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Conserved domains on  [gi|19922666|ref|NP_611548|]
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uncharacterized protein Dmel_CG9394, isoform A [Drosophila melanogaster]

Protein Classification

CBM20 and GDPD_GDE5 domain-containing protein( domain architecture ID 10333538)

CBM20 and GDPD_GDE5 domain-containing protein

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 ...
 345-630 1.12e-147

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: 430.56  E-value: 1.12e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 345 LEIGHRGLGKSLTvtTNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDLTEVLL 424
Cdd:cd08607   1 LDVGHRGAGNSYT--AASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKTYQIVGNKIVEYPA-HNNVEPPEQRLFPTLQDFFERVNLSTGFDIEIKWPQQRADGLFESEQ--TLDK 501
Cdd:cd08607  79 KDLTYEQLKLLKLFHISALKVKEYKSvEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELftYFDR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 502 NLFADRILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKEN---VFNDPRTSTVEQSVNFAQAFDLGGVS 578
Cdd:cd08607 159 NLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQrypEFMDLRTRTFEIAVNFAQAEELLGVN 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 19922666 579 PNAVFVKADPGLVQRAKAQVPIVLLWGSDLKDRESIDWFLQQGPTGVIYDRL 630
Cdd:cd08607 239 LHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
CBM20 super family cl15347
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 47-169 2.24e-38

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.


The actual alignment was detected with superfamily member cd05814:

Pssm-ID: 449530  Cd Length: 120  Bit Score: 138.22  E-value: 2.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666  47 KRNAPLVFNFTLtlpdadqlASFERPALVGNLPVLGAWQAGRAVLLNR-TAILNVWSASVEIPQNSSVEYRYFAAAV-GQ 124
Cdd:cd05814   1 CRVTFRVFASEL--------APGEVVAVVGSLPVLGNWQPEKAVPLEKeDDDCNLWKASIELPRGVDFQYRYFVAVVlND 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19922666 125 SGAVQI--RRWESHVQARTFNTT-KFSGNRSDEFGLIGNERQLSRGWL 169
Cdd:cd05814  73 SGPCQVivRKWETHLQPRSIKPLeEERLNDDDKFGIYDGVEQVDRGWL 120
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 345-630 1.12e-147

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: 430.56  E-value: 1.12e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 345 LEIGHRGLGKSLTvtTNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDLTEVLL 424
Cdd:cd08607   1 LDVGHRGAGNSYT--AASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKTYQIVGNKIVEYPA-HNNVEPPEQRLFPTLQDFFERVNLSTGFDIEIKWPQQRADGLFESEQ--TLDK 501
Cdd:cd08607  79 KDLTYEQLKLLKLFHISALKVKEYKSvEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELftYFDR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 502 NLFADRILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKEN---VFNDPRTSTVEQSVNFAQAFDLGGVS 578
Cdd:cd08607 159 NLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQrypEFMDLRTRTFEIAVNFAQAEELLGVN 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 19922666 579 PNAVFVKADPGLVQRAKAQVPIVLLWGSDLKDRESIDWFLQQGPTGVIYDRL 630
Cdd:cd08607 239 LHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 349-632 1.54e-59

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: 200.32  E-value: 1.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666   349 HRGLGKSLTvttnaapliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPtskddltevlLKDIS 428
Cdd:pfam03009   1 HRGASGSYP---------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY----------VRDLT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666   429 YEQLKDLKTyqivGNKIVEYPAHNNVEppeqrlFPTLQDFFERvNLSTGFDIEIKWPQQRADGLFES-EQTLDKNLFADR 507
Cdd:pfam03009  62 LEELKRLDI----GAGNSGPLSGERVP------FPTLEEVLEF-DWDVGFNIEIKIKPYVEAIAPEEgLIVKDLLLSVDE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666   508 ILAvvrRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKENVFNDprtsTVEQSVNFAQAFDLGGVSPNAVFVKad 587
Cdd:pfam03009 131 ILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRAYAEAD----LLERAAAFAGAPALLGEVALVDEAL-- 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 19922666   588 PGLVQRAKAQVPIVLLWGSDlkDRESIDWFLQQGPTGVIYDRLDL 632
Cdd:pfam03009 202 PDLVKRAHARGLVVHVWTVN--NEDEMKRLLELGVDGVITDRPDT 244
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 47-169 2.24e-38

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: 138.22  E-value: 2.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666  47 KRNAPLVFNFTLtlpdadqlASFERPALVGNLPVLGAWQAGRAVLLNR-TAILNVWSASVEIPQNSSVEYRYFAAAV-GQ 124
Cdd:cd05814   1 CRVTFRVFASEL--------APGEVVAVVGSLPVLGNWQPEKAVPLEKeDDDCNLWKASIELPRGVDFQYRYFVAVVlND 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19922666 125 SGAVQI--RRWESHVQARTFNTT-KFSGNRSDEFGLIGNERQLSRGWL 169
Cdd:cd05814  73 SGPCQVivRKWETHLQPRSIKPLeEERLNDDDKFGIYDGVEQVDRGWL 120
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
347-636 1.18e-31

