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Conserved domains on  [gi|33457301|ref|NP_878253|]
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glycerophosphodiester phosphodiesterase domain-containing protein 4 [Homo sapiens]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171263)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4) that might play a critical role in the completion of meiosis during male germ cell differentiation

EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 179-491 0e+00

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: 596.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 179 MPLGIYSPCIQEKENLGPKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEV 258
Cdd:cd08610   4 IPLGIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 259 QPESACENPAFFNWDFLSTLNAGKWFVKPelRPFYNMKPLSEADKERARNQSIPTLADLLTLAEKERKFVIFDLHRPPPK 338
Cdd:cd08610  84 QPESACENPAFFNWDFLSTLNAGKWFVKP--RPFYNMKPLSEADKERARNQSIPKLSNFLRLAEKENKLVIFDLYRPPPK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 339 HPLRHTFVRQVVSVILAS-KIEQHLIFWLPAHDRQYVRSVAPGF-QHVGRLVSIETLAKNNISIINVDYKKLFPNGLRDY 416
Cdd:cd08610 162 HPYRHTWIRRVLEVILNEvGIEQHLVLWLPAHDRQYVQSVAPGFkQHVGRKVPIETLLKNNISILNLAYKKLFSNDIRDY 241

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33457301 417 KAANIHINVYTVNEPWLFSLAWCSRINSVTTDNIGLLSQLDHPHFFMTPKFYVFMWLLADIISVLFIVAIFCFHW 491
Cdd:cd08610 242 KAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQLDHPHFFMTPKFYVFMWLLADIISVLFIVLIFCFHW 316
 
Name Accession Description Interval E-value
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 179-491 0e+00

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: 596.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 179 MPLGIYSPCIQEKENLGPKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEV 258
Cdd:cd08610   4 IPLGIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 259 QPESACENPAFFNWDFLSTLNAGKWFVKPelRPFYNMKPLSEADKERARNQSIPTLADLLTLAEKERKFVIFDLHRPPPK 338
Cdd:cd08610  84 QPESACENPAFFNWDFLSTLNAGKWFVKP--RPFYNMKPLSEADKERARNQSIPKLSNFLRLAEKENKLVIFDLYRPPPK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 339 HPLRHTFVRQVVSVILAS-KIEQHLIFWLPAHDRQYVRSVAPGF-QHVGRLVSIETLAKNNISIINVDYKKLFPNGLRDY 416
Cdd:cd08610 162 HPYRHTWIRRVLEVILNEvGIEQHLVLWLPAHDRQYVQSVAPGFkQHVGRKVPIETLLKNNISILNLAYKKLFSNDIRDY 241

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33457301 417 KAANIHINVYTVNEPWLFSLAWCSRINSVTTDNIGLLSQLDHPHFFMTPKFYVFMWLLADIISVLFIVAIFCFHW 491
Cdd:cd08610 242 KAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQLDHPHFFMTPKFYVFMWLLADIISVLFIVLIFCFHW 316
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
196-456 2.99e-43

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 153.49  E-value: 2.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 196 PKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVqpesacenpAFFNWDF 274
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGtGRV---------ADLTLAE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 275 LSTLNAGkwfvkpelrpfynmkplseaDKERARNQSIPTLADLLTLAEKERKFVIfDLhrpppKHP--LRHTFVRQVVSV 352
Cdd:COG0584  72 LRQLDAG--------------------SGPDFAGERIPTLEEVLELVPGDVGLNI-EI-----KSPpaAEPDLAEAVAAL 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 353 ILASKIEQHLI---FWLPAhdRQYVRSVAPGFQhVGRLVS------IETLAKNNISIINVDYKKLFPNGLRDYKAANIHI 423
Cdd:COG0584 126 LKRYGLEDRVIvssFDPEA--LRRLRELAPDVP-LGLLVEelpadpLELARALGADGVGPDYDLLTPELVAAAHAAGLKV 202

                       250       260       270
                ....*....|....*....|....*....|...
gi 33457301 424 NVYTVNEPWLFSLAWCSRINSVTTDNIGLLSQL 456
Cdd:COG0584 203 HVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAV 235
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 203-452 3.04e-23

