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Conserved domains on  [gi|24646223|ref|NP_650171|]
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uncharacterized protein Dmel_CG3942 [Drosophila melanogaster]

Protein Classification

glycerophosphodiester phosphodiesterase family protein; PI-PLC domain-containing protein( domain architecture ID 10146619)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to GDPD domain region of GPCPD1/GDE5 that may be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity| PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol; similar to Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 368-684 8.35e-140

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: 412.46  E-value: 8.35e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 368 MNIGHKGSGNTYRLGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFMLQRmpsfedllenqdllif 447
Cdd:cd08607   1 LDVGHRGAGNSYTAASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKS---------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 448 ayenlnklmllaMGGSKRKDLIAVPLEAFSYDQLKEVKVLRFAGSKGCDK---SCDRMLLEQRPFPllLDLLDEENLPVD 524
Cdd:cd08607  65 ------------KGDSDRDDLLEVPVKDLTYEQLKLLKLFHISALKVKEYksvEEDEDPPEHQPFP--TLSDVLESVPED 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 525 MGFLIEIKWPQMTNMRRWESGSFkPTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPHS 604
Cdd:cd08607 131 VGFNIEIKWPQQQKDGSWESELF-TYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQ 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 605 -PVQYADQRVSVQDVAVRFCNSLEFLGLTLHANSLLNKPSTMAYLHQINLDAFVYGSSTIDLEIRNKLKKHGVLGIIYDR 683
Cdd:cd08607 210 rYPEFMDLRTRTFEIAVNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDR 289


                .
gi 24646223 684 L 684
Cdd:cd08607 290 I 290
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 44-164 4.60e-42

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


:

Pssm-ID: 99888  Cd Length: 120  Bit Score: 148.63  E-value: 4.60e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223  44 FCVVFHSsLNGNEYVAISGNCPSLGNWDPKEVYILAKNDcisclCNCRQFEASLEIPRNIDIHYRYCVVIH--DPETDEV 121
Cdd:cd05814   5 FRVFASE-LAPGEVVAVVGSLPVLGNWQPEKAVPLEKED-----DDCNLWKASIELPRGVDFQYRYFVAVVlnDSGPCQV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24646223 122 YIRFWESQLYPRVIRTC-QNMLKNCDVFGKphdDDEANQVDRGW 164
Cdd:cd05814  79 IVRKWETHLQPRSIKPLeEERLNDDDKFGI---YDGVEQVDRGW 119
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 368-684 8.35e-140

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: 412.46  E-value: 8.35e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 368 MNIGHKGSGNTYRLGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFMLQRmpsfedllenqdllif 447
Cdd:cd08607   1 LDVGHRGAGNSYTAASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKS---------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 448 ayenlnklmllaMGGSKRKDLIAVPLEAFSYDQLKEVKVLRFAGSKGCDK---SCDRMLLEQRPFPllLDLLDEENLPVD 524
Cdd:cd08607  65 ------------KGDSDRDDLLEVPVKDLTYEQLKLLKLFHISALKVKEYksvEEDEDPPEHQPFP--TLSDVLESVPED 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 525 MGFLIEIKWPQMTNMRRWESGSFkPTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPHS 604
Cdd:cd08607 131 VGFNIEIKWPQQQKDGSWESELF-TYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQ 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 605 -PVQYADQRVSVQDVAVRFCNSLEFLGLTLHANSLLNKPSTMAYLHQINLDAFVYGSSTIDLEIRNKLKKHGVLGIIYDR 683
Cdd:cd08607 210 rYPEFMDLRTRTFEIAVNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDR 289


                .
gi 24646223 684 L 684
Cdd:cd08607 290 I 290
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 44-164 4.60e-42

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 148.63  E-value: 4.60e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223  44 FCVVFHSsLNGNEYVAISGNCPSLGNWDPKEVYILAKNDcisclCNCRQFEASLEIPRNIDIHYRYCVVIH--DPETDEV 121
Cdd:cd05814   5 FRVFASE-LAPGEVVAVVGSLPVLGNWQPEKAVPLEKED-----DDCNLWKASIELPRGVDFQYRYFVAVVlnDSGPCQV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24646223 122 YIRFWESQLYPRVIRTC-QNMLKNCDVFGKphdDDEANQVDRGW 164
Cdd:cd05814  79 IVRKWETHLQPRSIKPLeEERLNDDDKFGI---YDGVEQVDRGW 119
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 372-685 2.98e-31