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 123.06  E-value: 1.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKsltvttnAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIrvcidsktptskDDLTEV--LL 424
Cdd:COG0584   6 IAHRGASG-------LAP--ENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL------------DRTTNGtgRV 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKtyqivgnkiveypAHNNVEPPEQRLfPTLQDFFERVNLSTGFDIEIKWPQQRADGlfeseqtldknlF 504
Cdd:COG0584  65 ADLTLAELRQLD-------------AGSGPDFAGERI-PTLEEVLELVPGDVGLNIEIKSPPAAEPD------------L 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 505 ADRILAVVRRHGCGRLNVIKSFDADlcSLLRFKQHM--YPVLFLSSskenvfndprtSTVEQSVNFAQAFDLGGVSPNAV 582
Cdd:COG0584 119 AEAVAALLKRYGLEDRVIVSSFDPE--ALRRLRELApdVPLGLLVE-----------ELPADPLELARALGADGVGPDYD 185

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19922666 583 FVkaDPGLVQRAKAQ-VPiVLLWGsdLKDRESIDWFLQQGPTGVIYDRLDLWLGA 636
Cdd:COG0584 186 LL--TPELVAAAHAAgLK-VHVWT--VNDPEEMRRLLDLGVDGIITDRPDLLRAV 235
CBM_2 smart01065
Starch binding domain;
70-136 1.03e-10

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 58.51  E-value: 1.03e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922666     70 ERPALVGNLPVLGAWQAGRAVLLNR-TAILNVWSASVEIP-QNSSVEYRYFaaaVGQSGavQIRRWESH 136
Cdd:smart01065  16 ESVYVVGSVPELGNWNPKKAVPLSPdTDGYPLWKGTVSLPpAGTTIEYKYV---KVDED--GSVTWESG 79
CBM_20 pfam00686
Starch binding domain;
74-135 6.44e-08

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 50.75  E-value: 6.44e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922666    74 LVGNLPVLGAWQAGRAVLL--NRTAILNVWSASVEIPQNSSVEYRYfaAAVGQSGAVqirRWES 135
Cdd:pfam00686  19 IVGSIPELGNWNPKKAIALsaSEYSSYPLWSGTVSLPAGTTIEYKY--IKVDSDGSV---TWES 77
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 347-401 2.84e-04

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 43.00  E-value: 2.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19922666  347 IGHRGLGKsltvttnAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHD 401
Cdd:PRK09454  11 VAHRGGGK-------LAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHD 56
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 345-630 1.12e-147

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: 430.56  E-value: 1.12e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 345 LEIGHRGLGKSLTvtTNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDLTEVLL 424
Cdd:cd08607   1 LDVGHRGAGNSYT--AASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKTYQIVGNKIVEYPA-HNNVEPPEQRLFPTLQDFFERVNLSTGFDIEIKWPQQRADGLFESEQ--TLDK 501
Cdd:cd08607  79 KDLTYEQLKLLKLFHISALKVKEYKSvEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELftYFDR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 502 NLFADRILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKEN---VFNDPRTSTVEQSVNFAQAFDLGGVS 578
Cdd:cd08607 159 NLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQrypEFMDLRTRTFEIAVNFAQAEELLGVN 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 19922666 579 PNAVFVKADPGLVQRAKAQVPIVLLWGSDLKDRESIDWFLQQGPTGVIYDRL 630
Cdd:cd08607 239 LHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 345-630 6.60e-122

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: 364.68  E-value: 6.60e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 345 LEIGHRGLGKSLTvTTNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDLTEVLL 424
Cdd:cd08572   1 LVIGHRGLGKNYA-SGSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDEGELIEVPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKTYQIVGNKIVEY------PAHNNVEPPEQRLFPTLQDFFERVNLSTGFDIEIKWPQQRADGLFESEQT 498
Cdd:cd08572  80 HDLTLEQLKELGLQHISALKRKALtrkakgPKPNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYPQLLEDGEGELTPY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 499 LDKNLFADRILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKEN--VFNDPRTSTVEQSVNFAQAFDLGG 576
Cdd:cd08572 160 FERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNGGTNevEHMDPRRRSLQAAVNFALAEGLLG 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 19922666 577 VSPNAVFVKADPGLVQRAKAQVPIVLLWGSDLKDRESIDWFLQQGPTGVIYDRL 630
Cdd:cd08572 240 VVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQKELGVDGVIYDRV 293
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 349-632 1.54e-59

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: 200.32  E-value: 1.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666   349 HRGLGKSLTvttnaapliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPtskddltevlLKDIS 428
Cdd:pfam03009   1 HRGASGSYP---------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY----------VRDLT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666   429 YEQLKDLKTyqivGNKIVEYPAHNNVEppeqrlFPTLQDFFERvNLSTGFDIEIKWPQQRADGLFES-EQTLDKNLFADR 507
Cdd:pfam03009  62 LEELKRLDI----GAGNSGPLSGERVP------FPTLEEVLEF-DWDVGFNIEIKIKPYVEAIAPEEgLIVKDLLLSVDE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666   508 ILAvvrRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKENVFNDprtsTVEQSVNFAQAFDLGGVSPNAVFVKad 587
Cdd:pfam03009 131 ILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRAYAEAD----LLERAAAFAGAPALLGEVALVDEAL-- 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 19922666   588 PGLVQRAKAQVPIVLLWGSDlkDRESIDWFLQQGPTGVIYDRLDL 632
Cdd:pfam03009 202 PDLVKRAHARGLVVHVWTVN--NEDEMKRLLELGVDGVITDRPDT 244
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 347-629 2.05e-40