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: 98.63  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301   203 HRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPEsacenpafFNWDFLSTLNAGK 282
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRD--------LTLEELKRLDIGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301   283 WFVkpelRPFYNMKplseadkerarnQSIPTLADLLTLAEKeRKFVIFDLHRPPP--KHPLRHTFVR---QVVSVILASK 357
Cdd:pfam03009  73 GNS----GPLSGER------------VPFPTLEEVLEFDWD-VGFNIEIKIKPYVeaIAPEEGLIVKdllLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301   358 I-EQHLIFWLPAHDR-QYVRSVAP----GFQHVGRLVSIETLAKNNI--------SIINVDYKKLFPNGLRDYKAANIHI 423
Cdd:pfam03009 136 AdPRRVIFSSFNPDElKRLRELAPklplVFLSSGRAYAEADLLERAAafagapalLGEVALVDEALPDLVKRAHARGLVV 215

                         250       260       270
                  ....*....|....*....|....*....|...
gi 33457301   424 NVYTVNEP----WLFSLAwcsrINSVTTDNIGL 452
Cdd:pfam03009 216 HVWTVNNEdemkRLLELG----VDGVITDRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 196-284 2.00e-16

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 78.83  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301  196 PKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTN-IGEvqpesACENPaffnWDF 274
Cdd:PRK09454   6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNgWGV-----AGELT----WQD 76

                         90
                 ....*....|
gi 33457301  275 LSTLNAGKWF 284
Cdd:PRK09454  77 LAQLDAGSWF 86
 
Name Accession Description Interval E-value
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 179-491 0e+00

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: 596.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 179 MPLGIYSPCIQEKENLGPKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEV 258
Cdd:cd08610   4 IPLGIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 259 QPESACENPAFFNWDFLSTLNAGKWFVKPelRPFYNMKPLSEADKERARNQSIPTLADLLTLAEKERKFVIFDLHRPPPK 338
Cdd:cd08610  84 QPESACENPAFFNWDFLSTLNAGKWFVKP--RPFYNMKPLSEADKERARNQSIPKLSNFLRLAEKENKLVIFDLYRPPPK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 339 HPLRHTFVRQVVSVILAS-KIEQHLIFWLPAHDRQYVRSVAPGF-QHVGRLVSIETLAKNNISIINVDYKKLFPNGLRDY 416
Cdd:cd08610 162 HPYRHTWIRRVLEVILNEvGIEQHLVLWLPAHDRQYVQSVAPGFkQHVGRKVPIETLLKNNISILNLAYKKLFSNDIRDY 241

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33457301 417 KAANIHINVYTVNEPWLFSLAWCSRINSVTTDNIGLLSQLDHPHFFMTPKFYVFMWLLADIISVLFIVAIFCFHW 491
Cdd:cd08610 242 KAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQLDHPHFFMTPKFYVFMWLLADIISVLFIVLIFCFHW 316
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 197-449 1.80e-153

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: 437.89  E-value: 1.80e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 197 KPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAFFNWDFLS 276
Cdd:cd08574   1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHERASMFTWTDLQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 277 TLNAGKWFVKPelRPFYNMKPLSEADKERARNQSIPTLADLLTLAEKERKFVIFDLHRPPPKHPLRHTFVRQVVSVILAS 356
Cdd:cd08574  81 QLNAGQWFLKD--DPFWTASSLSESDREEAGNQSIPSLAELLRLAKKHNKSVIFDLRRPPPNHPYYQSYVNITLDTILAS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 357 KIEQHLIFWLPAHDRQYVRSVAPGF-QHVGRLVSIETLAKNNISIINVDYKKLFPNGLRDYKAANIHINVYTVNEPWLFS 435
Cdd:cd08574 159 GIPQHQVFWLPDEYRALVRKVAPGFqQVSGRKLPVESLRENGISRLNLEYSQLSAQEIREYSKANISVNLYVVNEPWLYS 238