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: 122.51  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223   372 HKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRfmlqRMPSfedllenqdllifayen 451
Cdd:pfam03009   1 HRGASGSYP-------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLD----RTTD----------------- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223   452 lnklmllamggskrkdlIAVPLEAFSYDQLKEVKVLRFAGSKGCDKSCDRMLLEQrpfpllldlldEENLPVDMGFLIEI 531
Cdd:pfam03009  53 -----------------GAGYVRDLTLEELKRLDIGAGNSGPLSGERVPFPTLEE-----------VLEFDWDVGFNIEI 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223   532 KWPQMTN-MRRWESGSfkpTFDRNFYVDTILEivlNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPhspvqyAD 610
Cdd:pfam03009 105 KIKPYVEaIAPEEGLI---VKDLLLSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGR------AY 172

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24646223   611 QRVSVQDVAVRFCNSLEFLGltLHANSLLNKPSTMAYLHQINLDAFVYgssTIDLEIRNK-LKKHGVLGIIYDRLD 685
Cdd:pfam03009 173 AEADLLERAAAFAGAPALLG--EVALVDEALPDLVKRAHARGLVVHVW---TVNNEDEMKrLLELGVDGVITDRPD 243
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
370-690 2.04e-19

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 88.00  E-value: 2.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDfvlrfmlqrmpsfedllenqdllifay 449
Cdd:COG0584   6 IAHRG-------ASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHD--------------------------- 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 450 ENLNKLmllaMGGSKRkdliavpLEAFSYDQLKEVKVLRFAGSKGcdkscDRM-----LLEQrpfpllldlldeenLPVD 524
Cdd:COG0584  52 PTLDRT----TNGTGR-------VADLTLAELRQLDAGSGPDFAG-----ERIptleeVLEL--------------VPGD 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 525 MGFLIEIKwpqmtnmrrwesgsfKPTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADicAMVRFKQNV--YPVTLLLEDp 602
Cdd:COG0584 102 VGLNIEIK---------------SPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPE--ALRRLRELApdVPLGLLVEE- 163

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 603 hspvqyadqrvsVQDVAVRFCNSLEFLGLTLHANSLlnKPSTMAYLHQINLDAFVYgssTI-DLEIRNKLKKHGVLGIIY 681
Cdd:COG0584 164 ------------LPADPLELARALGADGVGPDYDLL--TPELVAAAHAAGLKVHVW---TVnDPEEMRRLLDLGVDGIIT 226


                ....*....
gi 24646223 682 DRLDQLDQV 690
Cdd:COG0584 227 DRPDLLRAV 235
CBM_2 smart01065
Starch binding domain;
47-135 5.55e-13

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 65.06  E-value: 5.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223     47 VFHSSLNGNEYVAISGNCPSLGNWDPKEVYILAKNDCISCLcncrqFEASLEIP-RNIDIHYRYCVVihdpetDEVYIRF 125
Cdd:smart01065   7 VRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPL-----WKGTVSLPpAGTTIEYKYVKV------DEDGSVT 75

                           90
                   ....*....|
gi 24646223    126 WESQLYPRVI 135
Cdd:smart01065  76 WESGPNRRLT 85
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 368-684 8.35e-140

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: 412.46  E-value: 8.35e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 368 MNIGHKGSGNTYRLGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFMLQRmpsfedllenqdllif 447
Cdd:cd08607   1 LDVGHRGAGNSYTAASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKS---------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 448 ayenlnklmllaMGGSKRKDLIAVPLEAFSYDQLKEVKVLRFAGSKGCDK---SCDRMLLEQRPFPllLDLLDEENLPVD 524
Cdd:cd08607  65 ------------KGDSDRDDLLEVPVKDLTYEQLKLLKLFHISALKVKEYksvEEDEDPPEHQPFP--TLSDVLESVPED 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 525 MGFLIEIKWPQMTNMRRWESGSFkPTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPHS 604
Cdd:cd08607 131 VGFNIEIKWPQQQKDGSWESELF-TYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQ 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 605 -PVQYADQRVSVQDVAVRFCNSLEFLGLTLHANSLLNKPSTMAYLHQINLDAFVYGSSTIDLEIRNKLKKHGVLGIIYDR 683
Cdd:cd08607 210 rYPEFMDLRTRTFEIAVNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDR 289


                .
gi 24646223 684 L 684
Cdd:cd08607 290 I 290
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 368-684 4.98e-106