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: 149.48  E-value: 2.05e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKSLT-VTTNAAPLI-ENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVcidsktpTSKDDLTEVLL 424
Cdd:cd08605   3 IGHRGLGMNRAsHQPSVGPGIrENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVV-------ERGGEVESSRI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKTyQIVGNKIVEYPAHNNVEPPEQRLF--------PTLQDFFERVNLSTGFDIEIKWpqqrADGLFESE 496
Cdd:cd08605  76 RDLTLAELKALGP-QAESTKTSTVALYRKAKDPEPEPWimdvedsiPTLEEVFSEVPPSLGFNIELKF----GDDNKTEA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 497 QTLDKNLFAdrILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKENVFNDPRTSTVEQSVNFAQAFDLGG 576
Cdd:cd08605 151 EELVRELRA--ILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHNDPRRNSIEAAIQVALEGGLQG 228

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 19922666 577 VSPNAVFVKADPGLVQRAKAQVPIVLLWGSDLKDRESIDWFLQQGPTGVIYDR 629
Cdd:cd08605 229 IVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDH 281
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 347-630 2.24e-40

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: 149.52  E-value: 2.24e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKSlTVTTNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRvciDSKTPTSKDDLTEVLLKD 426
Cdd:cd08606   5 IGHRGLGKN-TAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVS---ETGTDVPIHDLTLEQFLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEQL-KDLKTYQIVGNKIveypAHNNVEPpeqrlFPTLQDFFERVNLSTGFDIEIKWPQqradgLFESEQ------TL 499
Cdd:cd08606  81 LSRMKYtVDFKKKGFKGNSR----GHSIQAP-----FTTLEELLKKLPKSVGFNIELKYPM-----LHEAEEeevapvAI 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 500 DKNLFADRILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKENVFNDPRTSTVEQSVNFAQAFDLGG-VS 578
Cdd:cd08606 147 ELNAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGKAPDMDVRAASLQEAIRFAKQWNLLGlVS 226

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 19922666 579 PNAVFVKAdPGLVQRAKAQVPIVLLWGSDLKDRESIDWFLQQGPTGVIYDRL 630
Cdd:cd08606 227 AAEPLVMC-PRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSV 277
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 47-169 2.24e-38

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: 138.22  E-value: 2.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666  47 KRNAPLVFNFTLtlpdadqlASFERPALVGNLPVLGAWQAGRAVLLNR-TAILNVWSASVEIPQNSSVEYRYFAAAV-GQ 124
Cdd:cd05814   1 CRVTFRVFASEL--------APGEVVAVVGSLPVLGNWQPEKAVPLEKeDDDCNLWKASIELPRGVDFQYRYFVAVVlND 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19922666 125 SGAVQI--RRWESHVQARTFNTT-KFSGNRSDEFGLIGNERQLSRGWL 169
Cdd:cd05814  73 SGPCQVivRKWETHLQPRSIKPLeEERLNDDDKFGIYDGVEQVDRGWL 120
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
347-636 1.18e-31

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 123.06  E-value: 1.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKsltvttnAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIrvcidsktptskDDLTEV--LL 424
Cdd:COG0584   6 IAHRGASG-------LAP--ENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL------------DRTTNGtgRV 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKtyqivgnkiveypAHNNVEPPEQRLfPTLQDFFERVNLSTGFDIEIKWPQQRADGlfeseqtldknlF 504
Cdd:COG0584  65 ADLTLAELRQLD-------------AGSGPDFAGERI-PTLEEVLELVPGDVGLNIEIKSPPAAEPD------------L 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 505 ADRILAVVRRHGCGRLNVIKSFDADlcSLLRFKQHM--YPVLFLSSskenvfndprtSTVEQSVNFAQAFDLGGVSPNAV 582
Cdd:COG0584 119 AEAVAALLKRYGLEDRVIVSSFDPE--ALRRLRELApdVPLGLLVE-----------ELPADPLELARALGADGVGPDYD 185

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19922666 583 FVkaDPGLVQRAKAQ-VPiVLLWGsdLKDRESIDWFLQQGPTGVIYDRLDLWLGA 636
Cdd:COG0584 186 LL--TPELVAAAHAAgLK-VHVWT--VNDPEEMRRLLDLGVDGIITDRPDLLRAV 235
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 347-629 7.09e-24

Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins; The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases.


Pssm-ID: 176499 [Multi-domain]  Cd Length: 189  Bit Score: 99.26  E-value: 7.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKsltvttnAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFsirvcidsktptskddltevllkd 426
Cdd:cd08556   2 IAHRGASG-------EAP--ENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDI------------------------ 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 isyeqlkdlktyqivgnkiveypahnnveppeqrlfPTLQDFFERVNLSTGFDIEIKWPQQRADglfeseqtldknlFAD 506
Cdd:cd08556  49 ------------------------------------PTLEEVLELVKGGVGLNIELKEPTRYPG-------------LEA 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 507 RILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKENVFNDPRTstveqsvnfAQAFDLGGVSPNAVFVka 586
Cdd:cd08556  80 KVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAEL---------ARALGADAVNPHYKLL-- 148