                       250
                ....*....|....
gi 33457301 436 LAWCSRINSVTTDN 449
Cdd:cd08574 239 LLWCSGVQSVTTNA 252
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 197-492 7.53e-115

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: 343.37  E-value: 7.53e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 197 KPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAFFNWDFLS 276
Cdd:cd08608   1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 277 TLNAGKWFVKPElrPFYNMKPLSEADKERARNQSIPTLADLLTLAEKERKFVIFDLHRPPPKHPLRHTFVRQVVSVILAS 356
Cdd:cd08608  81 RLNAGQWFLKDD--PFWTAQSLSPSDRKEAGNQSVCSLAELLELAKRYNASVLLNLRRPPPNHPYHQSWINLTLKTILAS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 357 KIEQHLIFWLPAHDRQYVRSVAPGFQHV-GRLVSIETLAKNNISIINVDYKKLFPNGLRDYKAANIHINVYTVNEPWLFS 435
Cdd:cd08608 159 GIPQEQVMWTPDWQRKLVRKVAPGFQQTsGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYS 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33457301 436 LAWCSRINSVTTDNIGLLSQLDHPHFFMTPKFYVFMWLLADIISVLFIVAIFCFH-WR 492
Cdd:cd08608 239 LLWCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQkWR 296
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 180-487 7.23e-98

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: 298.76  E-value: 7.23e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 180 PLGIYSPCIQEKENLGPKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQ 259
Cdd:cd08609   9 PLAICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVF 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 260 PESACENPAFFNWDFLSTLNAGKWFVkpELRPFYNMKPLSEADKERARNQSIPTLADLLTLAEKERKFVIFDLHRPPPKH 339
Cdd:cd08609  89 PGRDAAGSNNFTWTELKTLNAGSWFL--ERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDLRNENNSH 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 340 PLRHTFVRQVVSVILASKIEQHLIFWLPAHDRQYVRSVAPGFQHV-GRLVSIETLAKNnisIINVDYKKLFPNGLRDYKA 418
Cdd:cd08609 167 VFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQVyGRQKEMLMDGGN---FMNLPYQDLSALEIKELRK 243

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33457301 419 ANIHINVYTVNEPWLFSLAWCSRINSVTTDNIGLLSQLDHPHFFMTPKFYVFMWLLADIISVLFIVAIF 487
Cdd:cd08609 244 DNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKDMSKPIWLLEPNTYLGIWIATDCVSLLLMLWLF 312
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
196-456 2.99e-43

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 153.49  E-value: 2.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 196 PKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVqpesacenpAFFNWDF 274
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGtGRV---------ADLTLAE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 275 LSTLNAGkwfvkpelrpfynmkplseaDKERARNQSIPTLADLLTLAEKERKFVIfDLhrpppKHP--LRHTFVRQVVSV 352
Cdd:COG0584  72 LRQLDAG--------------------SGPDFAGERIPTLEEVLELVPGDVGLNI-EI-----KSPpaAEPDLAEAVAAL 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 353 ILASKIEQHLI---FWLPAhdRQYVRSVAPGFQhVGRLVS------IETLAKNNISIINVDYKKLFPNGLRDYKAANIHI 423
Cdd:COG0584 126 LKRYGLEDRVIvssFDPEA--LRRLRELAPDVP-LGLLVEelpadpLELARALGADGVGPDYDLLTPELVAAAHAAGLKV 202

                       250       260       270
                ....*....|....*....|....*....|...
gi 33457301 424 NVYTVNEPWLFSLAWCSRINSVTTDNIGLLSQL 456
Cdd:COG0584 203 HVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAV 235
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 200-449 1.10e-31

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: 120.45  E-value: 1.10e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDfdlkrttnigevqpesacenpaffnwdflstln 279
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 280 agkwfvkpelrpfynmkplseadkerarnqsIPTLADLLTLAeKERKFVIFDLHRPPPkhplRHTFVRQVVSVILASKIE 359
Cdd:cd08556  48 -------------------------------IPTLEEVLELV-KGGVGLNIELKEPTR----YPGLEAKVAELLREYGLE 91