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: 325.39  E-value: 4.98e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 368 MNIGHKGSGNTYRLGS-DVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFMLQRMpsfedllenqdlli 446
Cdd:cd08572   1 LVIGHRGLGKNYASGSlAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSK-------------- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 447 fayenlnklmllamGGSKRKDLIAVPLEAFSYDQLKEVKVLRFAGSKGC--------DKSCDRMLLEQRPFPLLLDLLDE 518
Cdd:cd08572  67 --------------TGSDEGELIEVPIHDLTLEQLKELGLQHISALKRKaltrkakgPKPNPWGMDEHDPFPTLQEVLEQ 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 519 EnlPVDMGFLIEIKWPQMTNMRrweSGSFKPTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLL 598
Cdd:cd08572 133 V--PKDLGFNIEIKYPQLLEDG---EGELTPYFERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFL 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 599 LEDPHSPVQYADQRVSVQDVAVRFCNSLEFLGLTLHANSLLNKPSTMAYLHQINLDAFVYGSSTIDLEIRNKLKKHGVLG 678
Cdd:cd08572 208 TNGGTNEVEHMDPRRRSLQAAVNFALAEGLLGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQKELGVDG 287


                ....*.
gi 24646223 679 IIYDRL 684
Cdd:cd08572 288 VIYDRV 293
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 44-164 4.60e-42

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 148.63  E-value: 4.60e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223  44 FCVVFHSsLNGNEYVAISGNCPSLGNWDPKEVYILAKNDcisclCNCRQFEASLEIPRNIDIHYRYCVVIH--DPETDEV 121
Cdd:cd05814   5 FRVFASE-LAPGEVVAVVGSLPVLGNWQPEKAVPLEKED-----DDCNLWKASIELPRGVDFQYRYFVAVVlnDSGPCQV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24646223 122 YIRFWESQLYPRVIRTC-QNMLKNCDVFGKphdDDEANQVDRGW 164
Cdd:cd05814  79 IVRKWETHLQPRSIKPLeEERLNDDDKFGI---YDGVEQVDRGW 119
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 370-684 4.03e-34

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: 132.18  E-value: 4.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGSG-NTYRLGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFMLQRMPsFEDLLENQDLLIFA 448
Cdd:cd08606   5 IGHRGLGkNTAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETGTDVP-IHDLTLEQFLHLSR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 449 YENLNKLMLLAMGGSKRKDLIAVPleafsYDQLKEvkvlrfagskgcdkscdrmLLEQrpfpllldlldeenLPVDMGFL 528
Cdd:cd08606  84 MKYTVDFKKKGFKGNSRGHSIQAP-----FTTLEE-------------------LLKK--------------LPKSVGFN 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 529 IEIKWPQMTNMRRWESGSFkpTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPHSPVqy 608
Cdd:cd08606 126 IELKYPMLHEAEEEEVAPV--AIELNAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGKAPD-- 201

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24646223 609 ADQRVSVQDVAVRFCNSLEFLGLTLHANSLLNKPSTMAYLHQINLDAFVYGSSTIDLEIRNKLKKHGVLGIIYDRL 684
Cdd:cd08606 202 MDVRAASLQEAIRFAKQWNLLGLVSAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSV 277
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 372-685 2.98e-31

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: 122.51  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223   372 HKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRfmlqRMPSfedllenqdllifayen 451
Cdd:pfam03009   1 HRGASGSYP-------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLD----RTTD----------------- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223   452 lnklmllamggskrkdlIAVPLEAFSYDQLKEVKVLRFAGSKGCDKSCDRMLLEQrpfpllldlldEENLPVDMGFLIEI 531
Cdd:pfam03009  53 -----------------GAGYVRDLTLEELKRLDIGAGNSGPLSGERVPFPTLEE-----------VLEFDWDVGFNIEI 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223   532 KWPQMTN-MRRWESGSfkpTFDRNFYVDTILEivlNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPhspvqyAD 610
Cdd:pfam03009 105 KIKPYVEaIAPEEGLI---VKDLLLSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGR------AY 172

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24646223   611 QRVSVQDVAVRFCNSLEFLGltLHANSLLNKPSTMAYLHQINLDAFVYgssTIDLEIRNK-LKKHGVLGIIYDRLD 685
Cdd:pfam03009 173 AEADLLERAAAFAGAPALLG--EVALVDEALPDLVKRAHARGLVVHVW---TVNNEDEMKrLLELGVDGVITDRPD 243
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 370-683 2.07e-22

