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Conserved domains on  [gi|1324321274|ref|WP_101508437|]
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glycerophosphoryl diester phosphodiesterase membrane domain-containing protein [Paraclostridium sordellii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpQ1 COG4781
Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain ...
 2-602 6.83e-84

Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain [Lipid transport and metabolism];


:

Pssm-ID: 443811 [Multi-domain]  Cd Length: 575  Bit Score: 273.91  E-value: 6.83e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274   2 AEDKKKYINKLPSFKIRRIWLYTKYQLITKLILAIAIFPLYRFAIEKLIQSSGRTNISSGDYLSFLFSFNGAGLLILTLI 81
Cdd:COG4781     1 MMKIKKLLKNTLKLFKKNWFRYLLFELIYKLLIAFVFIPLLSFIFNFLLKASGIPYLTNDNLLEILTSPLGLIFLLLLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274  82 LMTILIAMDINVFIIMSALIKENRiYMRTRDMFYVAIKSIKSFVSPHGFLLMVYVSLIFPIIGLGITISPMKNFQIPNFI 161
Cdd:COG4781    81 LLLLFIFFEFTFLIIGAYFILRGQ-PISLKELFKRTFKKLKKLFGPQLLLFLFYFLLIIPFANIGLSSSLLSKIKIPEFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 162 TSVIYSKPLYEIGYMTLILVLTFIGYKLIFSFHYIVICGYSAKESIKKSSQLIKRYKLDFFKNFIISEGLRILIAFIFIV 241
Cdd:COG4781   160 TDEIFKTPLGIILYILFYLILFYLAIRLIFTLPLFILERKSFKEAIKESWQLTKKNFFRLLLLLILINLLIILIVVLIIF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 242 VLMVLAFEVSSYFISNQEdyrIALIFSLLLILEIITYILFIFVPLMIERLTNLFYKYNekdnnpvviafdikaytwnkeg 321
Cdd:COG4781   240 LIYLLQLLVDSFPPGNAL---ITASINLTLLQLLTFLFTVIFSVLIIQVLVALYYQQS---------------------- 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 322 nnkiKIKTKIVVILLLAITLIFnllFSVALSVNFDILFKQDRKIDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQ 401
Cdd:COG4781   295 ----KRKKKALVIVLLVIFLIF---SGINNSPSTIILIILGRAVGGGNNTASLALAAALTIALLADAIILDADQTVVVVV 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 402 RTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFDISNKKQKVATLDEMINLSKGKIGLFIELKGASADKKM 481
Cdd:COG4781   368 VVLDLLLLLAKDKNIKRLTLLELLELILVSGGSKKISSLFEDLIAAKKLKILLLLEVIKKTGKTDEDADLVTVAKKKKKL 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 482 ADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLYFFSVGERDKMVGDYLIMEEREATLDNIYKIHQAKKKA 561
Cdd:COG4781   448 EARLAVEVSDDSAEDIKVEKSLPKEGVIIILLINNFTKTEADVFVSEYESTSLLDVLLVTEEAKAVYVAIVNIEKTDERE 527

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1324321274 562 VVWTVNTKQSMEKFINMPVDGIITDYVKELKHEIQVKQNRS 602
Cdd:COG4781   528 KMKNKNVIIIIDIKDVLAEIEILKDDKEYIPSLIDLDLVFL 568
 
Name Accession Description Interval E-value
UgpQ1 COG4781
Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain ...
 2-602 6.83e-84

Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain [Lipid transport and metabolism];


Pssm-ID: 443811 [Multi-domain]  Cd Length: 575  Bit Score: 273.91  E-value: 6.83e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274   2 AEDKKKYINKLPSFKIRRIWLYTKYQLITKLILAIAIFPLYRFAIEKLIQSSGRTNISSGDYLSFLFSFNGAGLLILTLI 81
Cdd:COG4781     1 MMKIKKLLKNTLKLFKKNWFRYLLFELIYKLLIAFVFIPLLSFIFNFLLKASGIPYLTNDNLLEILTSPLGLIFLLLLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274  82 LMTILIAMDINVFIIMSALIKENRiYMRTRDMFYVAIKSIKSFVSPHGFLLMVYVSLIFPIIGLGITISPMKNFQIPNFI 161
Cdd:COG4781    81 LLLLFIFFEFTFLIIGAYFILRGQ-PISLKELFKRTFKKLKKLFGPQLLLFLFYFLLIIPFANIGLSSSLLSKIKIPEFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 162 TSVIYSKPLYEIGYMTLILVLTFIGYKLIFSFHYIVICGYSAKESIKKSSQLIKRYKLDFFKNFIISEGLRILIAFIFIV 241
Cdd:COG4781   160 TDEIFKTPLGIILYILFYLILFYLAIRLIFTLPLFILERKSFKEAIKESWQLTKKNFFRLLLLLILINLLIILIVVLIIF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 242 VLMVLAFEVSSYFISNQEdyrIALIFSLLLILEIITYILFIFVPLMIERLTNLFYKYNekdnnpvviafdikaytwnkeg 321
Cdd:COG4781   240 LIYLLQLLVDSFPPGNAL---ITASINLTLLQLLTFLFTVIFSVLIIQVLVALYYQQS---------------------- 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 322 nnkiKIKTKIVVILLLAITLIFnllFSVALSVNFDILFKQDRKIDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQ 401
Cdd:COG4781   295 ----KRKKKALVIVLLVIFLIF---SGINNSPSTIILIILGRAVGGGNNTASLALAAALTIALLADAIILDADQTVVVVV 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 402 RTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFDISNKKQKVATLDEMINLSKGKIGLFIELKGASADKKM 481
Cdd:COG4781   368 VVLDLLLLLAKDKNIKRLTLLELLELILVSGGSKKISSLFEDLIAAKKLKILLLLEVIKKTGKTDEDADLVTVAKKKKKL 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 482 ADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLYFFSVGERDKMVGDYLIMEEREATLDNIYKIHQAKKKA 561
Cdd:COG4781   448 EARLAVEVSDDSAEDIKVEKSLPKEGVIIILLINNFTKTEADVFVSEYESTSLLDVLLVTEEAKAVYVAIVNIEKTDERE 527

