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Conserved domains on  [gi|1597555912|ref|XP_028380915|]
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glycerophosphocholine phosphodiesterase GPCPD1 isoform X1 [Phyllostomus discolor]

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 ...
 318-610 0e+00

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: 531.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 318 LDVGHRGAGNSTTTAQlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFDADPVELFEIPVK 397
Cdd:cd08607     1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 398 ELTFDQLQLLKLAHVTALKSKDRKEsmVAEENSFSENQPFPSLKMVLESLPEDVGFNIEIKWICQQRDGMWDGNLSAYFD 477
Cdd:cd08607    80 DLTYEQLKLLKLFHISALKVKEYKS--VEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELFTYFD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 478 MNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIYPELMDLRSRTTAIAMSFAQFENLLGI 557
Cdd:cd08607   158 RNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQAEELLGV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912 558 NAHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08607   238 NLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 4-126 1.83e-57

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: 189.84  E-value: 1.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912   4 QVTFEIRG-TLLPGEVFAICGNCDVLGNWNPQNAVALTPENEtgESMLWKATIVLSRGVSVQYRYFKGCFLepkTIGGPC 82
Cdd:cd05814     2 RVTFRVFAsELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDD--DCNLWKASIELPRGVDFQYRYFVAVVL---NDSGPC 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1597555912  83 QVIVHKWETHLQPRSITPLENEIIIDDGQFGIHNGVETLDSGWL 126
Cdd:cd05814    77 QVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVEQVDRGWL 120
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 318-610 0e+00

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: 531.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 318 LDVGHRGAGNSTTTAQlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFDADPVELFEIPVK 397
Cdd:cd08607     1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 398 ELTFDQLQLLKLAHVTALKSKDRKEsmVAEENSFSENQPFPSLKMVLESLPEDVGFNIEIKWICQQRDGMWDGNLSAYFD 477
Cdd:cd08607    80 DLTYEQLKLLKLFHISALKVKEYKS--VEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELFTYFD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 478 MNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIYPELMDLRSRTTAIAMSFAQFENLLGI 557
Cdd:cd08607   158 RNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQAEELLGV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912 558 NAHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08607   238 NLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 4-126 1.83e-57

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: 189.84  E-value: 1.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912   4 QVTFEIRG-TLLPGEVFAICGNCDVLGNWNPQNAVALTPENEtgESMLWKATIVLSRGVSVQYRYFKGCFLepkTIGGPC 82
Cdd:cd05814     2 RVTFRVFAsELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDD--DCNLWKASIELPRGVDFQYRYFVAVVL---NDSGPC 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1597555912  83 QVIVHKWETHLQPRSITPLENEIIIDDGQFGIHNGVETLDSGWL 126
Cdd:cd05814    77 QVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVEQVDRGWL 120
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 322-610 5.80e-49

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: 171.43  E-value: 5.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 322 HRGAGNSTTtaqlakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDADPvelfeiPVKELTF 401
Cdd:pfam03009   1 HRGASGSYP--------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHD----FNLDRTTDGAG------YVRDLTL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 402 DQLQLLKLAHVtalkskdrkesmvaEENSFSENQ-PFPSLKMVLEsLPEDVGFNIEIKW-ICQQRDGMWdgNLSAYFDMN 479
Cdd:pfam03009  63 EELKRLDIGAG--------------NSGPLSGERvPFPTLEEVLE-FDWDVGFNIEIKIkPYVEAIAPE--EGLIVKDLL 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 480 LFLDIILKtvlENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTqgkSDIYPELMDLRSRTTAiamsFAQFENLLGINA 559
Cdd:pfam03009 126 LSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLS---SGRAYAEADLLERAAA----FAGAPALLGEVA 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1597555912 560 HTEDllRNPSYIQEAKAKGLVIFCWGDdtNDPENRRKLKELGVNGLIYDRI 610
Cdd:pfam03009 196 LVDE--ALPDLVKRAHARGLVVHVWTV--NNEDEMKRLLELGVDGVITDRP 242
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
315-610 1.10e-40

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.48  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 315 RTPLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDADpvelfeI 394
Cdd:COG0584     1 PRPLIIAHRGAS--------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHD----PTLDRTTNGT------G 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 395 PVKELTFDQLQLLKLAHVTALKskdrkesmvaeensfseNQPFPSLKMVLESLPEDVGFNIEIKwicqqrdgmwdgnlSA 474
Cdd:COG0584    63 RVADLTLAELRQLDAGSGPDFA-----------------GERIPTLEEVLELVPGDVGLNIEIK--------------SP 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 475 YFDMNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTqgkSDIYPELMDLRSRTTAiamsfaqfenl 554
Cdd:COG0584   112 PAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV---EELPADPLELARALGA----------- 177

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912 555 LGINAHTEDLlrNPSYIQEAKAKGLVIFCWgddT-NDPENRRKLKELGVNGLIYDRI 610
Cdd:COG0584   178 DGVGPDYDLL--TPELVAAAHAAGLKVHVW---TvNDPEEMRRLLDLGVDGIITDRP 229
CBM_2 smart01065
Starch binding domain;
4-100 4.66e-24

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 96.26  E-value: 4.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912    4 QVTFEIRGTLL-PGEVFAICGNCDVLGNWNPQNAVALTPENETgeSMLWKATI-VLSRGVSVQYRYFKGCFLEpktiggp 81
Cdd:smart01065   2 SVTFKVRNGYTqPGESVYVVGSVPELGNWNPKKAVPLSPDTDG--YPLWKGTVsLPPAGTTIEYKYVKVDEDG------- 72

                           90
                   ....*....|....*....
gi 1597555912   82 cqviVHKWETHLQPRSITP 100
Cdd:smart01065  73 ----SVTWESGPNRRLTVP 87
CBM_20 pfam00686
Starch binding domain;
4-69 1.31e-12

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 64.23  E-value: 1.31e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1597555912   4 QVTFEIRGTLLPGEVFAICGNCDVLGNWNPQNAVALTPENETGESmLWKATIVLSRGVSVQYRYFK 69
Cdd:pfam00686   2 SVTFNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSYP-LWSGTVSLPAGTTIEYKYIK 66
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 320-610 1.86e-09