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 360 QHLIFWLPAHDR-QYVRSVAPGFQ-------HVGRLVSIETLAKNNISIINVDYKKLFPNGLRDYKAANIHINVYTVNEP 431
Cdd:cd08556  92 ERVVVSSFDHEAlRALKELDPEVPtgllvdkPPLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDP 171

                       250
                ....*....|....*...
gi 33457301 432 WLFSLAWCSRINSVTTDN 449
Cdd:cd08556 172 EDARRLLALGVDGIITDD 189
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 200-450 6.14e-30

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: 116.94  E-value: 6.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIgevqpesaCENPAFFNWDFLSTLN 279
Cdd:cd08562   1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNG--------SGAVTELTWAELAQLD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 280 AGKWFVkpelrpfynmkplseadkERARNQSIPTLADLLTLAEKERKFVIFDLhRPPPKHPLRhtFVRQVVSVILAskie 359
Cdd:cd08562  73 AGSWFS------------------PEFAGEPIPTLADVLELARELGLGLNLEI-KPDPGDEAL--TARVVAAALRE---- 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 360 qhlifwLPAHDRQ------------YVRSVAPGFqHVGRLVS------IETLAKNNISIINVDYKKLFPNGLRDYKAANI 421
Cdd:cd08562 128 ------LWPHASKlllssfslealrAARRAAPEL-PLGLLFDtlpadwLELLAALGAVSIHLNYRGLTEEQVKALKDAGY 200

                       250       260
                ....*....|....*....|....*....
gi 33457301 422 HINVYTVNEPWLFSLAWCSRINSVTTDNI 450
Cdd:cd08562 201 KLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 200-431 1.29e-25

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: 104.95  E-value: 1.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVqpesacenpAFFNWDFLSTL 278
Cdd:cd08563   3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGkGYV---------KDLTLEELKKL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 279 NAGKWFvkpelrpfynmkplseadKERARNQSIPTLADLLTLAEKERKFVIFDLhrpppKHPLRHTFV--RQVVSVILAS 356
Cdd:cd08563  74 DAGSWF------------------DEKFTGEKIPTLEEVLDLLKDKDLLLNIEI-----KTDVIHYPGieKKVLELVKEY 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 357 KIEQHLIFWLPAHDR-QYVRSVAPGFQhVGRLV------SIETLAKNNISIINVDYKKLFPNGLRDYKAANIHINVYTVN 429
Cdd:cd08563 131 NLEDRVIFSSFNHESlKRLKKLDPKIK-LALLYetglqdPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVN 209


                ..
gi 33457301 430 EP 431
Cdd:cd08563 210 EE 211
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 200-405 5.35e-24

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: 100.45  E-value: 5.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLG-PENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVqpesacenpAFFNWDFLST 277
Cdd:cd08566   2 VVAHRGGWGAGaPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGkGKV---------SDLTLAEIRK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 278 LNAGKWFvkpelrpfynmkplseadkERARNQSIPTLADLLTLAeKERKFVIFDlhrpppkhpLRHTFVRQVVSVILASK 357
Cdd:cd08566  73 LRLKDGD-------------------GEVTDEKVPTLEEALAWA-KGKILLNLD---------LKDADLDEVIALVKKHG 123

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 33457301 358 IEQHLIFWLPA-HDRQYVRSVAPGFQHVGRLVSIETLAKNNISIINVDY 405
Cdd:cd08566 124 ALDQVIFKSYSeEQAKELRALAPEVMLMPIVRDAEDLDEEEARAIDALN 172
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 203-452 3.04e-23

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: 98.63  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301   203 HRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPEsacenpafFNWDFLSTLNAGK 282
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRD--------LTLEELKRLDIGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301   283 WFVkpelRPFYNMKplseadkerarnQSIPTLADLLTLAEKeRKFVIFDLHRPPP--KHPLRHTFVR---QVVSVILASK 357
Cdd:pfam03009  73 GNS----GPLSGER------------VPFPTLEEVLEFDWD-VGFNIEIKIKPYVeaIAPEEGLIVKdllLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301   358 I-EQHLIFWLPAHDR-QYVRSVAP----GFQHVGRLVSIETLAKNNI--------SIINVDYKKLFPNGLRDYKAANIHI 423
Cdd:pfam03009 136 AdPRRVIFSSFNPDElKRLRELAPklplVFLSSGRAYAEADLLERAAafagapalLGEVALVDEALPDLVKRAHARGLVV 215