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 19922666 587 DPGLVQRAKAQVPIVLLWGSDlkDRESIDWFLQQGPTGVIYDR 629
Cdd:cd08556 149 TPELVRAAHAAGLKVYVWTVN--DPEDARRLLALGVDGIITDD 189
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 347-632 6.23e-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: 90.06  E-value: 6.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlGKSLTvttnaaplIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHD--FSIRVCIDSKTPTSKDDltEVLL 424
Cdd:cd08567   4 QGHRG-ARGLL--------PENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDpkLNPDITRDPDGAWLPYE--GPAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDL----KTYQIVGNKivEYPAHNNVepPEQRLfPTLQDFFERVNLSTG----FDIEIK-WPQQRADGLFES 495
Cdd:cd08567  73 YELTLAEIKQLdvgeKRPGSDYAK--LFPEQIPV--PGTRI-PTLEEVFALVEKYGNqkvrFNIETKsDPDRDILHPPPE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 496 EqtldknlFADRILAVVRRHGCGRLNVIKSFDAdlcSLLRFKQHMYPVLflssskenvfndpRTS--TVEQ-SVNFAQAF 572
Cdd:cd08567 148 E-------FVDAVLAVIRKAGLEDRVVLQSFDW---RTLQEVRRLAPDI-------------PTValTEETtLGNLPRAA 204

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922666 573 -DLGGVSPNAVFVKADPGLVQRAKAQVPIVLLWGSDlkDRESIDWFLQQGPTGVIYDRLDL 632
Cdd:cd08567 205 kKLGADIWSPYFTLVTKELVDEAHALGLKVVPWTVN--DPEDMARLIDLGVDGIITDYPDL 263
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 347-529 2.23e-14

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: 73.79  E-value: 2.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLgksltvttnAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDLTEVLLKD 426
Cdd:cd08575   4 IAHRGG---------AAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEqlkdlktYQIVGNKiVEYPAHNNVeppeqRLFPTLQDFFERVNlSTGFDIEIKwpqqradglfeseqTLDKNLFAD 506
Cdd:cd08575  75 AGYG-------YTFDGGK-TGYPRGGGD-----GRIPTLEEVFKAFP-DTPINIDIK--------------SPDAEELIA 126

                       170       180
                ....*....|....*....|...
gi 19922666 507 RILAVVRRHGCGRLNVIKSFDAD 529
Cdd:cd08575 127 AVLDLLEKYKREDRTVWGSTNPE 149
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 347-632 2.63e-14

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


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 72.73  E-value: 2.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLgksltvtTNAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSI-RVCIDSKtptskddltevLLK 425
Cdd:cd08582   2 IAHRGA-------SAEAP--ENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLkRTSGGDG-----------AVS 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 426 DISYEQLKDLKtyqiVGNKIVEYPAHNNVeppeqrlfPTLQDFFERVN-LSTGFDIEIKWPqQRADGLFEseqtldknlf 504
Cdd:cd08582  62 DLTLAELRKLD----IGSWKGESYKGEKV--------PTLEEYLAIVPkYGKKLFIEIKHP-RRGPEAEE---------- 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 505 adRILAVVRRHGCGRLN-VIKSFDADLcsLLRFKQHM--YPVLFLSSSKenvfnDPRTST--VEQSVNFAqafdlgGVSP 579
Cdd:cd08582 119 --ELLKLLKESGLLPEQiVIISFDAEA--LKRVRELAptLETLWLRNYK-----SPKEDPrpLAKSGGAA------GLDL 183

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 19922666 580 NAVFVKaDPGLVQRAKAQVPIVLLWGSDlkDRESIDWFLQQGPTGVIYDRLDL 632
Cdd:cd08582 184 SYEKKL-NPAFIKALRDAGLKLNVWTVD--DAEDAKRLIELGVDSITTNRPGR 233
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 347-535 3.28e-14

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: 72.72  E-value: 3.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLgksltvTTNAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIrvcidSKTPTSKDDLTEVLLKD 426
Cdd:cd08566   3 VAHRGG------WGAGAP--ENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTL-----DRTTNGKGKVSDLTLAE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEQLKDlktyqivgnkiveypahNNVEPPEQRLfPTLQDFFE----RVNLstgfDIEIKWPqqradglfeseqtldkn 502
Cdd:cd08566  70 IRKLRLKD-----------------GDGEVTDEKV-PTLEEALAwakgKILL----NLDLKDA----------------- 110

                       170       180       190
                ....*....|....*....|....*....|...
gi 19922666 503 lFADRILAVVRRHGCGRLNVIKSFDADLCSLLR 535
Cdd:cd08566 111 -DLDEVIALVKKHGALDQVIFKSYSEEQAKELR 142
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 347-557 2.20e-12

Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermotoga maritime glycerophosphodiester phosphodiesterase (TmGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. TmGDE exists as a monomer that might be the biologically relevant form.


Pssm-ID: 176511 [Multi-domain]  Cd Length: 226  Bit Score: 66.94  E-value: 2.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGksltvttnaAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRvcidsktptsKDDLTEVLLKD 426
Cdd:cd08568   3 LGHRGYR---------AKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLK----------RVGGVDLKVKE 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEQLKDLKtyqivgnkiveypahnnvepPEQRLFPTLQDFFERVNLSTGFDIEIKwpqqradglfeseqtlDKNLfAD 506
Cdd:cd08568  64 LTYKELKKLH--------------------PGGELIPTLEEVFRALPNDAIINVEIK----------------DIDA-VE 106