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1324321274 562 VVWTVNTKQSMEKFINMPVDGIITDYVKELKHEIQVKQNRS 602
Cdd:COG4781   528 KMKNKNVIIIIDIKDVLAEIEILKDDKEYIPSLIDLDLVFL 568
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 367-588 6.16e-69

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: 222.81  E-value: 6.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFdis 446
Cdd:cd08579     1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGENG--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 nKKQKVATLDEMINLSKG-KIGLFIELKGASAD-KKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLY 524
Cdd:cd08579    78 -HGAKIPSLDEYLALAKGlKQKLLIELKPHGHDsPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKIKTGYIL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1324321274 525 FFSVGERDKMVGDYLIMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDYV 588
Cdd:cd08579   157 PFNIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 370-588 7.72e-30

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: 117.89  E-value: 7.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 370 HRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFD--ISN 447
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSgpLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 448 KKQKVATLDEMINLSKG-------KIGLF---IELKGASADKKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPN 517
Cdd:pfam03009  81 ERVPFPTLEEVLEFDWDvgfnieiKIKPYveaIAPEEGLIVKDLLLSVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 518 IETGYLYF-FSVGERDKMVGDYL----------IMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITD 586
Cdd:pfam03009 161 LPLVFLSSgRAYAEADLLERAAAfagapallgeVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 1324321274 587 YV 588
Cdd:pfam03009 241 RP 242
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 340-489 4.88e-15

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 77.02  E-value: 4.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 340 TLIFNLLFSVALSVNFDILFKQDRKIdIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRL 419
Cdd:PRK11143    3 NLSLALLLAALLAGSAAAAADSAEKI-VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 420 TGEA-RSPK-----------DMTLKEIKSLWIKNEFDISNKKQ---------------KVATLDEMI------NLSKGK- 465
Cdd:PRK11143   82 TDVAeRFPDrarkdgryyaiDFTLDEIKSLKFTEGFDIENGKKvqvypgrfpmgksdfRVHTFEEEIefiqglNHSTGKn 161

                         170       180
                  ....*....|....*....|....
gi 1324321274 466 IGLFIELKGASADKKMADDVVKKV 489
Cdd:PRK11143  162 IGIYPEIKAPWFHHQEGKDIAAKV 185
 
Name Accession Description Interval E-value
UgpQ1 COG4781
Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain ...
 2-602 6.83e-84

Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain [Lipid transport and metabolism];


Pssm-ID: 443811 [Multi-domain]  Cd Length: 575  Bit Score: 273.91  E-value: 6.83e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274   2 AEDKKKYINKLPSFKIRRIWLYTKYQLITKLILAIAIFPLYRFAIEKLIQSSGRTNISSGDYLSFLFSFNGAGLLILTLI 81
Cdd:COG4781     1 MMKIKKLLKNTLKLFKKNWFRYLLFELIYKLLIAFVFIPLLSFIFNFLLKASGIPYLTNDNLLEILTSPLGLIFLLLLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274  82 LMTILIAMDINVFIIMSALIKENRiYMRTRDMFYVAIKSIKSFVSPHGFLLMVYVSLIFPIIGLGITISPMKNFQIPNFI 161
Cdd:COG4781    81 LLLLFIFFEFTFLIIGAYFILRGQ-PISLKELFKRTFKKLKKLFGPQLLLFLFYFLLIIPFANIGLSSSLLSKIKIPEFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 162 TSVIYSKPLYEIGYMTLILVLTFIGYKLIFSFHYIVICGYSAKESIKKSSQLIKRYKLDFFKNFIISEGLRILIAFIFIV 241
Cdd:COG4781   160 TDEIFKTPLGIILYILFYLILFYLAIRLIFTLPLFILERKSFKEAIKESWQLTKKNFFRLLLLLILINLLIILIVVLIIF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 242 VLMVLAFEVSSYFISNQEdyrIALIFSLLLILEIITYILFIFVPLMIERLTNLFYKYNekdnnpvviafdikaytwnkeg 321
Cdd:COG4781   240 LIYLLQLLVDSFPPGNAL---ITASINLTLLQLLTFLFTVIFSVLIIQVLVALYYQQS---------------------- 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 322 nnkiKIKTKIVVILLLAITLIFnllFSVALSVNFDILFKQDRKIDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQ 401
Cdd:COG4781   295 ----KRKKKALVIVLLVIFLIF---SGINNSPSTIILIILGRAVGGGNNTASLALAAALTIALLADAIILDADQTVVVVV 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 402 RTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFDISNKKQKVATLDEMINLSKGKIGLFIELKGASADKKM 481
Cdd:COG4781   368 VVLDLLLLLAKDKNIKRLTLLELLELILVSGGSKKISSLFEDLIAAKKLKILLLLEVIKKTGKTDEDADLVTVAKKKKKL 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 482 ADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLYFFSVGERDKMVGDYLIMEEREATLDNIYKIHQAKKKA 561
Cdd:COG4781   448 EARLAVEVSDDSAEDIKVEKSLPKEGVIIILLINNFTKTEADVFVSEYESTSLLDVLLVTEEAKAVYVAIVNIEKTDERE 527