                         250       260       270
                  ....*....|....*....|....*....|...
gi 33457301   424 NVYTVNEP----WLFSLAwcsrINSVTTDNIGL 452
Cdd:pfam03009 216 HVWTVNNEdemkRLLELG----VDGVITDRPDT 244
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 198-326 1.25e-22

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: 98.11  E-value: 1.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAFFNWDF--- 274
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKDTGYFVIDFtla 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33457301 275 -LSTLNAGKWFVK--PELRPFYNmkplseadkeraRNQSIPTLADLLTLAEKERK 326
Cdd:cd08559  81 eLKTLRAGSWFNQryPERAPSYY------------GGFKIPTLEEVIELAQGLNK 123
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 200-431 8.01e-21

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: 91.55  E-value: 8.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVQPesacenpafFNWDFLSTL 278
Cdd:cd08561   1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGtGPVAD---------LTLAELRRL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 279 NAGKWFVKPELRPFYNmkplseadkeRARNQSIPTLADLLTLAEKERkfVIFDLHRPPPkhPLRHTFVRQVV------SV 352
Cdd:cd08561  72 DAGYHFTDDGGRTYPY----------RGQGIRIPTLEELFEAFPDVR--LNIEIKDDGP--AAAAALADLIErygaqdRV 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 353 ILASKIEQHLifwlpahdrQYVRSVAP------GFQHVGRLV-----SIETLAKNNI---------SIINVDYKKLfpng 412
Cdd:cd08561 138 LVASFSDRVL---------RRFRRLCPrvatsaGEGEVAAFVlasrlGLGSLYSPPYdalqipvryGGVPLVTPRF---- 204

                       250
                ....*....|....*....
gi 33457301 413 LRDYKAANIHINVYTVNEP 431
Cdd:cd08561 205 VRAAHAAGLEVHVWTVNDP 223
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 200-448 8.04e-21

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: 91.22  E-value: 8.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESacenpaffNWDFLSTLN 279
Cdd:cd08582   1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDL--------TLAELRKLD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 280 AGKWfvkpelrpfynmKPLSEADKerarnqSIPTLADLLTLAEKERKFVIFDLhrpppKHPLR-HTFVRQVVSVILASKI 358
Cdd:cd08582  73 IGSW------------KGESYKGE------KVPTLEEYLAIVPKYGKKLFIEI-----KHPRRgPEAEEELLKLLKESGL 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 359 EQ---HLI-FWLPAHDRqyVRSVAPGF--QHVGRLVSIETLAKNNISIINVD------YKKLFPNGLRDYKAANIHINVY 426
Cdd:cd08582 130 LPeqiVIIsFDAEALKR--VRELAPTLetLWLRNYKSPKEDPRPLAKSGGAAgldlsyEKKLNPAFIKALRDAGLKLNVW 207

                       250       260
                ....*....|....*....|....
gi 33457301 427 TVNEPWlfSLAWCSR--INSVTTD 448
Cdd:cd08582 208 TVDDAE--DAKRLIElgVDSITTN 229
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 200-448 1.27e-20

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: 90.74  E-value: 1.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVQPESacenpaffNWDFLSTL 278
Cdd:cd08570   1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKdGLIIDDS--------TWDELSHL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 279 NAGKwfvKPElrpfynmkplseadkerarnQSIPTLADLLT-LAEKERKFVIFDLHRPPPKHPLRhtfVRQVVSVILASK 357
Cdd:cd08570  73 RTIE---EPH--------------------QPMPTLKDVLEwLVEHELPDVKLMLDIKRDNDPEI---LFKLIAEMLAVK 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 358 --IE---QHLIFWLPAHDR-QYVRSVAPGFQ--HVG--RLVSIETLAKNN----ISIINVDYKKLFPNGLRDY-KAANIH 422
Cdd:cd08570 127 pdLDfwrERIILGLWHLDFlKYGKEVLPGFPvfHIGfsLDYARHFLNYSEklvgISMHFVSLWGPFGQAFLPElKKNGKK 206