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19922666 507 RILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKENVFNDP 557
Cdd:cd08568 107 PVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEGFSIP 157
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 347-546 4.01e-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: 67.30  E-value: 4.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvTTNAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSI-RVC-IDSKTPTSKDDLTEVLL 424
Cdd:cd08559   4 IAHRG-------ASGYAP--EHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLdRTTnVAEHFPFRGRKDTGYFV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKtyqiVGNKIVE-YPahnNVEPPEQRLF--PTLQDFFERV---NLSTGFD----IEIKWPQqradglFE 494
Cdd:cd08559  75 IDFTLAELKTLR----AGSWFNQrYP---ERAPSYYGGFkiPTLEEVIELAqglNKSTGRNvgiyPETKHPT------FH 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922666 495 SEQTLDknlFADRILAVVRRHGCGRLN---VIKSFDADlcSLLRFKQHM--YPVLFL 546
Cdd:cd08559 142 KQEGPD---IEEKLLEVLKKYGYTGKNdpvFIQSFEPE--SLKRLRNETpdIPLVQL 193
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 347-595 9.46e-12

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: 65.80  E-value: 9.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvTTNAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSirvcIDSKTPTSKDDltevLLKD 426
Cdd:cd08601   4 IAHRG-------ASGYAP--EHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDET----LDRTTNIERPG----PVKD 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEQLKDLKtyqiVG---NKivEYPAHNNVEPPEQRLfPTLQDFFERVNLSTGFDIEIKWPqqradglfeseqtldkNL 503
Cdd:cd08601  67 YTLAEIKQLD----AGswfNK--AYPEYARESYSGLKV-PTLEEVIERYGGRANYYIETKSP----------------DL 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 504 FAD---RILAVVRRHGCGRLN------VIKSFDADlcSLLRFKQHM--YPVLFLSSSKENVfndprtSTVEQSVNFAQAF 572
Cdd:cd08601 124 YPGmeeKLLATLDKYGLLTDNlkngqvIIQSFSKE--SLKKLHQLNpnIPLVQLLWYGEGA------ETYDKWLDEIKEY 195

                       250       260
                ....*....|....*....|...
gi 19922666 573 DLgGVSPNavFVKADPGLVQRAK 595
Cdd:cd08601 196 AI-GIGPS--IADADPWMVHLIH 215
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 347-483 3.00e-11

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: 63.78  E-value: 3.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKSltvttnaAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSkddltevllkD 426
Cdd:cd08562   2 IAHRGASSL-------AP--ENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVT----------E 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19922666 427 ISYEQLKDLKtyqiVGNKIVEYPAHnnvEPpeqrlFPTLQDFFERVN-LSTGFDIEIK 483
Cdd:cd08562  63 LTWAELAQLD----AGSWFSPEFAG---EP-----IPTLADVLELAReLGLGLNLEIK 108
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 347-540 3.53e-11

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: 63.73  E-value: 3.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRG-LGKsltvttnaAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSI-RVCidsktptskdDLTEVlL 424
Cdd:cd08563   4 FAHRGySGT--------AP--ENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVdRTT----------NGKGY-V 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 425 KDISYEQLKDLKtyqiVGNKIveypahnNVEPPEQRLfPTLQDFFervNLSTGFD----IEIKwpqqradglfeSEQTLD 500
Cdd:cd08563  63 KDLTLEELKKLD----AGSWF-------DEKFTGEKI-PTLEEVL---DLLKDKDlllnIEIK-----------TDVIHY 116

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19922666 501 KNLfADRILAVVRRHGCGRLNVIKSFDADlcSLLRFKQHM 540
Cdd:cd08563 117 PGI-EKKVLELVKEYNLEDRVIFSSFNHE--SLKRLKKLD 153
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 347-630 7.31e-11

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: 62.56  E-value: 7.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltVTTNAApliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSI-RVCIDSKTPtskDDLTevllk 425
Cdd:cd08579   2 IAHRG------VSSNGV---ENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLkRLAGVNKKV---WDLT----- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 426 disyeqLKDLKTYQIVGNKIVEYpahnnveppeqrlFPTLQDFFERVN-LSTGFDIEIKWPQQradglfESEQTLDKnlF 504
Cdd:cd08579  65 ------LEELKKLTIGENGHGAK-------------IPSLDEYLALAKgLKQKLLIELKPHGH------DSPDLVEK--F 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 505 ADRILAVVRRHGCgrlnVIKSFDADLcsLLRFKQ--------HMYPVLFLSSSKENV-FndprtSTVEQSVnfaqafdlg 575
Cdd:cd08579 118 VKLYKQNLIENQH----QVHSLDYRV--IEKVKKldpkiktgYILPFNIGNLPKTNVdF-----YSIEYST--------- 177

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19922666 576 gvspnavfvkADPGLVQRAKAQVPIVLLWGSDlkDRESIDWFLQQGPTGVIYDRL 630
Cdd:cd08579 178 ----------LNKEFIRQAHQNGKKVYVWTVN--DPDDMQRYLAMGVDGIITDYP 220
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 347-548 8.49e-11

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: 62.35  E-value: 8.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvttNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSI-RVCIdsktptskddlTEVLLK 425
Cdd:cd08581   2 VAHRG---------YPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLlRLTG-----------VEGLLH 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 426 DISYEQLKDLKtyqivgnkiVEYPAHNNVEPPEQRLfPTLQDFFERVNLSTGFD--IEIKWPqqrADGLFESEQTLDKNL 503
Cdd:cd08581  62 ELEDAELDSLR---------VAEPARFGSRFAGEPL-PSLAAVVQWLAQHPQVTlfVEIKTE---SLDRFGLERVVDKVL 128

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19922666 504 FADRILAVVRrhgcgrlnVIKSFDADLCSLLRfKQHMYPVLFLSS 548
Cdd:cd08581 129 RALPAVAAQR--------VLISFDYDLLALAK-QQGGPRTGWVLP 164
CBM_2 smart01065
Starch binding domain;
70-136 1.03e-10