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 58.80  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGnstttaQLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFdadpvelfeiPVKEL 399
Cdd:PRK09454   11 VAHRGGG------KLAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWG----------VAGEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQllklahvtALKSKDRKESMVAEEnsfsenqPFPSLKMVLESLPEDvGF--NIEIKwICQQRDgmWD-GNLSAYF 476
Cdd:PRK09454   73 TWQDLA--------QLDAGSWFSAAFAGE-------PLPTLSQVAARCRAH-GMaaNIEIK-PTTGRE--AEtGRVVALA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 477 DMNLFLDIILKTVLensgkrrivfSSFDADICTMVRHKQNRYPILFLtqgkSDIYPElmDLRSRTTAIAmsfaqfenLLG 556
Cdd:PRK09454  134 ARALWAGAAVPPLL----------SSFSEDALEAARQAAPELPRGLL----LDEWPD--DWLELTRRLG--------CVS 189

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1597555912 557 INAHTEDLlrNPSYIQEAKAKGLVIFCWgdDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:PRK09454  190 LHLNHKLL--DEARVAALKAAGLRILVY--TVNDPARARELLRWGVDCICTDRI 239
PLN02950 PLN02950
4-alpha-glucanotransferase
 16-68 9.43e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 45.87  E-value: 9.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912  16 GEVFAICGNCDVLGNWNPQNAVALTPENEtGESMLWKATIVLSRGVSVQYRYF 68
Cdd:PLN02950   22 GQSLLVCGSEPLLGSWNVKKGLLLSPVHQ-GDELVWEGSVSVPEGFSCEYSYY 73
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 318-610 0e+00

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: 531.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 318 LDVGHRGAGNSTTTAQlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFDADPVELFEIPVK 397
Cdd:cd08607     1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 398 ELTFDQLQLLKLAHVTALKSKDRKEsmVAEENSFSENQPFPSLKMVLESLPEDVGFNIEIKWICQQRDGMWDGNLSAYFD 477
Cdd:cd08607    80 DLTYEQLKLLKLFHISALKVKEYKS--VEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELFTYFD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 478 MNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIYPELMDLRSRTTAIAMSFAQFENLLGI 557
Cdd:cd08607   158 RNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQAEELLGV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912 558 NAHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08607   238 NLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 318-610 1.30e-153

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: 445.57  E-value: 1.30e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 318 LDVGHRGAGNSTTTAQLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFDADPVELFEIPVK 397
Cdd:cd08572     1 LVIGHRGLGKNYASGSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDEGELIEVPIH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 398 ELTFDQLQLLKLAHVTALKSKDRKESMVA---EENSFSENQPFPSLKMVLESLPEDVGFNIEIKWICQQRDGMwdGNLSA 474
Cdd:cd08572    81 DLTLEQLKELGLQHISALKRKALTRKAKGpkpNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYPQLLEDGE--GELTP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 475 YFDMNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIyPELMDLRSRTTAIAMSFAQFENL 554
Cdd:cd08572   159 YFERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNGGTNE-VEHMDPRRRSLQAAVNFALAEGL 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1597555912 555 LGINAHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08572   238 LGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQKELGVDGVIYDRV 293
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 320-610 3.25e-59

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: 200.75  E-value: 3.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGNSTTTAQLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMkkkfdadpvelFEIPVKEL 399
Cdd:cd08606     5 IGHRGLGKNTAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETG-----------TDVPIHDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQ-LQLLKLAHVTALKSKDRKesmvAEENSFSENQPFPSLKMVLESLPEDVGFNIEIKWIcQQRDGMWDGNLSAYFDM 478
Cdd:cd08606    74 TLEQfLHLSRMKYTVDFKKKGFK----GNSRGHSIQAPFTTLEELLKKLPKSVGFNIELKYP-MLHEAEEEEVAPVAIEL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 479 NLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSdiyPELMDLRSRTTAIAMSFAQFENLLGIN 558
Cdd:cd08606   149 NAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGK---APDMDVRAASLQEAIRFAKQWNLLGLV 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1597555912 559 AHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08606   226 SAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSV 277
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 4-126 1.83e-57

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: 189.84  E-value: 1.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912   4 QVTFEIRG-TLLPGEVFAICGNCDVLGNWNPQNAVALTPENEtgESMLWKATIVLSRGVSVQYRYFKGCFLepkTIGGPC 82
Cdd:cd05814     2 RVTFRVFAsELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDD--DCNLWKASIELPRGVDFQYRYFVAVVL---NDSGPC 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1597555912  83 QVIVHKWETHLQPRSITPLENEIIIDDGQFGIHNGVETLDSGWL 126
Cdd:cd05814    77 QVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVEQVDRGWL 120
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 322-610 5.80e-49

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: 171.43  E-value: 5.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 322 HRGAGNSTTtaqlakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDADPvelfeiPVKELTF 401
Cdd:pfam03009   1 HRGASGSYP--------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHD----FNLDRTTDGAG------YVRDLTL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 402 DQLQLLKLAHVtalkskdrkesmvaEENSFSENQ-PFPSLKMVLEsLPEDVGFNIEIKW-ICQQRDGMWdgNLSAYFDMN 479
Cdd:pfam03009  63 EELKRLDIGAG--------------NSGPLSGERvPFPTLEEVLE-FDWDVGFNIEIKIkPYVEAIAPE--EGLIVKDLL 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 480 LFLDIILKtvlENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTqgkSDIYPELMDLRSRTTAiamsFAQFENLLGINA 559
Cdd:pfam03009 126 LSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLS---SGRAYAEADLLERAAA----FAGAPALLGEVA 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1597555912 560 HTEDllRNPSYIQEAKAKGLVIFCWGDdtNDPENRRKLKELGVNGLIYDRI 610
Cdd:pfam03009 196 LVDE--ALPDLVKRAHARGLVVHVWTV--NNEDEMKRLLELGVDGVITDRP 242
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 320-610 8.56e-47