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1324321274 562 VVWTVNTKQSMEKFINMPVDGIITDYVKELKHEIQVKQNRS 602
Cdd:COG4781   528 KMKNKNVIIIIDIKDVLAEIEILKDDKEYIPSLIDLDLVFL 568
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 367-588 6.16e-69

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: 222.81  E-value: 6.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFdis 446
Cdd:cd08579     1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGENG--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 nKKQKVATLDEMINLSKG-KIGLFIELKGASAD-KKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLY 524
Cdd:cd08579    78 -HGAKIPSLDEYLALAKGlKQKLLIELKPHGHDsPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKIKTGYIL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1324321274 525 FFSVGERDKMVGDYLIMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDYV 588
Cdd:cd08579   157 PFNIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
363-596 2.10e-59

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 198.55  E-value: 2.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 363 RKIDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNE 442
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 443 FDISNkkQKVATLDEMINLSKGKIGLFIELKGASAD-KKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETG 521
Cdd:COG0584    81 PDFAG--ERIPTLEEVLELVPGDVGLNIEIKSPPAAePDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1324321274 522 YLYFFSVGE----RDKMVGDYLIMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDYVKELKHEIQ 596
Cdd:COG0584   159 LLVEELPADplelARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLR 237
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 367-587 1.13e-42

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: 151.65  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDknfkrltgearspkdmtlkeikslwiknefdis 446
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 nkkqkVATLDEMINLSKGKIGLFIELKGASADKKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLYF- 525
Cdd:cd08556    48 -----IPTLEEVLELVKGGVGLNIELKEPTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVDk 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1324321274 526 ----FSVGERDKMVG-DYLIMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDY 587
Cdd:cd08556   123 ppldPLLAELARALGaDAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 367-587 4.12e-40

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: 146.31  E-value: 4.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFDIS 446
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 NKKQKVATLDEMINL-SKGKIGLFIELKGASADKKMADDVVKKVKENKI-EKEAVILSLDYSLIQYIEKKYPNIETGYLY 524
Cdd:cd08582    81 YKGEKVPTLEEYLAIvPKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLlPEQIVIISFDAEALKRVRELAPTLETLWLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1324321274 525 FFsvgERDKMVGDYLIMEEREATLD----------NIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDY 587
Cdd:cd08582   161 NY---KSPKEDPRPLAKSGGAAGLDlsyekklnpaFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNR 230
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 365-587 1.89e-36

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: 137.06  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 365 IDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHD----------KNFKRLTGEARSPKDMTLKEI 434
Cdd:cd08567     1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDpklnpditrdPDGAWLPYEGPALYELTLAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 435 KSLWI--KNEFDISNKK---------QKVATLDEMINLSKG----KIGLFIELK------GASAD-KKMADDVVKKVKEN 492
Cdd:cd08567    81 KQLDVgeKRPGSDYAKLfpeqipvpgTRIPTLEEVFALVEKygnqKVRFNIETKsdpdrdILHPPpEEFVDAVLAVIRKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 493 KIEKEAVILSLDYSLIQYIEKKYPNIETGYLYFF-SVGERDKMV----GDYLIMEEREATLDNIYKIHQAKKKAVVWTVN 567
Cdd:cd08567   161 GLEDRVVLQSFDWRTLQEVRRLAPDIPTVALTEEtTLGNLPRAAkklgADIWSPYFTLVTKELVDEAHALGLKVVPWTVN 240

                         250       260
                  ....*....|....*....|
gi 1324321274 568 TKQSMEKFINMPVDGIITDY 587
Cdd:cd08567   241 DPEDMARLIDLGVDGIITDY 260
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 367-587 4.25e-31

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: 121.12  E-value: 4.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFDIS 446
Cdd:cd08563     3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 NKKQKVATLDEMINLSKGKIGLF-IELK-GASADKKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLY 524
Cdd:cd08563    83 FTGEKIPTLEEVLDLLKDKDLLLnIEIKtDVIHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKLALLY 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1324321274 525 ---FFSVGERDKMVGDYLIMEEREATLDNIYK-IHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDY 587
Cdd:cd08563   163 etgLQDPKDYAKKIGADSLHPDFKLLTEEVVEeLKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNY 229
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 370-588 7.72e-30