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 58.51  E-value: 1.03e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922666     70 ERPALVGNLPVLGAWQAGRAVLLNR-TAILNVWSASVEIP-QNSSVEYRYFaaaVGQSGavQIRRWESH 136
Cdd:smart01065  16 ESVYVVGSVPELGNWNPKKAVPLSPdTDGYPLWKGTVSLPpAGTTIEYKYV---KVDED--GSVTWESG 79
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 347-461 1.36e-10

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: 63.15  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKS-----LTVTTNAA--------PLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTP 413
Cdd:cd08613  27 LAHRGLAQTfdregVENDTCTAeridppthDYLENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGV 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19922666 414 TSKDDLTEVLLKDISYEQLKD-LKTYQIVGNKIVEYPAHNNV--EPPEQRL 461
Cdd:cd08613 107 TRDHTMAELKTLDIGYGYTADgGKTFPFRGKGVGMMPTLDEVfaAFPDRRF 157
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 347-480 4.57e-10

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: 60.74  E-value: 4.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKSltvttnaAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSirvcIDSKTPTSKDdltevlLKD 426
Cdd:cd08573   2 IGHRGAGHD-------AP--ENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDT----VDRTTDGTGL------VAE 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922666 427 ISYEQLKDLktyqivgNKIVEYPAHNNVepPEQRLfPTLQD---FFERVNLSTGFDI 480
Cdd:cd08573  63 LTWEELRKL-------NAAAKHRLSSRF--PGEKI-PTLEEavkECLENNLRMIFDV 109
GDPD_NUC-2_fungi cd08578
Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and ...
 354-577 4.85e-10

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: 61.18  E-value: 4.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 354 KSLTVTTNAAPLIENTVATmlaSSELGADLVEFDVQLTSDLVPIIHHDFSIRVcidsktPTSKddlteVLLKDISYEQLK 433
Cdd:cd08578   5 KSTSGSDTQANKDGNSFVT---ASSLSGEYLRVKVCVLKDGTPVVAPEWFVPV------GGIK-----LLVSDLTAEQLE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 434 DLKTYQIVGNKiveyPAHNNVEPPEQRL---FPTLQDFFERVNLSTGFDIEIKWP--QQRADGLFESEQTLDKNLFADRI 508
Cdd:cd08578  71 SILDYSLDDLN----SEISDMVDLKRLLssrVVSLETLLELLPPSIQLDIQVLFPtaAEIASIPVKGSPLVDLNKFIDTV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 509 LAVV------RRHGCG--RLNVIKSFDADLCSLLRFKQHMYPVLF-------------------LSSSKEN----VFNDP 557
Cdd:cd08578 147 LLVVfdharyLRHTPGstRSIVFSSCNPEVCTILNWKQPNFPVFFamnglvrnndtlsfdtphhLDSLAVDpqklNEADP 226

                       250       260
                ....*....|....*....|
gi 19922666 558 RTSTVEQSVNFAQAFDLGGV 577
Cdd:cd08578 227 RSRSIKEAVRFAKNNNLLGL 246
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 347-552 1.70e-09

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: 58.57  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvTTNAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDLTEVLLKD 426
Cdd:cd08565   2 AGHRG-------GRNLWP--ENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEQlkdlktyqivGNKIveypahnnveppeqrlfPTLQDFFE-RVNLSTGFDIEIKwpqQRADGLFESEqtldknlFA 505
Cdd:cd08565  73 LRDSF----------GEKI-----------------PTLEEVLAlFAPSGLELHVEIK---TDADGTPYPG-------AA 115

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19922666 506 DRILAVVRRHGCGRLNVIKSFDADLCSLLRFKQHMYPVLFLSSSKEN 552
Cdd:cd08565 116 ALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPGVRTLGSVDEDMLE 162
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 347-516 2.92e-09

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: 58.04  E-value: 2.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlGKSLtvttnaAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSirvcIDSKTptskdDLTEvLLKD 426
Cdd:cd08561   2 IAHRG-GAGL------AP--ENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDET----LDRTT-----DGTG-PVAD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 427 ISYEQLKDLK-TYQIVGNKIVEYPAHNNVEPPeqrlfPTLQDFFE-----RVNlstgfdIEIKWPQQRAdglfeseqtld 500
Cdd:cd08561  63 LTLAELRRLDaGYHFTDDGGRTYPYRGQGIRI-----PTLEELFEafpdvRLN------IEIKDDGPAA----------- 120

                       170
                ....*....|....*.
gi 19922666 501 knlfADRILAVVRRHG 516
Cdd:cd08561 121 ----AAALADLIERYG 132
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 70-135 2.78e-08

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: 51.91  E-value: 2.78e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922666  70 ERPALVGNLPVLGAWQAGRAVLLNRTAILNVWSASVEIP--QNSSVEYRYFaaAVGQSGAVQirrWES 135
Cdd:cd05467  14 QSVYVVGSHPELGNWDPAKALRLNTSNSYPLWTGEIPLPapEGQVIEYKYV--IVDDDGNVQ---WES 76
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 74-135 3.14e-08

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: 51.89  E-value: 3.14e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922666  74 LVGNLPVLGAWQAGRAVLLNR---TAILNVWSASVEIPQNSSVEYRYFaaAVGQSGAVqirRWES 135
Cdd:cd05811  25 IVGSIPQLGNWDTSSAVALSAsqyTSSNPLWSVTIPLPAGTSFEYKFI--RKESDGSV---TWES 84
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 74-144 6.41e-08