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: 166.82  E-value: 8.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGNSTTTAQL---AKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTmkkkfDADPVELFEIpv 396
Cdd:cd08605     3 IGHRGLGMNRASHQPsvgPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVE-----RGGEVESSRI-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 397 KELTFDQLQLLKlAHVTALKSKDRKESMVAEENSFSE-----NQPFPSLKMVLESLPEDVGFNIEIKWicqqrdgmWDGN 471
Cdd:cd08605    76 RDLTLAELKALG-PQAESTKTSTVALYRKAKDPEPEPwimdvEDSIPTLEEVFSEVPPSLGFNIELKF--------GDDN 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 472 LSAYFDMNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIYpelMDLRSRTTAIAMSFAQF 551
Cdd:cd08605   147 KTEAEELVRELRAILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTH---NDPRRNSIEAAIQVALE 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1597555912 552 ENLLGINAHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08605   224 GGLQGIVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDHV 282
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
315-610 1.10e-40

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.48  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 315 RTPLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDADpvelfeI 394
Cdd:COG0584     1 PRPLIIAHRGAS--------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHD----PTLDRTTNGT------G 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 395 PVKELTFDQLQLLKLAHVTALKskdrkesmvaeensfseNQPFPSLKMVLESLPEDVGFNIEIKwicqqrdgmwdgnlSA 474
Cdd:COG0584    63 RVADLTLAELRQLDAGSGPDFA-----------------GERIPTLEEVLELVPGDVGLNIEIK--------------SP 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 475 YFDMNLFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTqgkSDIYPELMDLRSRTTAiamsfaqfenl 554
Cdd:COG0584   112 PAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV---EELPADPLELARALGA----------- 177

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912 555 LGINAHTEDLlrNPSYIQEAKAKGLVIFCWgddT-NDPENRRKLKELGVNGLIYDRI 610
Cdd:COG0584   178 DGVGPDYDLL--TPELVAAAHAAGLKVHVW---TvNDPEEMRRLLDLGVDGIITDRP 229
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 320-609 6.86e-37

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: 136.24  E-value: 6.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLtccltmkkkfdadpvelfeipvkel 399
Cdd:cd08556     2 IAHRGAS--------GEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDI------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 tfdqlqllklahvtalkskdrkesmvaeensfsenqpfPSLKMVLESLPEDVGFNIEIKWICQQRDgmwdgnlsayfDMN 479
Cdd:cd08556    49 --------------------------------------PTLEEVLELVKGGVGLNIELKEPTRYPG-----------LEA 79

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 480 LFLDIILKTVLENsgkrRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIYPELMDLRS-RTTAIAMSFAqfenllgin 558
Cdd:cd08556    80 KVAELLREYGLEE----RVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAELARAlGADAVNPHYK--------- 146

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1597555912 559 ahtedlLRNPSYIQEAKAKGLVIFCWGDdtNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08556   147 ------LLTPELVRAAHAAGLKVYVWTV--NDPEDARRLLALGVDGIITDD 189
CBM_2 smart01065
Starch binding domain;
4-100 4.66e-24

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 96.26  E-value: 4.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912    4 QVTFEIRGTLL-PGEVFAICGNCDVLGNWNPQNAVALTPENETgeSMLWKATI-VLSRGVSVQYRYFKGCFLEpktiggp 81
Cdd:smart01065   2 SVTFKVRNGYTqPGESVYVVGSVPELGNWNPKKAVPLSPDTDG--YPLWKGTVsLPPAGTTIEYKYVKVDEDG------- 72

                           90
                   ....*....|....*....
gi 1597555912   82 cqviVHKWETHLQPRSITP 100
Cdd:smart01065  73 ----SVTWESGPNRRLTVP 87
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 320-610 4.53e-22

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: 95.37  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTC--CLTMKKkfdadpvelfeiPVK 397
Cdd:cd08562     2 IAHRGAS--------SLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLdrTTNGSG------------AVT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 398 ELTFDQLQLLKLAHvtalkskdrkesmvaeenSFSE---NQPFPSLKMVLESLPE-DVGFNIEIKwICQQRDGMW----D 469
Cdd:cd08562    62 ELTWAELAQLDAGS------------------WFSPefaGEPIPTLADVLELARElGLGLNLEIK-PDPGDEALTarvvA 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 470 GNLSAYFDMNlfldiilktvlensgkRRIVFSSFDADICTMVRHKQNRYPILFLTqgksdiypelmdlrsrTTAIAMSFA 549
Cdd:cd08562   123 AALRELWPHA----------------SKLLLSSFSLEALRAARRAAPELPLGLLF----------------DTLPADWLE 170

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1597555912 550 QFENLLGINAHTEDLLRNPSYIQEAKAKGLVIFCWgddT-NDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08562   171 LLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVY---TvNDPARAAELLEWGVDAIFTDRP 229
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 321-608 6.55e-22

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: 94.67  E-value: 6.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 321 GHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccltmkKKFDADPVELFEipVKELT 400
Cdd:cd08568     4 GHRGYR--------AKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHD--------ENLKRVGGVDLK--VKELT 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 401 FDQLQLLKLahvtalkskdrkesmvaeensfsENQPFPSLKMVLESLPEDVGFNIEIKwicqqrdgmwdgnlsayfDMNL 480
Cdd:cd08568    66 YKELKKLHP-----------------------GGELIPTLEEVFRALPNDAIINVEIK------------------DIDA 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 481 fLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIY-----PELMDLRSRTTAI-AMSFAQFENL 554
Cdd:cd08568   105 -VEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEGFsipelHEKLKLYSLHVPIdAIGYIGFEKF 183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1597555912 555 LginahtedllrnpSYIQEAKAKGLVIFCWgdDTNDPENRRKLKELgVNGLIYD 608
Cdd:cd08568   184 V-------------ELLRLLRKLGLKIVLW--TVNDPELVPKLKGL-VDGVITD 221
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 320-609 2.69e-21