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: 117.89  E-value: 7.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 370 HRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFD--ISN 447
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSgpLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 448 KKQKVATLDEMINLSKG-------KIGLF---IELKGASADKKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPN 517
Cdd:pfam03009  81 ERVPFPTLEEVLEFDWDvgfnieiKIKPYveaIAPEEGLIVKDLLLSVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 518 IETGYLYF-FSVGERDKMVGDYL----------IMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITD 586
Cdd:pfam03009 161 LPLVFLSSgRAYAEADLLERAAAfagapallgeVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 1324321274 587 YV 588
Cdd:pfam03009 241 RP 242
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 367-518 4.25e-29

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: 115.86  E-value: 4.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGA-ENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFDi 445
Cdd:cd08566     2 VVAHRGGWGAGApENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDG- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1324321274 446 SNKKQKVATLDEMINLSKGKIGLFIELKGASadkkmADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNI 518
Cdd:cd08566    81 EVTDEKVPTLEEALAWAKGKILLNLDLKDAD-----LDEVIALVKKHGALDQVIFKSYSEEQAKELRALAPEV 148
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 367-592 7.72e-29

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: 115.05  E-value: 7.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSL-----WIKN 441
Cdd:cd08561     1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLdagyhFTDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 442 E---FDISNKKQKVATLDEM--------INlskgkiglfIELKGasADKKMADDVVKKVKENKIEKEAVILSLDYSLIQY 510
Cdd:cd08561    81 GgrtYPYRGQGIRIPTLEELfeafpdvrLN---------IEIKD--DGPAAAAALADLIERYGAQDRVLVASFSDRVLRR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 511 IEKKYPNIETGY----------LYFFSVGERDKMVGDYLIMEERE-----ATLDNIYKIHQAKKKAVVWTVNTKQSMEKF 575
Cdd:cd08561   150 FRRLCPRVATSAgegevaafvlASRLGLGSLYSPPYDALQIPVRYggvplVTPRFVRAAHAAGLEVHVWTVNDPAEMRRL 229

                         250
                  ....*....|....*..
gi 1324321274 576 INMPVDGIITDYVKELK 592
Cdd:cd08561   230 LDLGVDGIITDRPDLLL 246
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 367-592 9.61e-27

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: 109.33  E-value: 9.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT-GEARSP-KDMTLKEIKSL----WIk 440
Cdd:cd08601     3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTnIERPGPvKDYTLAEIKQLdagsWF- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 441 NEFDISNKK-----QKVATLDEMINLSKGKIGLFIELKGASADKKMADDVVKKVKENKIEKEA------VILSLDYSLIQ 509
Cdd:cd08601    82 NKAYPEYAResysgLKVPTLEEVIERYGGRANYYIETKSPDLYPGMEEKLLATLDKYGLLTDNlkngqvIIQSFSKESLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 510 YIEKKYPNIETGYLYFFSVGERD-----KMVGDYLI---MEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVD 581
Cdd:cd08601   162 KLHQLNPNIPLVQLLWYGEGAETydkwlDEIKEYAIgigPSIADADPWMVHLIHKKGLLVHPYTVNEKADMIRLINWGVD 241

                         250
                  ....*....|.
gi 1324321274 582 GIITDYVKELK 592
Cdd:cd08601   242 GMFTNYPDRLK 252
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 367-587 1.94e-24

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: 103.89  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT-GEARSP-----------KDMTLKEI 434
Cdd:cd08559     3 VIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTnVAEHFPfrgrkdtgyfvIDFTLAEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 435 KSL----W----IKNEFDISNKKQKVATLDEMINLSKG-------KIGLFIELK----GASADKKMADDVVKKVKENKIE 495
Cdd:cd08559    83 KTLragsWfnqrYPERAPSYYGGFKIPTLEEVIELAQGlnkstgrNVGIYPETKhptfHKQEGPDIEEKLLEVLKKYGYT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 496 KE---AVILSLDYSLIQYIEKKYPNI----------------ETGYLYFFSVGERDKM------VG---DYLIMEEREAT 547
Cdd:cd08559   163 GKndpVFIQSFEPESLKRLRNETPDIplvqlidygdwaetdkKYTYAWLTTDAGLKEIakyadgIGpwkSLIIPEDSNGL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1324321274 548 L---DNIYKIHQAKKKAVVWTVNT---------KQSMEKFIN-MPVDGIITDY 587
Cdd:cd08559   243 LvptDLVKDAHKAGLLVHPYTFRNenlflapdfKQDMDALYNaAGVDGVFTDF 295
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 367-587 1.04e-23

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: 99.99  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSL----Wikne 442
Cdd:cd08562     1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLdagsW---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 443 FDISNKKQKVATLDEMINL-SKGKIGLFIELKGASADKKMADDVVKKV-KENKIEKEAVIL-SLDYSLIQYIEKKYPNIE 519
Cdd:cd08562    77 FSPEFAGEPIPTLADVLELaRELGLGLNLEIKPDPGDEALTARVVAAAlRELWPHASKLLLsSFSLEALRAARRAAPELP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1324321274 520 TGYLYffsvgerDKMVGD-----------YLIMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDY 587
Cdd:cd08562   157 LGLLF-------DTLPADwlellaalgavSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDR 228
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 367-588 1.49e-21