                       250       260
                ....*....|....*....|....*.
gi 33457301 423 INVYTVNEPWLFSLAWCSRINSVTTD 448
Cdd:cd08570 207 VFVWTVNTEEDMRYAIRLGVDGVITD 232
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 198-329 1.29e-17

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: 82.75  E-value: 1.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESAcenpafFNWDFLST 277
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPGPVKD------YTLAEIKQ 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33457301 278 LNAGKWFVK--PEL-RPFYnmkplseadkeraRNQSIPTLADLLTLAEKERKFVI 329
Cdd:cd08601  75 LDAGSWFNKayPEYaRESY-------------SGLKVPTLEEVIERYGGRANYYI 116
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 198-365 1.59e-16

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: 79.57  E-value: 1.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI-GEVQPESACENPaffnwdfls 276
Cdd:cd08575   1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGsGLVSDLTYAELP--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 277 TLNAGkWFVKPE-LRPFYnmkplseadKERARNQSIPTLADLLTlAEKERKFVIfDLHRPPPKhplrhTFVRQVVSVILA 355
Cdd:cd08575  72 PLDAG-YGYTFDgGKTGY---------PRGGGDGRIPTLEEVFK-AFPDTPINI-DIKSPDAE-----ELIAAVLDLLEK 134

                       170
                ....*....|
gi 33457301 356 SKiEQHLIFW 365
Cdd:cd08575 135 YK-REDRTVW 143
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 196-284 2.00e-16

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 78.83  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301  196 PKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTN-IGEvqpesACENPaffnWDF 274
Cdd:PRK09454   6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNgWGV-----AGELT----WQD 76

                         90
                 ....*....|
gi 33457301  275 LSTLNAGKWF 284
Cdd:PRK09454  77 LAQLDAGSWF 86
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 198-383 3.10e-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: 75.83  E-value: 3.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTN-IGEVQPESACEnpaffnwdfLS 276
Cdd:cd08580   1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNgSGAVSAYTAAQ---------LA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 277 TLNAGkWFVKPElrpfynmkplsEADKERARNQSIPTLADLLTLAEKerKFVIFDLHRPPPKhplrhTFVRQVVSVILAS 356
Cdd:cd08580  72 TLNAG-YNFKPE-----------GGYPYRGKPVGIPTLEQVLRAFPD--TPFILDMKSLPAD-----PQAKAVARVLERE 132

                       170       180
                ....*....|....*....|....*..
gi 33457301 357 KIEQHLIFWlpAHDRQYVRSVAPGFQH 383
Cdd:cd08580 133 NAWSRVRIY--STNADYQDALAPYPQA 157
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 200-332 3.43e-15

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: 75.37  E-value: 3.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTN----IGEvqpesacenpafFNWDFL 275
Cdd:cd08573   1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDgtglVAE------------LTWEEL 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33457301 276 STLNAGKWFvkpelrpfynmkplseADKERARNQSIPTLADLLTLAEKERKFVIFDL 332
Cdd:cd08573  69 RKLNAAAKH----------------RLSSRFPGEKIPTLEEAVKECLENNLRMIFDV 109
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 200-449 4.76e-15

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: 74.12  E-value: 4.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGevqpesacENPAFFNWDFLSTLN 279
Cdd:cd08579   1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVN--------KKVWDLTLEELKKLT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 280 AGKWFVKpelrpfynmkplseadkerarnQSIPTLADLLTLAEKERKFVIFDLhRPPPKHPlrHTFVRQVVSVILASKIE 359
Cdd:cd08579  73 IGENGHG----------------------AKIPSLDEYLALAKGLKQKLLIEL-KPHGHDS--PDLVEKFVKLYKQNLIE 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 360 QHLIFwlpaH--DRQYVRSV---APGFQhVGRLV--SIETLAKNNISIINVDYKKLFPNGLRDYKAANIHINVYTVNEPW 432
Cdd:cd08579 128 NQHQV----HslDYRVIEKVkklDPKIK-TGYILpfNIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPD 202