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: 50.83  E-value: 6.41e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922666  74 LVGNLPVLGAWQAGRAVLLnRTAILNVWSASVEIPQNSSVEYRYFaaAVGQSGAVQirrWESHvQARTFNT 144
Cdd:cd05808  19 VVGNVPELGNWSPANAVAL-SAATYPVWSGTVDLPAGTAIEYKYI--KKDGSGTVT---WESG-PNRTATT 82
CBM_20 pfam00686
Starch binding domain;
74-135 6.44e-08

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 50.75  E-value: 6.44e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922666    74 LVGNLPVLGAWQAGRAVLL--NRTAILNVWSASVEIPQNSSVEYRYfaAAVGQSGAVqirRWES 135
Cdd:pfam00686  19 IVGSIPELGNWNPKKAIALsaSEYSSYPLWSGTVSLPAGTTIEYKY--IKVDSDGSV---TWES 77
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 347-470 3.75e-06

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: 48.76  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKSLTvttnaapliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIRVCIDSKTPTSKDDltevllkd 426
Cdd:cd08570   2 IGHRGYKAKYP---------ENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDS-------- 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19922666 427 iSYEQLKDLKTyqivgnkiveypahnnVEPPEQRLfPTLQDFFE 470
Cdd:cd08570  65 -TWDELSHLRT----------------IEEPHQPM-PTLKDVLE 90
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 347-578 8.80e-06

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


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 47.85  E-value: 8.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLGKSLTvttnaAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHH--------DFSIRvCIDSKTPTSKDD 418
Cdd:cd08564   7 VGHRGAGCSTL-----YP--ENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQ-LDDSGFKNINDL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 419 -LTEVLLKDISYEQLKDLKTYQIVGNKIVeypahnnveppeqrlfPTLQDFFERVNLSTGFDIEIKWPqqradglfeseq 497
Cdd:cd08564  79 sLDEITRLHFKQLFDEKPCGADEIKGEKI----------------PTLEDVLVTFKDKLKYNIELKGR------------ 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 498 tldKNLFADRILAVVRRHGCGRLNVIKSFdadlcsllrfkQHMYPVLF---LSSSKENV-----FNDPRTSTVEQSVNFA 569
Cdd:cd08564 131 ---EVGLGERVLNLVEKYGMILQVHFSSF-----------LHYDRLDLlkaLRPNKLNVpiallFNEVKSPSPLDFLEQA 196


                ....*....
gi 19922666 570 QAFDLGGVS 578
Cdd:cd08564 197 KYYNATWVN 205
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 347-539 1.80e-05

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


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 46.55  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGLgksltvTTNAAPLIENTVATMLASSELGADlVEFDVQLTSDLVPIIHHDFSI-RVCidsktptskddLTEVLLK 425
Cdd:cd08585   7 IAHRGL------HDRDAGIPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLkRLT-----------GVEGRVE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 426 DISYEQLKDLKtyqIVGNKiveypahnnvEPpeqrlFPTLQDFFERVNLSTGFDIEIKWPQQRADGLfeseqtldknlfA 505
Cdd:cd08585  69 ELTAAELRALR---LLGTD----------EH-----IPTLDEVLELVAGRVPLLIELKSCGGGDGGL------------E 118

                       170       180       190
                ....*....|....*....|....*....|....
gi 19922666 506 DRILAVVRRHGcGRLnVIKSFDADLcsLLRFKQH 539
Cdd:cd08585 119 RRVLAALKDYK-GPA-AIMSFDPRV--VRWFRKL 148
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 347-526 2.77e-05

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: 46.52  E-value: 2.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvttnaAPLI--ENTVATMLASSELGADLVEFDVQLTSDLVPIIHHD--------------FSirvciDS 410
Cdd:cd08602   4 IAHRG-----------ASGYrpEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEpelsgttdvadhpeFA-----DR 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 411 KTpTSKDD---LTEVLLKDISYEQLKDLKTYQivgnkivEYPAHNnvePPEQRLF--PTLQDFFE-------RVNLSTGF 478
Cdd:cd08602  68 KT-TKTVDgvnVTGWFTEDFTLAELKTLRARQ-------RLPYRD---QSYDGQFpiPTFEEIIAlakaasaATGRTVGI 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 19922666 479 DIEIKWP---QQRADGLFEseqtldknlfaDRILAVVRRHGCGRLN---VIKSF 526
Cdd:cd08602 137 YPEIKHPtyfNAPLGLPME-----------DKLLETLKKYGYTGKKapvFIQSF 179
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 75-135 4.76e-05

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: 42.78  E-value: 4.76e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922666  75 VGNLPVLGAWQAGRAVLLNRTAiLNVWSASVEIPQNSSVEYRYFAAAvgQSGAVQIRRWES 135
Cdd:cd05810  21 VGNVPQLGNWSPADAVKLDPTA-YPTWSGSISLPASTNVEWKCLKRN--ETNPTAGVQWQG 78
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 347-534 5.20e-05

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: 45.67  E-value: 5.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvttNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSI-RVCIDSKTptskddltevlLK 425
Cdd:cd08612  30 ISHRG---------GSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLlRSCGVDKL-----------VS 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 426 DISYEQLKDLKTYQivgnKIVEYPAHNNVEPPEQRLFPTLQDFFERVNlSTGFDIEIKWPQqradglfeseqtldkNLFA 505
Cdd:cd08612  90 DLNYADLPPYLEKL----EVTFSPGDYCVPKGSDRRIPLLEEVFEAFP-DTPINIDIKVEN---------------DELI 149