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: 97.87  E-value: 2.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGSGNTYRLGSDV----VRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLrfmlqrmpSFEDLLENQDll 445
Cdd:cd08605   3 IGHRGLGMNRASHQPSvgpgIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFI--------VVERGGEVES-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 446 iFAYENLNKLMLLAMGGSKRKDLIAVpleAFSYDQLKEVKVLRFAgskgCDKSCDRMLLEQrpfpllldllDEENLPVDM 525
Cdd:cd08605  73 -SRIRDLTLAELKALGPQAESTKTST---VALYRKAKDPEPEPWI----MDVEDSIPTLEE----------VFSEVPPSL 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 526 GFLIEIKWPqmtnmrrwESGSFKPTFDRNFyVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVtLLLEDPHSP 605
Cdd:cd08605 135 GFNIELKFG--------DDNKTEAEELVRE-LRAILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPV-MFLTDCGPY 204

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24646223 606 VQYADQRVSVQdVAVRFCNSLEFLGLTLHANSLLNKPSTMAYLHQINLDAFVYGSSTIDLEIRNKLKKHGVLGIIYDR 683
Cdd:cd08605 205 THNDPRRNSIE-AAIQVALEGGLQGIVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDH 281
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
370-690 2.04e-19

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 88.00  E-value: 2.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDfvlrfmlqrmpsfedllenqdllifay 449
Cdd:COG0584   6 IAHRG-------ASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHD--------------------------- 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 450 ENLNKLmllaMGGSKRkdliavpLEAFSYDQLKEVKVLRFAGSKGcdkscDRM-----LLEQrpfpllldlldeenLPVD 524
Cdd:COG0584  52 PTLDRT----TNGTGR-------VADLTLAELRQLDAGSGPDFAG-----ERIptleeVLEL--------------VPGD 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 525 MGFLIEIKwpqmtnmrrwesgsfKPTFDRNFYVDTILEIVLNKAGKRRIVFCSFDADicAMVRFKQNV--YPVTLLLEDp 602
Cdd:COG0584 102 VGLNIEIK---------------SPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPE--ALRRLRELApdVPLGLLVEE- 163

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 603 hspvqyadqrvsVQDVAVRFCNSLEFLGLTLHANSLlnKPSTMAYLHQINLDAFVYgssTI-DLEIRNKLKKHGVLGIIY 681
Cdd:COG0584 164 ------------LPADPLELARALGADGVGPDYDLL--TPELVAAAHAAGLKVHVW---TVnDPEEMRRLLDLGVDGIIT 226


                ....*....
gi 24646223 682 DRLDQLDQV 690
Cdd:COG0584 227 DRPDLLRAV 235
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 370-683 8.36e-18

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: 81.93  E-value: 8.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDfvlrfmlqrMPSFEDLLEnqdllifay 449
Cdd:cd08556   2 IAHRG-------ASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------IPTLEEVLE--------- 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 450 enlnklmllamggskrkdliavpleafsydqlkevkvlRFAGskgcdkscdrmlleqrpfpllldlldeenlpvDMGFLI 529
Cdd:cd08556  57 --------------------------------------LVKG--------------------------------GVGLNI 66

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 530 EIKWPQmtnmrrwesgsfkptfDRNFYVDTILEIVLNKAGKRRIVFCSFDADICAMVRFKQNVYPVTLLLEDPHspvqya 609
Cdd:cd08556  67 ELKEPT----------------RYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVDKPP------ 124

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24646223 610 DQRVSVQDVAVRFCNSleflgltLHANSLLNKPSTMAYLHQINLDAFVYgssTI-DLEIRNKLKKHGVLGIIYDR 683
Cdd:cd08556 125 LDPLLAELARALGADA-------VNPHYKLLTPELVRAAHAAGLKVYVW---TVnDPEDARRLLALGVDGIITDD 189
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-422 1.21e-13

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: 71.48  E-value: 1.21e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24646223 367 CMNIGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08575   1 PLHIAHRG-------GAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHD 49
CBM_2 smart01065
Starch binding domain;
47-135 5.55e-13

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 65.06  E-value: 5.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223     47 VFHSSLNGNEYVAISGNCPSLGNWDPKEVYILAKNDCISCLcncrqFEASLEIP-RNIDIHYRYCVVihdpetDEVYIRF 125
Cdd:smart01065   7 VRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPL-----WKGTVSLPpAGTTIEYKYVKV------DEDGSVT 75

                           90
                   ....*....|
gi 24646223    126 WESQLYPRVI 135
Cdd:smart01065  76 WESGPNRRLT 85
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 370-446 8.08e-12