                       250
                ....*....|....*..
gi 33457301 433 LFSLAWCSRINSVTTDN 449
Cdd:cd08579 203 DMQRYLAMGVDGIITDY 219
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 200-255 1.87e-14

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: 72.72  E-value: 1.87e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI 255
Cdd:cd08568   2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGV 57
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 200-450 2.41e-14

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 72.36  E-value: 2.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNigevqpesacENPAFFNWDFLS--- 276
Cdd:cd08581   1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTG----------VEGLLHELEDAElds 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 277 -TLNAGKWFVKpelrpfynmkplseadkeRARNQSIPTLADLLTLAekerkfvifdLHRPP------PKHPLRHTF---- 345
Cdd:cd08581  71 lRVAEPARFGS------------------RFAGEPLPSLAAVVQWL----------AQHPQvtlfveIKTESLDRFgler 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 346 VRQVVSVILASKIEQ-HLI-FWLP------AHDRQYVRSVAPGFQHvgrlVSIETLAKNNISIINVDYKKLFPNGlrDYK 417
Cdd:cd08581 123 VVDKVLRALPAVAAQrVLIsFDYDllalakQQGGPRTGWVLPDWDD----ASLAEADELQPDYLFCDKNLLPDTG--DLW 196

                       250       260       270
                ....*....|....*....|....*....|....
gi 33457301 418 AANIHINVYTVNEPWLfSLAWCSR-INSVTTDNI 450
Cdd:cd08581 197 AGTWKWVIYEVNEPAE-ALALAARgVALIETDNI 229
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 200-359 7.87e-13

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: 68.49  E-value: 7.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAFFNWDF--LST 277
Cdd:cd08567   3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLPYEGPALYELTLaeIKQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 278 LNAGkwfvkpELRPFYNMKPLSeADKERARNQSIPTLADLLTLAEK----ERKFVI----FDLHRPPpkHPLRHTFVRQV 349
Cdd:cd08567  83 LDVG------EKRPGSDYAKLF-PEQIPVPGTRIPTLEEVFALVEKygnqKVRFNIetksDPDRDIL--HPPPEEFVDAV 153

                       170
                ....*....|
gi 33457301 350 VSVILASKIE 359
Cdd:cd08567 154 LAVIRKAGLE 163
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 198-381 1.79e-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: 68.09  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEvQPESACEN----------P 267
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVAD-HPEFADRKttktvdgvnvT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 268 AFFNWDF----LSTLNAGKwfVKPELRPFYNMKplseadkerarnQSIPTLADLLTLA-----EKERKFVIFdlhrPPPK 338
Cdd:cd08602  80 GWFTEDFtlaeLKTLRARQ--RLPYRDQSYDGQ------------FPIPTFEEIIALAkaasaATGRTVGIY----PEIK 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 33457301 339 HPlrhTFVRQVvsviLASKIEQHLIFWLPAHDrqYVRSVAPGF 381
Cdd:cd08602 142 HP---TYFNAP----LGLPMEDKLLETLKKYG--YTGKKAPVF 175
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 202-355 8.87e-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: 65.76  E-value: 8.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 202 GHRGA---------PMLGpENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDL----KRTTNIGEVQPESACENPa 268
Cdd:cd08572   4 GHRGLgknyasgslAGIR-ENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvseKSKTGSDEGELIEVPIHD- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 269 fFNWDFLSTLNAGK---WFVKPELRPFYNMKPLSEADKErarNQSIPTLADLLTLAEKERKFVI---FDLHRPPPKHPLR 342
Cdd:cd08572  82 -LTLEQLKELGLQHisaLKRKALTRKAKGPKPNPWGMDE---HDPFPTLQEVLEQVPKDLGFNIeikYPQLLEDGEGELT 157