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: 93.52  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNefdis 446
Cdd:cd08568     2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPGG----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 nkkQKVATLDEMI-NLSKGKIgLFIELKgasaDKKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYPNIETGYLyf 525
Cdd:cd08568    77 ---ELIPTLEEVFrALPNDAI-INVEIK----DIDAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLL-- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 526 fsVGERDKmvgdyLIMEEREATLDNIYKIH---QA-------------------KKKAVVWTVNTKQSMEKFINMpVDGI 583
Cdd:cd08568   147 --IGEEEE-----GFSIPELHEKLKLYSLHvpiDAigyigfekfvellrllrklGLKIVLWTVNDPELVPKLKGL-VDGV 218


                  ....*
gi 1324321274 584 ITDYV 588
Cdd:cd08568   219 ITDDV 223
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 367-588 5.40e-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: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 92.01  E-value: 5.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNE--FD 444
Cdd:cd08581     1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEParFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 445 ISNKKQKVATLDEMINL--SKGKIGLFIELKGASADKKMADDVVKKVKE--NKIEKEAVILSLDYSLIQYIeKKYPNIET 520
Cdd:cd08581    81 SRFAGEPLPSLAAVVQWlaQHPQVTLFVEIKTESLDRFGLERVVDKVLRalPAVAAQRVLISFDYDLLALA-KQQGGPRT 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1324321274 521 GYLY----FFSVGERDKMVGDYLIMEEReaTLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITDYV 588
Cdd:cd08581   160 GWVLpdwdDASLAEADELQPDYLFCDKN--LLPDTGDLWAGTWKWVIYEVNEPAEALALAARGVALIETDNI 229
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 367-586 1.24e-20

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: 91.31  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRlTGEARSP-KDMTLKEIKSLWIKNEFDi 445
Cdd:cd08565     1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDR-TTHGTGAvRDLTLAERKALRLRDSFG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 446 snkkQKVATLDEMINLSK-GKIGLFIELKGASADK---KMADDVVKKVKENKIEKEAVILSLDYSLIQYIeKKYPNIETg 521
Cdd:cd08565    79 ----EKIPTLEEVLALFApSGLELHVEIKTDADGTpypGAAALAAATLRRHGLLERSVLTSFDPAVLTEV-RKHPGVRT- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 522 ylyFFSVGER-DKMVGDYLIMEEREATLDNIYKIHQAKKKAV--------------VWTVNTKQSMEKFINMPVDGIITD 586
Cdd:cd08565   153 ---LGSVDEDmLERLGGELPFLTATALKAHIVAVEQSLLAATwelvraavpglrlgVWTVNDDSLIRYWLACGVRQLTTD 229
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-587 1.26e-20

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: 91.90  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKNEFD-- 444
Cdd:cd08575     3 HIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYTfd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 445 -------ISNKKQKVATLDEMinLSK-GKIGLFIELKGASADkKMADDVVKKVKENKIEKEAVILSLDYSLIQYIEKKYP 516
Cdd:cd08575    83 ggktgypRGGGDGRIPTLEEV--FKAfPDTPINIDIKSPDAE-ELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 517 NI-----------------ETGYLYFFSVGE------RDKMV------------GDYLIMeeREATLDniykiHQAKKKA 561
Cdd:cd08575   160 NLfesfsmtrclllylalgYTGLLPFVPIKEsffeipRPVIVletftlgegasiVAALLW--WPNLFD-----HLRKRGI 232

                         250       260
                  ....*....|....*....|....*...
gi 1324321274 562 --VVWTVNTKQSMEKFINMPVDGIITDY 587
Cdd:cd08575   233 qvYLWVLNDEEDFEEAFDLGADGVMTDS 260
GPDPase_memb pfam10110
Membrane domain of glycerophosphoryl diester phosphodiesterase; Members of this family ...
 20-342 1.55e-19

Membrane domain of glycerophosphoryl diester phosphodiesterase; Members of this family comprise the membrane domain of the prokaryotic enzyme glycerophosphoryl diester phosphodiesterase.


Pssm-ID: 431062  Cd Length: 321  Bit Score: 89.99  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274  20 IWLYTKYQLITKLILAIAIFPLYRFAIEKLIQSSGRTNISSGDYLSFL-FSFNGAGLLILTLILMTILIAMDINVFIIMS 98
Cdd:pfam10110  12 WFRYLLLFLLLKLLLSFIIIPLFTWITNFLLKVGGIPYLSYNNLLSILtQHPLVILLLILLLLLILLLIYFEFAFLLLGI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274  99 ALIKENRIYmRTRDMFYVAIKSIKSFVSPHGFLLMVYVSLIFPIIGLGITISPMKNFQIPNFITSVIYSKP-LYEIGYMT 177
Cdd:pfam10110  92 YQILKREKI-SLKALFKESFKRLRKLRGGSLLFFLIYFLLIIPFANLGFSSPLLNKIKIPAFIVDYILTTRiWIWLGYLI 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 178 LILVLTFIGYKLIFSFHYIVICGYSAKESIKKSSQLIKRyklDFFKNFIISEGLRILIAFIFIVVLMVLAFEVSSYFISN 257
Cdd:pfam10110 171 FYLIIFYLGIRLIFTLPLIILEGKSFREAIKKSWQLTKK---NFWRILLGRLLLILIIGILVTVIGYLLIYLLQLLLDTF 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 258 QEDYRIALIFSLLLILEIITYILFIFVPLMIerlTNLFYKYNEKDNNPVVIAFdikaytwnKEGNNKIKIKTKIVVILLL 337
Cdd:pfam10110 248 PPGYSLILAIINLTLLQIISFFILPISSVII---TSLLVKQLNSEGELPAPPL--------KKKKLFIFSKIVINLLVLL 316