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: 65.26  E-value: 8.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGSgntyrlgSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLR----------------------- 426
Cdd:cd08579   2 IAHRGV-------SSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKrlagvnkkvwdltleelkkltig 74

                        90       100
                ....*....|....*....|....*..
gi 24646223 427 --FMLQRMPSFEDLLE-----NQDLLI 446
Cdd:cd08579  75 enGHGAKIPSLDEYLAlakglKQKLLI 101
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 369-457 2.08e-11

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: 64.55  E-value: 2.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 369 NIGHKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD------FV----------------LR 426
Cdd:cd08570   1 VIGHRGYKAKYP-------ENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDpnlkrcFGkdgliiddstwdelshLR 73

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 24646223 427 fML----QRMPSFEDLLEnqdlLIFAYENLN-KLML 457
Cdd:cd08570  74 -TIeephQPMPTLKDVLE----WLVEHELPDvKLML 104
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 361-422 2.64e-11

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: 65.31  E-value: 2.64e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24646223 361 WRKNRL---CMNIGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08612  18 HKKKKSpfpCRHISHRG-------GSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHD 75
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 370-422 8.22e-11

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 62.81  E-value: 8.22e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24646223 370 IGHKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08565   2 AGHRGGRNLWP-------ENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHD 47
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 369-422 1.46e-10

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: 62.27  E-value: 1.46e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24646223 369 NIGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08561   1 VIAHRG-------GAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHD 47
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 368-487 1.25e-09

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: 59.11  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 368 MNIGHKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD------------------------- 422
Cdd:cd08563   2 LIFAHRGYSGTAP-------ENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDetvdrttngkgyvkdltleelkkld 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 423 ----FVLRFMLQRMPSFE---DLLENQDLLI--------FAYENLNKLMLLAMggsKRKDLI-AVPLEAFSYDQLKEVKV 486
Cdd:cd08563  75 agswFDEKFTGEKIPTLEevlDLLKDKDLLLnieiktdvIHYPGIEKKVLELV---KEYNLEdRVIFSSFNHESLKRLKK 151


                .
gi 24646223 487 L 487
Cdd:cd08563 152 L 152
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 370-426 1.33e-09

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: 58.85  E-value: 1.33e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24646223 370 IGHKGsgntYRLGSDvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLR 426
Cdd:cd08568   3 LGHRG----YRAKYP---ENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLK 52
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 370-422 2.91e-08

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: 55.03  E-value: 2.91e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24646223 370 IGHKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08581   2 VAHRGYPARYP-------ENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHD 47
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 370-510 3.63e-08

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: 55.40  E-value: 3.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGsgntyrlGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFMLQRMPSFEDLlenqdllifAY 449
Cdd:cd08567   4 QGHRG-------ARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWL---------PY 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24646223 450 ENLnklmllamggskrkdliavPLEAFSYDQLKEVKVlrfaGSKGCDKSCDRMLLEQRPFP 510
Cdd:cd08567  68 EGP-------------------ALYELTLAEIKQLDV----GEKRPGSDYAKLFPEQIPVP 105
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 378-442 3.18e-07

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: 50.90  E-value: 3.18e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24646223 378 TYRLGSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLRFML--QRMPSFEDLLENQ 442
Cdd:cd08555   3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTagILPPTLEEVLELI 69
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 370-440 6.99e-07

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: 51.07  E-value: 6.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 370 IGHKGsgntyrLGSDVVrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD--------------------------- 422
Cdd:cd08562   2 IAHRG------ASSLAP-ENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDdtldrttngsgavteltwaelaqldag 74

                        90       100
                ....*....|....*....|
gi 24646223 423 --FVLRFMLQRMPSFEDLLE 440
Cdd:cd08562  75 swFSPEFAGEPIPTLADVLE 94
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 370-422 1.05e-06

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: 50.39  E-value: 1.05e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24646223 370 IGHKGSGNTYRlgsdvvrENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08582   2 IAHRGASAEAP-------ENTLAAFELAWEQGADGIETDVRLTKDGELVCVHD 47
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 370-422 1.45e-06

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: 50.33  E-value: 1.45e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24646223 370 IGHKGSGntyrlgsDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHD 422
Cdd:cd08573   2 IGHRGAG-------HDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHD 47
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 56-148 1.61e-06

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 46.91  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223  56 EYVAISGNCPSLGNWDPK--------EVYILAKNDCisclcncrqfeaSLEIPRNIDIHYRYCVVihdpETDEVYIrfWE 127
Cdd:cd05467  14 QSVYVVGSHPELGNWDPAkalrlntsNSYPLWTGEI------------PLPAPEGQVIEYKYVIV----DDDGNVQ--WE 75