                       170       180
                ....*....|....*....|....*....
gi 19922666 506 DRILAVVRRHGCGRLNVIKSFDADLCSLL 534
Cdd:cd08612 150 KKVSDLVRKYKREDITVWGSFNDEIVKKC 178
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 347-542 1.77e-04

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: 44.30  E-value: 1.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvttNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIrvcidsktptskDDLTEVLLK- 425
Cdd:cd08600   4 IAHRG---------ASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYL------------DNVTNVAEKf 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 426 -------------DISYEQLKDLKT---YQIVGNKIVE-YPahnNVEPPEQRLF--PTLQ---DFFERVNLSTGFDI--- 480
Cdd:cd08600  63 pdrkrkdgryyviDFTLDELKSLSVterFDIENGKKVQvYP---NRFPLWKSDFkiHTLEeeiELIQGLNKSTGKNVgiy 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922666 481 -EIKWPQqradglFESEQtlDKNLfADRILAVVRRHGCGRLN---VIKSFDADlcSLLRFKQHMYP 542
Cdd:cd08600 140 pEIKAPW------FHHQE--GKDI-AAATLEVLKKYGYTSKNdkvYLQTFDPN--ELKRIKNELLP 194
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 347-401 2.84e-04

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 43.00  E-value: 2.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19922666  347 IGHRGLGKsltvttnAAPliENTVATMLASSELGADLVEFDVQLTSDLVPIIHHD 401
Cdd:PRK09454  11 VAHRGGGK-------LAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHD 56
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 347-480 8.42e-04

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: 41.83  E-value: 8.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvttnaAPLI--ENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDfsirvCIDSKTPTSKDDLTEVLL 424
Cdd:cd08609  30 VGHRG-----------APMLapENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHD-----EGLLRTTNVKDVFPGRDA 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922666 425 KDISYEQLKDLKTYQiVGNKIVE---YPAHNNVEPPEQR-----LFPTLQDFFERV---NLSTGFDI 480
Cdd:cd08609  94 AGSNNFTWTELKTLN-AGSWFLErrpFWTLSSLSEEDRReadnqTVPSLSELLDLAkkhNVSIMFDL 159
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 74-135 9.51e-04

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: 38.99  E-value: 9.51e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922666  74 LVGNLPVLGAWQAGRAVLLNRTaILNVWSASVEIPQNSSVEYRYFaaaVGQSGAVQIRRWES 135
Cdd:cd05817  18 ISGNCNQLGNWNPSKAKRMQWN-EGDLWTVDVGIPESVYIEYKYF---VSNYDDPNTVLWES 75
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 347-446 1.06e-03

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: 40.50  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666 347 IGHRGlgksltvttNAAPLIENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDF-SIRVCIDSKTPTSKDDLTEV--- 422
Cdd:cd08555   2 LSHRG---------YSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPtLDRTTAGILPPTLEEVLELIady 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19922666 423 -------------------LLKDISYEQLKDLKTYQIVG--NKIV 446
Cdd:cd08555  73 lknpdytiilsleikqdspEYDEFLAKVLKELRVYFDYDlrGKVV 117
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 347-405 1.86e-03

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: 40.75  E-value: 1.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922666 347 IGHRGlgksltvttnaAPLI--ENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIR 405
Cdd:cd08574   5 IGHRG-----------APMLapENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLR 54
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 345-544 1.99e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 40.81  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666  345 LEIGHRGLgksltvttnAAPLIENTV-ATMLASSeLGADLVEFDVQLTSDLVPIIHHDFSIrvcidsktptskDDLTEVL 423
Cdd:PRK11143  28 IVIAHRGA---------SGYLPEHTLpAKAMAYA-QGADYLEQDLVMTKDDQLVVLHDHYL------------DRVTDVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922666  424 LK--------------DISYEQLKDLKT---YQIV-GNKIVEYPAHNNVEPPEQRLfPTLQD---FFERVNLSTGFDI-- 480
Cdd:PRK11143  86 ERfpdrarkdgryyaiDFTLDEIKSLKFtegFDIEnGKKVQVYPGRFPMGKSDFRV-HTFEEeieFIQGLNHSTGKNIgi 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922666  481 --EIKWPQqradglFESEQTLDknlFADRILAVVRRHGCG--RLNV-IKSFDADlcSLLRFKQHMYPVL 544
Cdd:PRK11143 165 ypEIKAPW------FHHQEGKD---IAAKVLEVLKKYGYTgkDDKVyLQCFDAN--ELKRIKNELEPKM 222
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 347-405 2.51e-03

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: 40.63  E-value: 2.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922666 347 IGHRGlgksltvttnaAPLI--ENTVATMLASSELGADLVEFDVQLTSDLVPIIHHDFSIR 405
Cdd:cd08610  26 IGHRG-----------APMLapENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLK 75
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 73-136 7.82e-03

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


Pssm-ID: 99890  Cd Length: 99  Bit Score: 36.54  E-value: 7.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922666  73 ALVGNLPVLGAWQAGRAVLLNRTAiLNVWSASVEIPQNS-SVEYRYFAAAVGQSGAvqirRWESH 136
Cdd:cd05816  18 YVTGSSPELGNWDPQKALKLSDVG-FPIWEADIDISKDSfPFEYKYIIANKDSGVV----SWENG 77
 
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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