                  ....*
gi 1324321274 338 AITLI 342
Cdd:pfam10110 317 GIGFI 321
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 367-588 1.99e-17

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: 81.88  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTG-EARSPKDMTLKEIKSLWIKNEfdi 445
Cdd:cd08570     1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGkDGLIIDDSTWDELSHLRTIEE--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 446 snKKQKVATLDEMINL-----SKGkIGLFIELK---GASADKKMADDVVKKVKENKIEKEAVIL---SLDYslIQYIEKK 514
Cdd:cd08570    78 --PHQPMPTLKDVLEWlveheLPD-VKLMLDIKrdnDPEILFKLIAEMLAVKPDLDFWRERIILglwHLDF--LKYGKEV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 515 YPNIETGY--------LYFFSVGERDKMVGDYLIMEEREATLDNIYKIHQAKKKAVVWTVNTKQSMEKFINMPVDGIITD 586
Cdd:cd08570   153 LPGFPVFHigfsldyaRHFLNYSEKLVGISMHFVSLWGPFGQAFLPELKKNGKKVFVWTVNTEEDMRYAIRLGVDGVITD 232


                  ..
gi 1324321274 587 YV 588
Cdd:cd08570   233 DP 234
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-588 2.21e-16

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: 79.22  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWI--KNEFD 444
Cdd:cd08573     1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAaaKHRLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 445 ISNKKQKVATLDEMINLS-KGKIGLFIELKGASadKKMADDVVKK-VKENKIEKEAVILSLDYSLIQYIEKKYPNIETG- 521
Cdd:cd08573    81 SRFPGEKIPTLEEAVKEClENNLRMIFDVKSNS--SKLVDALKNLfKKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGl 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 522 ------YLYFFSVGERDK---------MVGDYLIMEE----------------REATLDNIYKIHQAKK--KAVVWTVNT 568
Cdd:cd08573   159 twrpwfLSYTDDEGGPRRksgwkhflySMLDVILEWSlhswlpyflgvsalliHKDDISSAYVRYWRARgiRVIAWTVNT 238

                         250       260
                  ....*....|....*....|...
gi 1324321274 569 ---KQSMEKFINMPvdgIITDYV 588
Cdd:cd08573   239 pteKQYFAKTLNVP---YITDSL 258
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 368-593 2.25e-16

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: 79.95  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 368 IAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKD-------MTLKEIKSLWIK 440
Cdd:cd08612    30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDlnyadlpPYLEKLEVTFSP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 441 NEF-DISNKKQKVATLDEM--------INlskgkiglfIELKGASAD--KKMADDVVKKVKENKIekeaVILSLDYSLIQ 509
Cdd:cd08612   110 GDYcVPKGSDRRIPLLEEVfeafpdtpIN---------IDIKVENDEliKKVSDLVRKYKREDIT----VWGSFNDEIVK 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 510 YIEKKYPNIE----------------TGYLYFFSVGER----------------DKMVG---------DYLIMEEreatl 548
Cdd:cd08612   177 KCHKENPNIPlffslkrvllllllyyTGLLPFIPIKESfleipmpsiflktyfpKSMSRlnrfvlfliDWLLMRP----- 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1324321274 549 dNIYKIHQAKKKAVV-WTVNTKQSMEKFINMPVDGIITDYVKELKH 593
Cdd:cd08612   252 -SLFRHLQKRGIQVYgWVLNDEEEFERAFELGADGVMTDYPTKLRE 296
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 340-489 4.88e-15

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 77.02  E-value: 4.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 340 TLIFNLLFSVALSVNFDILFKQDRKIdIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRL 419
Cdd:PRK11143    3 NLSLALLLAALLAGSAAAAADSAEKI-VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 420 TGEA-RSPK-----------DMTLKEIKSLWIKNEFDISNKKQ---------------KVATLDEMI------NLSKGK- 465
Cdd:PRK11143   82 TDVAeRFPDrarkdgryyaiDFTLDEIKSLKFTEGFDIENGKKvqvypgrfpmgksdfRVHTFEEEIefiqglNHSTGKn 161

                         170       180
                  ....*....|....*....|....
gi 1324321274 466 IGLFIELKGASADKKMADDVVKKV 489
Cdd:PRK11143  162 IGIYPEIKAPWFHHQEGKDIAAKV 185
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 368-574 1.34e-13