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


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 93.15  E-value: 2.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAgnSTTtaqlakVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTccltmkkkfdADPVELFEIPVKEL 399
Cdd:cd08582     2 IAHRGA--SAE------APENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPT----------LKRTSGGDGAVSDL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQLLKlahVTALKSKDRKESMVaeensfsenqpfPSLKMVLESLPE-DVGFNIEIKwicQQRDGMwdgnlsayfdm 478
Cdd:cd08582    64 TLAELRKLD---IGSWKGESYKGEKV------------PTLEEYLAIVPKyGKKLFIEIK---HPRRGP----------- 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 479 nLFLDIILKTVLENSGKR-RIVFSSFDADICTMVRHKQNRYPILFLTQGKSDIYPELMDLRSRTTAiamsfaqfenllGI 557
Cdd:cd08582   115 -EAEEELLKLLKESGLLPeQIVIISFDAEALKRVRELAPTLETLWLRNYKSPKEDPRPLAKSGGAA------------GL 181

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912 558 NAHTEDLLrNPSYIQEAKAKGLVIFCWgddT-NDPENRRKLKELGVNGLIYDR 609
Cdd:cd08582   182 DLSYEKKL-NPAFIKALRDAGLKLNVW---TvDDAEDAKRLIELGVDSITTNR 230
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 317-610 1.01e-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: 92.28  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 317 PLDVGHRGAgnstttAQLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT-CCLTMKKKfdadpvelfeiP 395
Cdd:cd08575     1 PLHIAHRGG------AAEFP--ENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDlDRLTGGSG-----------L 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 396 VKELTFDQLQLLKLA-HVTALKSKDRkesmvaeenSFS--ENQPFPSLKMVLESLPeDVGFNIEIKwicqqrdgmwdgnl 472
Cdd:cd08575    62 VSDLTYAELPPLDAGyGYTFDGGKTG---------YPRggGDGRIPTLEEVFKAFP-DTPINIDIK-------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 473 saYFDMNLFLDIILKTVLENSGKRRIVFSSFDADICTMvRHKQNRY-PILFLTQGKSDIY---------------PELMD 536
Cdd:cd08575   118 --SPDAEELIAAVLDLLEKYKREDRTVWGSTNPEYLRA-LHPENPNlFESFSMTRCLLLYlalgytgllpfvpikESFFE 194

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1597555912 537 LRsRTTAIAMSFAQFENLLGINAhtedLLRNPSYIQEAKAKGLVIFCWGddTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08575   195 IP-RPVIVLETFTLGEGASIVAA----LLWWPNLFDHLRKRGIQVYLWV--LNDEEDFEEAFDLGADGVMTDSP 261
GDPD_NUC-2_fungi cd08578
Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and ...
 311-607 2.95e-20

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: 91.61  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 311 YWKPRTPLDVGHRGAGNSTTTAqlakvqentiaslrnaASHGAAFVEFDVHLSKDFVPVVYHDLTCcltmkkkfdadPVE 390
Cdd:cd08578     3 YWKSTSGSDTQANKDGNSFVTA----------------SSLSGEYLRVKVCVLKDGTPVVAPEWFV-----------PVG 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 391 LFEIPVKELTFDQLQLLklahvtALKSKDRKESMVAEENSFSE--NQPFPSLKMVLESLPEDVGFNIEIKWICQQRDGMW 468
Cdd:cd08578    56 GIKLLVSDLTAEQLESI------LDYSLDDLNSEISDMVDLKRllSSRVVSLETLLELLPPSIQLDIQVLFPTAAEIASI 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 469 DGNLSAYFDMNLFLDIILKTVLENSGK--------RRIVFSSFDADICTMVRHKQNRYPILF-----------------L 523
Cdd:cd08578   130 PVKGSPLVDLNKFIDTVLLVVFDHARYlrhtpgstRSIVFSSCNPEVCTILNWKQPNFPVFFamnglvrnndtlsfdtpH 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 524 TQGKSDIYPELM---DLRSRTTAIAMSFAQFENLLGINAHTEDLLRNPSYIQEAKAKGLVIFCWGDDTNDPENrrKLKEL 600
Cdd:cd08578   210 HLDSLAVDPQKLneaDPRSRSIKEAVRFAKNNNLLGLILPYSLLNIVPQLVESIKSRGLLLIASGEPESLIEV--AEAGD 287


                  ....*..
gi 1597555912 601 GVNGLIY 607
Cdd:cd08578   288 GINGVVT 294
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 321-609 2.99e-20

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: 90.83  E-value: 2.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 321 GHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTccLTMKKKFDADPVELFEIP--VKE 398
Cdd:cd08567     5 GHRGAR--------GLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPK--LNPDITRDPDGAWLPYEGpaLYE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 399 LTFDQLQLLKlahVTALKSKDRKESMVAEENSFsENQPFPSLKMVLESLPEDVG----FNIEIKWICQQRDGMWDGnlsa 474
Cdd:cd08567    75 LTLAEIKQLD---VGEKRPGSDYAKLFPEQIPV-PGTRIPTLEEVFALVEKYGNqkvrFNIETKSDPDRDILHPPP---- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 475 yfdmNLFLDIILKtVLENSGK-RRIVFSSFD-----------ADICTM--VRHKQNRYPILFLTQGKSDIY-PELMDLrs 539
Cdd:cd08567   147 ----EEFVDAVLA-VIRKAGLeDRVVLQSFDwrtlqevrrlaPDIPTValTEETTLGNLPRAAKKLGADIWsPYFTLV-- 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 540 rttaiamsfaqfenllginahtedllrNPSYIQEAKAKGLVIFCWGddTNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08567   220 ---------------------------TKELVDEAHALGLKVVPWT--VNDPEDMARLIDLGVDGIITDY 260
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 321-609 3.15e-19

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: 87.70  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 321 GHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTccltmkkkfdADPVELFEIPVKELT 400
Cdd:cd08561     3 AHRGGA--------GLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDET----------LDRTTDGTGPVADLT 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 401 FDQLQLLKLAHvtalKSKDRKESMVAEENsfsENQPFPSLKMVLESLPeDVGFNIEIKwicQQRDGMWDgnlsayfdmnL 480
Cdd:cd08561    65 LAELRRLDAGY----HFTDDGGRTYPYRG---QGIRIPTLEELFEAFP-DVRLNIEIK---DDGPAAAA----------A 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 481 FLDIILKTVLENsgkrRIVFSSFDADIctmVRHKQNRYPILFLTQGKSDIYP-----ELMD---LRSRTTAIAMSFAQFe 552
Cdd:cd08561   124 LADLIERYGAQD----RVLVASFSDRV---LRRFRRLCPRVATSAGEGEVAAfvlasRLGLgslYSPPYDALQIPVRYG- 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912 553 nllGINahtedlLRNPSYIQEAKAKGLVIFCWGDdtNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08561   196 ---GVP------LVTPRFVRAAHAAGLEVHVWTV--NDPAEMRRLLDLGVDGIITDR 241
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 321-608 5.92e-19