                        90       100
                ....*....|....*....|..
gi 24646223 128 SqLYPRVIRTC-QNMLKNCDVF 148
Cdd:cd05467  76 S-GSNRVLTVPsTSSLIVVDDW 96
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 388-440 1.89e-06

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: 49.61  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 388 ENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVL----------------------------RFMLQRMPSFEDLL 439
Cdd:cd08566  15 ENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLdrttngkgkvsdltlaeirklrlkdgdgEVTDEKVPTLEEAL 94


                .
gi 24646223 440 E 440
Cdd:cd08566  95 A 95
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 370-421 3.43e-06

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: 49.39  E-value: 3.43e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24646223 370 IGHKGSGNtyrlgSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYH 421
Cdd:cd08564   7 VGHRGAGC-----STLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFH 53
GDPD_NUC-2_fungi cd08578
Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and ...
 549-640 3.59e-06

Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and similar proteins; This subfamily corresponds to a putative glycerophosphodiester phosphodiesterase domain (GDPD) present in Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81. Some uncharacterized NUC-2 sequence homologs are also included in this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in Neurospora crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein PHO81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both NUC-2 and PHO81 have multi-domain architecture, including an SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal GDPD domain with unknown function. Although the putative GDPD domain displays sequence homology to that of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), the residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in members of this family, which suggests the function of putative GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs.


Pssm-ID: 176520  Cd Length: 300  Bit Score: 49.63  E-value: 3.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223 549 PTFDRNFYVDTILEIVLNKAGK--------RRIVFCSFDADICAMVRFKQNVYPV------------TLLLEDPH----- 603
Cdd:cd08578 135 PLVDLNKFIDTVLLVVFDHARYlrhtpgstRSIVFSSCNPEVCTILNWKQPNFPVffamnglvrnndTLSFDTPHhldsl 214

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24646223 604 ----SPVQYADQR-VSVQDvAVRFCNSLEFLGLTLhANSLLN 640
Cdd:cd08578 215 avdpQKLNEADPRsRSIKE-AVRFAKNNNLLGLIL-PYSLLN 254
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 388-425 4.91e-06

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: 49.28  E-value: 4.91e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24646223 388 ENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVL 425
Cdd:cd08613  60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTL 97
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 388-421 6.80e-06

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: 48.48  E-value: 6.80e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 24646223 388 ENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYH 421
Cdd:cd08580  15 ENTLLAISKALANGADAIWLTVQLSKDGVPVLYR 48
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 388-440 6.13e-05

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: 45.01  E-value: 6.13e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24646223 388 ENTLYGFKQAVLANADmVEMDVQLTQDAQVVVYHDFVLRFML-----------------------QRMPSFEDLLE 440
Cdd:cd08585  21 ENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTgvegrveeltaaelralrllgtdEHIPTLDEVLE 95
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 369-426 8.26e-04

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: 41.92  E-value: 8.26e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24646223 369 NIGHKGSgntyrlgSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVLR 426
Cdd:cd08601   3 VIAHRGA-------SGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLD 53
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 58-129 2.10e-03

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 38.08  E-value: 2.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24646223  58 VAISGNCPSLGNWDPKEvYILAKNDCISclcncrQFEASLEIPrNID--IHYRYCvvIHDPETDEVYirfWESQ 129
Cdd:cd05816  17 VYVTGSSPELGNWDPQK-ALKLSDVGFP------IWEADIDIS-KDSfpFEYKYI--IANKDSGVVS---WENG 77
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 370-425 2.93e-03

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: 40.45  E-value: 2.93e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24646223 370 IGHKGSgntyrlgSDVVRENTLYGFKQAVLANADMVEMDVQLTQDAQVVVYHDFVL 425
Cdd:cd08600   4 IAHRGA-------SGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYL 52
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 56-137 5.09e-03

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 37.07  E-value: 5.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646223  56 EYVAISGNCPSLGNWDPKEvyilAK--NDCISCLcncrqFEASLEIPRNIDIHYRYCVVIHDPETDEVyirfWESqLYPR 133
Cdd:cd05817  14 EAVYISGNCNQLGNWNPSK----AKrmQWNEGDL-----WTVDVGIPESVYIEYKYFVSNYDDPNTVL----WES-GPNR 79


                ....
gi 24646223 134 VIRT 137
Cdd:cd05817  80 VLRT 83
 
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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