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: 70.81  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 368 IAHRG--GGNLGA-ENTLEGVEKAIkEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWIKnefd 444
Cdd:cd08585     7 IAHRGlhDRDAGIpENSLSAFRAAA-EAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLL---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 445 isNKKQKVATLDEMINLSKGKIGLFIELKGasaDKKMADDVVKKVKENKIEK--EAVILSLDYSLIQYIEKKYPNIETGY 522
Cdd:cd08585    82 --GTDEHIPTLDEVLELVAGRVPLLIELKS---CGGGDGGLERRVLAALKDYkgPAAIMSFDPRVVRWFRKLAPGIPRGQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1324321274 523 LyffSVGERDKMVGDYLIMEEREATLDNI--------YKIHQAKKKAV------------VWTVNTKQSMEK 574
Cdd:cd08585   157 L---SEGSNDEADPAFWNEALLSALFSNLltrpdfiaYHLDDLPNPFVtlarallgmpviVWTVRTEEDIAR 225
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 367-587 2.38e-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: 71.27  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEA-RSPK-----------DMTLKEI 434
Cdd:cd08600     3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAeKFPDrkrkdgryyviDFTLDEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 435 KSLWIKNEFDISNKKQ---------------KVATLDEMINLSKG-------KIGLFIELKGASADKKMADDVVKKV--- 489
Cdd:cd08600    83 KSLSVTERFDIENGKKvqvypnrfplwksdfKIHTLEEEIELIQGlnkstgkNVGIYPEIKAPWFHHQEGKDIAAATlev 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 490 --------KENKI--------EKEAV------ILSLDYSLIQYIEK----KYPNIETG------YLYFFSVGERDKM--- 534
Cdd:cd08600   163 lkkygytsKNDKVylqtfdpnELKRIknellpKMGMDLKLVQLIAYtdwgETQEKDPGgwvnydYDWMFTKGGLKEIaky 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1324321274 535 ---VGD--YLIMEEREA----TLDNIYK-IHQAKKKAVVWTVNTKQ---------SMEK--FINMPVDGIITDY 587
Cdd:cd08600   243 adgVGPwySMIIEEKSSkgniVLTDLVKdAHEAGLEVHPYTVRKDAlpeyakdadQLLDalLNKAGVDGVFTDF 316
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 367-587 3.85e-13

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: 67.85  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPkdmTLKEIkslwiknefdis 446
Cdd:cd08555     1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILPP---TLEEV------------ 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 447 nkkqkVATLDEMINLSKGKIGLFIELK-GASADKKMADDVVKKVKENKIE--KEAVILSLDYSLIQyiekkypnietGYL 523
Cdd:cd08555    66 -----LELIADYLKNPDYTIILSLEIKqDSPEYDEFLAKVLKELRVYFDYdlRGKVVLSSFNALGV-----------DYY 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1324321274 524 YFFSVGERDKMVgdylimeereatldnIYKIHQAKKKAVVWTVNT-KQSMEKFINMPVDGIITDY 587
Cdd:cd08555   130 NFSSKLIKDTEL---------------IASANKLGLLSRIWTVNDnNEIINKFLNLGVDGLITDF 179
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 364-592 4.69e-12

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: 66.73  E-value: 4.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 364 KIDIIAHRGGG--NLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT--------GEARSPKDMTLKE 433
Cdd:cd08564     3 RPIIVGHRGAGcsTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEDDTNPdtsiqlddSGFKNINDLSLDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 434 IKSLWIKNEFDI------SNKKQKVATLDEMINLSKGKIGLFIELKGASADkkMADDVVKKVKENKIEKEAVILSLDYS- 506
Cdd:cd08564    83 ITRLHFKQLFDEkpcgadEIKGEKIPTLEDVLVTFKDKLKYNIELKGREVG--LGERVLNLVEKYGMILQVHFSSFLHYd 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 507 ---LIQYIEKKYPNIETGYLyFFSVGERDkmVGDYL-----------IMEEREATLDNIYKIHQAKKKAVVW----TVNT 568
Cdd:cd08564   161 rldLLKALRPNKLNVPIALL-FNEVKSPS--PLDFLeqakyynatwvNFSYDFWTEEFVKKAHENGLKVMTYfdepVNDN 237

                         250       260
                  ....*....|....*....|....
gi 1324321274 569 KQSMEKFINMPVDGIITDYVKELK 592
Cdd:cd08564   238 EEDYKVYLELGVDCICPNDPVLLV 261
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 367-514 6.78e-11

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: 63.86  E-value: 6.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHD------------------KNFKRLTGEARS--- 425
Cdd:cd08602     3 VIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEpelsgttdvadhpefadrKTTKTVDGVNVTgwf 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 426 PKDMTLKEIKSLWIKNEfdISNKKQK------VATLDEMINLSKGK-------IGLFIELK-----GASADKKMADDVVK 487
Cdd:cd08602    83 TEDFTLAELKTLRARQR--LPYRDQSydgqfpIPTFEEIIALAKAAsaatgrtVGIYPEIKhptyfNAPLGLPMEDKLLE 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1324321274 488 KVKE---NKIEKEAVILSLDYSLIQYIEKK 514
Cdd:cd08602   161 TLKKygyTGKKAPVFIQSFEVTNLKYLRNK 190
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 367-437 2.02e-08

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: 55.79  E-value: 2.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSL 437
Cdd:cd08580     3 IVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATL 73
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-588 1.48e-07