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 86.46  E-value: 5.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 321 GHRGAgnstttaqLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMK-KKFdadpvelfeipVKEL 399
Cdd:cd08563     5 AHRGY--------SGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNgKGY-----------VKDL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQLLKLAhvtalkSKDrkesmvaeENSFSEnQPFPSLKMVLESLPE-DVGFNIEIKwicqqrdgmwdGNLSAYFDM 478
Cdd:cd08563    66 TLEELKKLDAG------SWF--------DEKFTG-EKIPTLEEVLDLLKDkDLLLNIEIK-----------TDVIHYPGI 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 479 -NLFLDIILKTVLENsgkrRIVFSSFDADicTMVRHKQ--NRYPILFLTQGKSDIYPElmdlrsrttaiamsFAQFENLL 555
Cdd:cd08563   120 eKKVLELVKEYNLED----RVIFSSFNHE--SLKRLKKldPKIKLALLYETGLQDPKD--------------YAKKIGAD 179

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1597555912 556 GINAHTEDLlrNPSYIQEAKAKGLVIFCWgddT-NDPENRRKLKELGVNGLIYD 608
Cdd:cd08563   180 SLHPDFKLL--TEEVVEELKKRGIPVRLW---TvNEEEDMKRLKDLGVDGIITN 228
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 4-110 2.76e-18

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: 80.42  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912   4 QVTFEIRGTLLPGEVFAICGNCDVLGNWNPQNAVALTPENetgESMLWKATIVL--SRGVSVQYRYFKgcfLEpktiggp 81
Cdd:cd05467     1 QVRFQVRCTTQFGQSVYVVGSHPELGNWDPAKALRLNTSN---SYPLWTGEIPLpaPEGQVIEYKYVI---VD------- 67

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1597555912  82 cQVIVHKWETHlQPRSI-TP-LENEIIIDDG 110
Cdd:cd05467    68 -DDGNVQWESG-SNRVLtVPsTSSLIVVDDW 96
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 320-520 3.05e-16

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


Pssm-ID: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 78.53  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDAdpvelfEIPVKEL 399
Cdd:cd08581     2 VAHRGYP--------ARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHD----DTLLRLTGV------EGLLHEL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQLLKLAHVTALKSKdrkesmvaeensfSENQPFPSLKMV---LESLPEdVGFNIEIKWICQQRdgmwdgnlsayF 476
Cdd:cd08581    64 EDAELDSLRVAEPARFGSR-------------FAGEPLPSLAAVvqwLAQHPQ-VTLFVEIKTESLDR-----------F 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1597555912 477 DMNLFLDIILKtVLENSGKRRiVFSSFDADICTMVRHkQNRYPI 520
Cdd:cd08581   119 GLERVVDKVLR-ALPAVAAQR-VLISFDYDLLALAKQ-QGGPRT 159
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 320-609 1.07e-15

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: 76.96  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGNstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDADpvelfeIPVKEL 399
Cdd:cd08566     3 VAHRGGWG-------AGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHD----DTLDRTTNGK------GKVSDL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQLLKlahvtaLKSKDRKESmvaeensfseNQPFPSLKMVLESLPEDVGFNIEIKWicqqrdgmwdgnlsayFDMN 479
Cdd:cd08566    66 TLAEIRKLR------LKDGDGEVT----------DEKVPTLEEALAWAKGKILLNLDLKD----------------ADLD 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 480 LFLDIILKTVLENsgkrRIVFSSFDADICTMVRHKQNRYPIlfltqgkSDIYPELMDLRSRTTAIAMsfaqFENLLGINA 559
Cdd:cd08566   114 EVIALVKKHGALD----QVIFKSYSEEQAKELRALAPEVML-------MPIVRDAEDLDEEEARAID----ALNLLAFEI 178

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1597555912 560 HTEDLLRNPSYIQEAKAKGLVIFC---WGDD--------TNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08566   179 TFDDLDLPPLFDELLRALGIRVWVntlGDDDtagldralSDPREVWGELVDAGVDVIQTDR 239
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 320-609 3.32e-15

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


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 75.27  E-value: 3.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRG-AGNSTttaqlakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCC-LTMKKKfdadpvelfeiPVK 397
Cdd:cd08579     2 IAHRGvSSNGV---------ENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKrLAGVNK-----------KVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 398 ELTFDQLQllklahvtalkskdrkeSMVAEENSFSEnqPFPSLKMVLE-SLPEDVGFNIEIKwicqqRDGMWDGNLsayf 476
Cdd:cd08579    62 DLTLEELK-----------------KLTIGENGHGA--KIPSLDEYLAlAKGLKQKLLIELK-----PHGHDSPDL---- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 477 dMNLFLDIILKTVLENSgkrrIVFSSFDADICTMVRHkqnrypilfltqgksdIYPELmdlrsrTTAIAMSFaQFENL-- 554
Cdd:cd08579   114 -VEKFVKLYKQNLIENQ----HQVHSLDYRVIEKVKK----------------LDPKI------KTGYILPF-NIGNLpk 165

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1597555912 555 LGINAHT-EDLLRNPSYIQEAKAKGLVIFCWgdDTNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08579   166 TNVDFYSiEYSTLNKEFIRQAHQNGKKVYVW--TVNDPDDMQRYLAMGVDGIITDY 219
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 5-69 1.69e-13

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. 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: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 66.91  E-value: 1.69e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1597555912   5 VTFEIRGTLLPGEVFAICGNCDVLGNWNPQNAVALTPENETGESMLWKATIVLSRGVSVQYRYFK 69
Cdd:cd05811     9 VTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIR 73
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 4-78 1.69e-13

