                          90
                  ....*....|
gi 1907206193 296 DFSWAELQRL 305
Cdd:cd08605    77 DLTLAELKAL 86
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 225-305 2.73e-06

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


Pssm-ID: 176546  Cd Length: 300  Bit Score: 49.26  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 225 PGLVGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNV--------ASVFPErISAHSSD 296
Cdd:cd08604     1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVatskfsnrATTVPE-IGSTSGI 79

                          90
                  ....*....|...
gi 1907206193 297 FS----WAELQRL 305
Cdd:cd08604    80 FTfdltWSEIQTL 92
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 228-379 3.62e-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: 48.83  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 228 VGHRGA--------PMLaPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDerLSRTTNVASVFPERISAHSS---- 295
Cdd:cd08607     3 VGHRGAgnsytaasAVV-RENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHD--FTLRVSLKSKGDSDRDDLLEvpvk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 296 DFSWAELQRLNagtwfLERQPFWG--AKKLSGSDRKEAENQTIPALEELLKEaaaLNLSIMFDL----------RRPPRN 363
Cdd:cd08607    80 DLTYEQLKLLK-----LFHISALKvkEYKSVEEDEDPPEHQPFPTLSDVLES---VPEDVGFNIeikwpqqqkdGSWESE 151

                         170
                  ....*....|....*....
gi 1907206193 364 H-TYYDT--FVNQTLEAVL 379
Cdd:cd08607   152 LfTYFDRnlFVDIILKIVL 170
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 228-285 4.32e-06

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: 47.43  E-value: 4.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907206193 228 VGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTNVASV 285
Cdd:cd08555     2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILP 59
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 228-305 7.16e-06

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176503  Cd Length: 356  Bit Score: 48.19  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 228 VGHRGAPMLAPENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDE-RLSRTTNV---------------ASVFPERIS 291
Cdd:cd08560    20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQcDLHTTTNIlaipelaakctqpftPANATKPAS 99

                          90
                  ....*....|....*.
gi 1907206193 292 AH--SSDFSWAELQRL 305
Cdd:cd08560   100 AEccTSDITLAEFKSL 115
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 225-279 6.72e-04

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 41.66  E-value: 6.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907206193 225 PGLVGHRGAPMLAP--------ENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRT 279
Cdd:cd08606     2 VQVIGHRGLGKNTAerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSET 64
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 224-308 9.45e-04

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: 41.58  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206193 224 KPGLVGHRG----------------APMLAP------ENTLMSLRKTAECGAAVFETDVMVSSDGVPFLMHDERLSRTTN 281
Cdd:cd08613    23 KPKLLAHRGlaqtfdregvendtctAERIDPpthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTD 102

                          90       100
                  ....*....|....*....|....*..
gi 1907206193 282 vasvfperISAHSSDFSWAELQRLNAG 308
Cdd:cd08613   103 --------GSGVTRDHTMAELKTLDIG 121
 
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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