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: 53.44  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGN-----LGA---ENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHD---------KNFKRLTGEARSP-KD 428
Cdd:cd08572     2 VIGHRGLGKnyasgSLAgirENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDftisvseksKTGSDEGELIEVPiHD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 429 MTLKEIKSLWI------------------KNEFDISNKKQKVATLDE-MINLSKgKIGLFIELK------GASADK---- 479
Cdd:cd08572    82 LTLEQLKELGLqhisalkrkaltrkakgpKPNPWGMDEHDPFPTLQEvLEQVPK-DLGFNIEIKypqlleDGEGELtpyf 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 480 ---KMADDVVKKVKENKIEKEAVILSLD---YSLIQYIEKKYPnietgyLYFFSVGERDKMVgdylIMEEREATL----- 548
Cdd:cd08572   161 ernAFVDTILAVVFEHAGGRRIIFSSFDpdiCIMLRLKQNKYP------VLFLTNGGTNEVE----HMDPRRRSLqaavn 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1324321274 549 --------------DNIYKIHQAKKKA-----VVWT----VNTKQSMEKFINMPVDGIITDYV 588
Cdd:cd08572   231 falaegllgvvlhaEDLLKNPSLISLVkalglVLFTygddNNDPENVKKQKELGVDGVIYDRV 293
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 367-437 4.51e-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: 51.64  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRG-GGNLGA----------ENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKN--FKRlTGEARSP--KDMTL 431
Cdd:cd08605     2 VIGHRGlGMNRAShqpsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFivVER-GGEVESSriRDLTL 80


                  ....*.
gi 1324321274 432 KEIKSL 437
Cdd:cd08605    81 AELKAL 86
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 367-457 1.98e-05

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 46.47  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT---GEArspKDMTLKEIKSLWIKNEF 443
Cdd:PRK09454   10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSngwGVA---GELTWQDLAQLDAGSWF 86

                          90
                  ....*....|....
gi 1324321274 444 DISNKKQKVATLDE 457
Cdd:PRK09454   87 SAAFAGEPLPTLSQ 100
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 368-437 1.14e-04

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: 44.59  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 368 IAHRGGGN---LGA----ENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNF----KRLTGEARSP------KDMT 430
Cdd:cd08607     3 VGHRGAGNsytAASavvrENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvslKSKGDSDRDDllevpvKDLT 82


                  ....*..
gi 1324321274 431 LKEIKSL 437
Cdd:cd08607    83 YEQLKLL 89
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 379-439 2.15e-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: 43.50  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1324321274 379 ENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTGEARSPKDMTLKEIKSLWI 439
Cdd:cd08613    60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDI 120
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 363-420 5.51e-04

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: 42.55  E-value: 5.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1324321274 363 RKIDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT 420
Cdd:cd08610    21 PKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTT 78
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-463 6.31e-04

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2, GDE3, GDE6-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase domain-containing protein subtype 5 (GDE2), subtype 2 (GDE3), subtype 1 (GDE6), and their eukaryotic homologs. Mammalian GDE2, GDE3, and GDE6 show very high sequence similarity to each other and have been classified into the same family. Although they are all transmembrane proteins, based on different pattern of tissue distribution, these enzymes might display diverse cellular functions. Mammalian GDE2 is primarily expressed in mature neurons. It selectively hydrolyzes glycerophosphocholine (GPC) and mainly functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE3 is specifically expressed in bone tissues and spleen. It selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol and functions as an inducer of osteoblast differentiation. Mammalian GDE6 is predominantly expressed in the spermatocytes of testis, and its specific physiological function has not been elucidated yet.


Pssm-ID: 176516 [Multi-domain]  Cd Length: 252  Bit Score: 41.91  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT-------GEARSPKDM-TLKEIKSL- 437
Cdd:cd08574     4 LIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTnvadvfpERAHERASMfTWTDLQQLn 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1324321274 438 ----WIK----------NEFD---ISNkkQKVATLDEMINLSK 463
Cdd:cd08574    84 agqwFLKddpfwtasslSESDreeAGN--QSIPSLAELLRLAK 124
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 367-413 1.09e-03

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


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 41.28  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1324321274 367 IIAHRGGG---------NLGaENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHD 413
Cdd:cd08606     4 VIGHRGLGkntaerkslQLG-ENTVESFILAASLGASYVEVDVQLTKDLVPVIYHD 58
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 560-588 1.73e-03

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as 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: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 35.94  E-value: 1.73e-03
                          10        20
                  ....*....|....*....|....*....
gi 1324321274 560 KAVVWTVNTKQSMEKFINMPVDGIITDYV 588
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDP 29
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-420 5.12e-03

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: 39.44  E-value: 5.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1324321274 367 IIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLT 420
Cdd:cd08608     4 IIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTT 57
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 364-473 5.19e-03

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: 39.52  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1324321274 364 KIDIIAHRGGGNLGAENTLEGVEKAIKEKANWTEIDVQRTKDNHYIINHDKNFKRLTG--------EARSPKDMTLKEIK 435
Cdd:cd08609    26 KPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNvkdvfpgrDAAGSNNFTWTELK 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1324321274 436 SL----W------------IKNEFDISNKKQKVATLDEMINLSKG-KIGLFIELK 473
Cdd:cd08609   106 TLnagsWflerrpfwtlssLSEEDRREADNQTVPSLSELLDLAKKhNVSIMFDLR 160
 
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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