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: 66.73  E-value: 1.69e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1597555912   4 QVTFEIRGTLLPGEVFAICGNCDVLGNWNPQNAVALTpeneTGESMLWKATIVLSRGVSVQYRYFKGCFLEPKTI 78
Cdd:cd05817     1 MVTFKIHYPTQFGEAVYISGNCNQLGNWNPSKAKRMQ----WNEGDLWTVDVGIPESVYIEYKYFVSNYDDPNTV 71
CBM_20 pfam00686
Starch binding domain;
4-69 1.31e-12

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 64.23  E-value: 1.31e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1597555912   4 QVTFEIRGTLLPGEVFAICGNCDVLGNWNPQNAVALTPENETGESmLWKATIVLSRGVSVQYRYFK 69
Cdd:pfam00686   2 SVTFNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSYP-LWSGTVSLPAGTTIEYKYIK 66
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 317-610 1.37e-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: 68.27  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 317 PLDVGHRGAGNSTTTAqlakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYH---DLTCCLTMKKKFDADPVElfe 393
Cdd:cd08564     4 PIIVGHRGAGCSTLYP------ENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSIQLDDSGFKN--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 394 ipVKELTFDQLQLLKLAHVTALKSKDRKESMvaeensfseNQPFPSLKMVLESLPEDVGFNIEIKwicqqrdgmwdGNLS 473
Cdd:cd08564    75 --INDLSLDEITRLHFKQLFDEKPCGADEIK---------GEKIPTLEDVLVTFKDKLKYNIELK-----------GREV 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 474 ayfDMNLFldiILKTVLENSGKRRIVFSSFD----ADICTMVRHKQNRYPI--LFLTQGKSDIYPELmdlrsrttaiamS 547
Cdd:cd08564   133 ---GLGER---VLNLVEKYGMILQVHFSSFLhydrLDLLKALRPNKLNVPIalLFNEVKSPSPLDFL------------E 194

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1597555912 548 FAQFENLLGinAHTEDLLRNPSYIQEAKAKGLVIFCW--GDDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:cd08564   195 QAKYYNATW--VNFSYDFWTEEFVKKAHENGLKVMTYfdEPVNDNEEDYKVYLELGVDCICPNDP 257
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 317-609 7.43e-12

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: 66.53  E-value: 7.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 317 PLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLT--MKKKFDADPVELFEI 394
Cdd:cd08559     1 PLVIAHRGAS--------GYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTtnVAEHFPFRGRKDTGY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 395 PVKELTFDQLQLLKLAHVTALKSKDRKEsmvaeenSFSENQPFPSLKMVLE-------SLPEDVGFNIEIKwicqqrdgm 467
Cdd:cd08559    73 FVIDFTLAELKTLRAGSWFNQRYPERAP-------SYYGGFKIPTLEEVIElaqglnkSTGRNVGIYPETK--------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 468 wdgnlSAYFDMNLFLDI--ILKTVLE----NSGKRRIVFSSFDADICTMVRHKQNRYPILFLT-QGKSDIYPELMDLRSR 540
Cdd:cd08559   137 -----HPTFHKQEGPDIeeKLLEVLKkygyTGKNDPVFIQSFEPESLKRLRNETPDIPLVQLIdYGDWAETDKKYTYAWL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 541 TTAIAMSF-AQFENLLG------INAHTEDLLRNPSYIQEAKAKGLVIFCWgddTNDPEN-----------RRKLKELGV 602
Cdd:cd08559   212 TTDAGLKEiAKYADGIGpwksliIPEDSNGLLVPTDLVKDAHKAGLLVHPY---TFRNENlflapdfkqdmDALYNAAGV 288


                  ....*..
gi 1597555912 603 NGLIYDR 609
Cdd:cd08559   289 DGVFTDF 295
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 320-609 1.01e-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: 65.12  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGNstttaqlaKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFdadpvelfeiPVKEL 399
Cdd:cd08565     2 AGHRGGRN--------LWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTG----------AVRDL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TfdqlqllkLAHVTALKSKDRKESMVaeensfsenqpfPSLKMVLESL-PEDVGFNIEIKwicqqrdgmWDGNLSAYFDm 478
Cdd:cd08565    64 T--------LAERKALRLRDSFGEKI------------PTLEEVLALFaPSGLELHVEIK---------TDADGTPYPG- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 479 nlFLDIILKTVLENSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGKSdiypELMDLRSRTTAIAmsfaqFENLLGIN 558
Cdd:cd08565   114 --AAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPGVRTLGSVDEDML----ERLGGELPFLTAT-----ALKAHIVA 182

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1597555912 559 AHTEDLLRNPSYIQEAKaKGLVIFCWGddTNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08565   183 VEQSLLAATWELVRAAV-PGLRLGVWT--VNDDSLIRYWLACGVRQLTTDR 230
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 320-423 1.05e-11

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: 65.74  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGNStttaqlakVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFDadpvelfeipVKEL 399
Cdd:cd08573     2 IGHRGAGHD--------APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGL----------VAEL 63

                          90       100
                  ....*....|....*....|....
gi 1597555912 400 TFDQLQLLKLAHVTALKSKDRKES 423
Cdd:cd08573    64 TWEELRKLNAAAKHRLSSRFPGEK 87
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 5-69 4.57e-11

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). 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: 99883  Cd Length: 95  Bit Score: 59.69  E-value: 4.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1597555912   5 VTFEIRGTLLPGEVFAICGNCDVLGNWNPQNAVALTPENETgesmLWKATIVLSRGVSVQYRYFK 69
Cdd:cd05808     3 VTFNVTATTVWGQNVYVVGNVPELGNWSPANAVALSAATYP----VWSGTVDLPAGTAIEYKYIK 63
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 320-609 2.92e-10

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: 59.76  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAgnstttaqLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCcltmKKKFDADPVELFEIPVKEL 399
Cdd:cd08555     2 LSHRGY--------SQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTL----DRTTAGILPPTLEEVLELI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TfdqlQLLKlahvtalkskdrkesmvaeensfsenqpfpslkmvleSLPEDVGFNIEIKwicqQRDGMWDGNLSAyfdmn 479
Cdd:cd08555    70 A----DYLK-------------------------------------NPDYTIILSLEIK----QDSPEYDEFLAK----- 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 480 lFLDiILKTVLENSGKRRIVFSSFDAdictmvrhkqnrypilfLTQGKSDIYPelmdlrsrttaiamsfaqfenllgina 559
Cdd:cd08555   100 -VLK-ELRVYFDYDLRGKVVLSSFNA-----------------LGVDYYNFSS--------------------------- 133