                       170
                ....*....|....
gi 33457301 343 HTF-VRQVVSVILA 355
Cdd:cd08572 158 PYFeRNAFVDTILA 171
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 200-258 4.62e-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: 62.81  E-value: 4.62e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 200 IFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTN-IGEV 258
Cdd:cd08565   1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHgTGAV 60
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 198-322 1.49e-10

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: 62.41  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAF----FNWD 273
Cdd:cd08600   1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRYyvidFTLD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33457301 274 FLSTLNAGKWFvKPELR---PFY-NMKPLSEADKErarnqsIPTLADLLTLAE 322
Cdd:cd08600  81 ELKSLSVTERF-DIENGkkvQVYpNRFPLWKSDFK------IHTLEEEIELIQ 126
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 202-249 3.22e-09

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: 58.07  E-value: 3.22e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33457301 202 GHRGA--------PMLgPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDL 249
Cdd:cd08607   4 GHRGAgnsytaasAVV-RENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTL 58
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 203-255 7.71e-09

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: 57.22  E-value: 7.71e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 33457301 203 HRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNI 255
Cdd:cd08612  32 HRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGV 84
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 196-318 4.02e-08

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: 54.40  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 196 PKPTIFGHRGA--PMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAFFNWD 273
Cdd:cd08564   2 VRPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEDDTNPDTSIQLDDSGFKNINDLSLD 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 33457301 274 FLSTLNAGKWFVKpelrpfyNMKPLSEADKERarnqsIPTLADLL 318
Cdd:cd08564  82 EITRLHFKQLFDE-------KPCGADEIKGEK-----IPTLEDVL 114
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 198-323 1.36e-07

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: 53.11  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQ--------PESACENPAF 269
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKfsnrattvPEIGSTSGIF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33457301 270 -FN--WDFLSTLnagkwfvKPELRPFYNMKPLSEadKERARNQ-SIPTLADLLTLAEK 323
Cdd:cd08604  81 tFDltWSEIQTL-------KPAISNPYSVTGLFR--NPANKNAgKFLTLSDFLDLAKN 129
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 211-262 8.29e-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: 50.01  E-value: 8.29e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 33457301 211 PENTMMSFEKAVEHGaHGLETDIHLSYDHVPFLMHDFDLKRTTNiGEVQPES 262
Cdd:cd08585  20 PENSLSAFRAAAEAG-YGIELDVQLTADGEVVVFHDDNLKRLTG-VEGRVEE 69
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 198-321 9.43e-07

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: 50.75  E-value: 9.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33457301 198 PTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESA---CENPAF----- 269
Cdd:cd08571   1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKktyVVEGQStsgif 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33457301 270 ---FNWDFLSTLNA--GKWFVKPELRPFYnmkplseadkeraRNQ-SIPTLADLLTLA 321
Cdd:cd08571  81 sfdLTWAEIQTLKPiiSNPFSVLFRNPRN-------------DNAgKILTLEDFLTLA 125
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 202-258 1.03e-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: 48.97  E-value: 1.03e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33457301 202 GHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEV 258
Cdd:cd08555   3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILP 59
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 196-274 4.82e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 48.90  E-value: 4.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33457301  196 PKPTIFGHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRTTNIGEVQPESACENPAFFNWDF 274
Cdd:PRK11143  25 AEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERFPDRARKDGRYYAIDF 103
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 202-267 4.44e-05

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: 45.88  E-value: 4.44e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33457301 202 GHRGAPMLGPENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDF-DLKRTTNIGEVqPESA--CENP 267
Cdd:cd08560  21 GHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQcDLHTTTNILAI-PELAakCTQP 88
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 198-252 4.52e-05

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: 45.51  E-value: 4.52e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33457301 198 PTIFGHRGapmLGP-----------ENTMMSFEKAVEHGAHGLETDIHLSYDHVPFLMHDFDLKRT 252
Cdd:cd08606   2 VQVIGHRG---LGKntaerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSET 64
 
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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