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1597555912 560 hteDLLRNPSYIQEAKAKGLVIFCWGDDTNdPENRRKLKELGVNGLIYDR 609
Cdd:cd08555   134 ---KLIKDTELIASANKLGLLSRIWTVNDN-NEIINKFLNLGVDGLITDF 179
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 320-608 1.35e-09

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: 58.77  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKKKFDADPVElfeipVKEL 399
Cdd:cd08570     2 IGHRGYK--------AKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHD----PNLKRCFGKDGLI-----IDDS 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQLLKlahvtaLKSKDRkesmvaeensfsenQPFPSLKMVLESL----PEDVGFNIEIKwicqqrdgmwdgnlsay 475
Cdd:cd08570    65 TWDELSHLR------TIEEPH--------------QPMPTLKDVLEWLveheLPDVKLMLDIK----------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 476 FDMNlfLDIILKTVLE--------NSGKRRIVFSSFDADIctmvrhkqnrypILFLTQgksdIYPELmdlrsRTTAIAMS 547
Cdd:cd08570   108 RDND--PEILFKLIAEmlavkpdlDFWRERIILGLWHLDF------------LKYGKE----VLPGF-----PVFHIGFS 164

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1597555912 548 FA---QF----ENLLGINAH-----TEDLLRnpsYIQEAKAKGLVIFCWgddT-NDPENRRKLKELGVNGLIYD 608
Cdd:cd08570   165 LDyarHFlnysEKLVGISMHfvslwGPFGQA---FLPELKKNGKKVFVW---TvNTEEDMRYAIRLGVDGVITD 232
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 320-610 1.86e-09

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 58.80  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGnstttaQLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFdadpvelfeiPVKEL 399
Cdd:PRK09454   11 VAHRGGG------KLAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWG----------VAGEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 400 TFDQLQllklahvtALKSKDRKESMVAEEnsfsenqPFPSLKMVLESLPEDvGF--NIEIKwICQQRDgmWD-GNLSAYF 476
Cdd:PRK09454   73 TWQDLA--------QLDAGSWFSAAFAGE-------PLPTLSQVAARCRAH-GMaaNIEIK-PTTGRE--AEtGRVVALA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 477 DMNLFLDIILKTVLensgkrrivfSSFDADICTMVRHKQNRYPILFLtqgkSDIYPElmDLRSRTTAIAmsfaqfenLLG 556
Cdd:PRK09454  134 ARALWAGAAVPPLL----------SSFSEDALEAARQAAPELPRGLL----LDEWPD--DWLELTRRLG--------CVS 189

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1597555912 557 INAHTEDLlrNPSYIQEAKAKGLVIFCWgdDTNDPENRRKLKELGVNGLIYDRI 610
Cdd:PRK09454  190 LHLNHKLL--DEARVAALKAAGLRILVY--TVNDPARARELLRWGVDCICTDRI 239
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 4-69 2.41e-08

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: 51.94  E-value: 2.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1597555912   4 QVTFEIRGTLLP-GEVFAICGNCDVLGNWNPQNAVALTPENETgesmLWKATIVLSR-GVSVQYRYFK 69
Cdd:cd05816     1 VVQFKILCPYVPkGQSVYVTGSSPELGNWDPQKALKLSDVGFP----IWEADIDISKdSFPFEYKYII 64
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 323-458 4.73e-08

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: 55.06  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 323 RGAGNSTTTAqlAKVQ-------ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTC-CLTMKKKfdadpvelfei 394
Cdd:cd08613    39 EGVENDTCTA--ERIDppthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLdCRTDGSG----------- 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1597555912 395 PVKELTFDQLQLLKLAH-VTALKSKdrkesmvaeenSFsenqPF--------PSLKMVLESLPeDVGFNIEIK 458
Cdd:cd08613   106 VTRDHTMAELKTLDIGYgYTADGGK-----------TF----PFrgkgvgmmPTLDEVFAAFP-DRRFLINFK 162
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 317-609 5.52e-08

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: 54.24  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 317 PLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKKKFDAdpvelfeiPV 396
Cdd:cd08601     1 NAVIAHRGAS--------GYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPG--------PV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 397 KELTFDQLQLLklahvTALKSKDRKESMVAEEnSFSeNQPFPSLKMVLESLPEDVGFNIEIKwicqqrdgmwDGNLsaYF 476
Cdd:cd08601    65 KDYTLAEIKQL-----DAGSWFNKAYPEYARE-SYS-GLKVPTLEEVIERYGGRANYYIETK----------SPDL--YP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 477 DMNL-FLDIILKTVLE--NSGKRRIVFSSFDADICTMVRHKQNRYPILFLTQGK--SDIYPELMDL-RSRTTAIAMSFAQ 550
Cdd:cd08601   126 GMEEkLLATLDKYGLLtdNLKNGQVIIQSFSKESLKKLHQLNPNIPLVQLLWYGegAETYDKWLDEiKEYAIGIGPSIAD 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1597555912 551 FenllginahtedllrNPSYIQEAKAKGLVIFCWgdDTNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08601   206 A---------------DPWMVHLIHKKGLLVHPY--TVNEKADMIRLINWGVDGMFTNY 247
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 317-375 2.69e-07

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: 52.31  E-value: 2.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1597555912 317 PLDVGHRGAgnstttAQLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 375
Cdd:cd08574     2 PALIGHRGA------PMLAP--ENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRT 52
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 320-466 3.76e-07

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


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 51.55  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 320 VGHRGAGNSTTTaqlakVQENTIASLRNAASHGAAFvEFDVHLSKDFVPVVYHD-----LTCCltmkkkfdadpvelfEI 394
Cdd:cd08585     7 IAHRGLHDRDAG-----IPENSLSAFRAAAEAGYGI-ELDVQLTADGEVVVFHDdnlkrLTGV---------------EG 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1597555912 395 PVKELTFDQLqllklahvTALKSKDRKEsmvaeensfsenqPFPSLKMVLESLPEDVGFNIEIKwICQQRDG 466
Cdd:cd08585    66 RVEELTAAEL--------RALRLLGTDE-------------HIPTLDEVLELVAGRVPLLIELK-SCGGGDG 115
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 339-609 6.34e-07

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


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 51.45  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 339 ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCC-LTMKKKFdadpvelfeipVKELTFDQLQLLKL-------- 409
Cdd:cd08612    41 ENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLrSCGVDKL-----------VSDLNYADLPPYLEklevtfsp 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 410 AHVTALKSKDRKesmvaeensfsenqpFPSLKMVLESLPeDVGFNIEIKwicqqrdgmwdgnlsayFDMNLFLDIILKTV 489
Cdd:cd08612   110 GDYCVPKGSDRR---------------IPLLEEVFEAFP-DTPINIDIK-----------------VENDELIKKVSDLV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 490 LENSGKRRIVFSSFDADICTMvRHKQNRYPILFLTQGK---------------SDIYPELMDLRSRTTAIAMSFAQFENL 554
Cdd:cd08612   157 RKYKREDITVWGSFNDEIVKK-CHKENPNIPLFFSLKRvllllllyytgllpfIPIKESFLEIPMPSIFLKTYFPKSMSR 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912 555 LG--INAHTEDLLRNPSYIQEAKAKGLVIFCWgdDTNDPENRRKLKELGVNGLIYDR 609
Cdd:cd08612   236 LNrfVLFLIDWLLMRPSLFRHLQKRGIQVYGW--VLNDEEEFERAFELGADGVMTDY 290
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 314-449 2.76e-06

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: 49.92  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 314 PRTPLDVGHRGAgnstttAQLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD--LTCCLTMKKKFDadpvEL 391
Cdd:cd08609    24 PPKPALVGHRGA------PMLAP--ENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDegLLRTTNVKDVFP----GR 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1597555912 392 FEIPVKELTFDQLQLLKLAH----------VTALKSKDRKEsmvaeensfSENQPFPSLKMVLESLPE 449
Cdd:cd08609    92 DAAGSNNFTWTELKTLNAGSwflerrpfwtLSSLSEEDRRE---------ADNQTVPSLSELLDLAKK 150
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 317-458 3.79e-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: 48.86  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 317 PLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYH--DLTcCLTMKkkfdadpvelfEI 394
Cdd:cd08580     1 PLIVAHRGGT--------ADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRpsDLK-SLTNG-----------SG 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1597555912 395 PVKELTFDQLQLLKLAHvtALKSKDrkesmvaeeNSFSENQPF--PSLKMVLESLPeDVGFNIEIK 458
Cdd:cd08580    61 AVSAYTAAQLATLNAGY--NFKPEG---------GYPYRGKPVgiPTLEQVLRAFP-DTPFILDMK 114
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 315-375 1.34e-05

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation.


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 47.56  E-value: 1.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1597555912 315 RTPLDVGHRGAgnstttAQLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 375
Cdd:cd08610    21 PKPTIIGHRGA------PMLAP--ENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFT 73
CBM20_DPE2_repeat1 cd05815
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 16-68 1.52e-05

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 1. 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 starch binding 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 carbohydrate-binding domains. 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: 99889  Cd Length: 101  Bit Score: 43.97  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912  16 GEVFAICGNCDVLGNWNPQNAVALTPENEtGESMLWKATIVLSRGVSVQYRYF 68
Cdd:cd05815    13 GQSLLICGSDPLLGSWNVKKGLLLKPSHQ-GDVLVWSGSISVPPGFSSEYNYY 64
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 317-465 3.13e-05

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: 46.62  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 317 PLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD--LTCCLTMKKKFDADPVELFEI 394
Cdd:cd08600     1 KIIIAHRGAS--------GYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDhyLDNVTNVAEKFPDRKRKDGRY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597555912 395 PVKELTFDQLQLLKLAHVTALKSKDRKESMvaeENSFSENQP---FPSLKMVLE-------SLPEDVGFNIEIK--WICQ 462
Cdd:cd08600    73 YVIDFTLDELKSLSVTERFDIENGKKVQVY---PNRFPLWKSdfkIHTLEEEIEliqglnkSTGKNVGIYPEIKapWFHH 149


                  ...
gi 1597555912 463 QRD 465
Cdd:cd08600   150 QEG 152
PLN02950 PLN02950
4-alpha-glucanotransferase
 16-68 9.43e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 45.87  E-value: 9.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1597555912  16 GEVFAICGNCDVLGNWNPQNAVALTPENEtGESMLWKATIVLSRGVSVQYRYF 68
Cdd:PLN02950   22 GQSLLVCGSEPLLGSWNVKKGLLLSPVHQ-GDELVWEGSVSVPEGFSCEYSYY 73
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 18-69 6.11e-04

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic 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: 99885  Cd Length: 97  Bit Score: 39.31  E-value: 6.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1597555912  18 VFAIcGNCDVLGNWNPQNAVALTPENETgesmLWKATIVLSRGVSVQYRYFK 69
Cdd:cd05810    18 VYVV-GNVPQLGNWSPADAVKLDPTAYP----TWSGSISLPASTNVEWKCLK 64
PLN02950 PLN02950
4-alpha-glucanotransferase
 5-69 1.59e-03

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 41.63  E-value: 1.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912   5 VTFEIRGT-LLPGEVFAICGNCDVLGNWNPQNAVALtpeNETGESmLWKATIVLSRG-VSVQYRYFK 69
Cdd:PLN02950  155 VRFKIACPrLEEGTSVYVTGSIAQLGNWQVDDGLKL---NYTGDS-IWEADCLVPKSdFPIKYKYAL 217
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 317-373 1.80e-03

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: 40.74  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912 317 PLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD 373
Cdd:cd08602     1 PLVIAHRGAS--------GYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHE 49
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 317-373 2.51e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 40.81  E-value: 2.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1597555912 317 PLDVGHRGAGnstttaqlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD 373
Cdd:PRK11143   27 KIVIAHRGAS--------GYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHD 75
 
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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