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Conserved domains on  [gi|374634320|gb|AEZ54393|]
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AvrBs2 type three effector [Xanthomonas axonopodis pv. begoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AvrBs2 NF041304
type III secretion system effector avirulence protein AvrBs2;
1-714 0e+00

type III secretion system effector avirulence protein AvrBs2;


:

Pssm-ID: 469201  Cd Length: 716  Bit Score: 1348.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320   1 MRIGPLQPSVAHTAAPALPTHTSAISPTQVPHMPGNTPPLRERPRRRAGNMPPLVPLNGSAMTGRPALVALDSEFSEQRL 80
Cdd:NF041304   1 MRIAPLQPAATHTAAPATPTHTSASTPTQVPHAPGSNPPLRPRPRRRAAGAPPLVPLPDSAMTGKPALVALDGEFSEQRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  81 AEVQARQITVQTLQTKLATHLAQAGTAPKPDSIAARFAAGTLEPVYLDTAAFNAMSRGLPARARAAAGPVLIDAQQGRII 160
Cdd:NF041304  81 AEVQARQITVQALQSKLATHLAQAGTALKPDSIAARFAAGTLQPVYLDTAAFRAMARSLPGRARAAAGPVLVDAQQGRII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 161 FNLQRAFAPGDTFSDAALAALGKQLNLSGHGLATPNWLQPAAGTPGRRKLQQAARYHGHEVPARDGGAGFFKANDHRLLE 240
Cdd:NF041304 161 FDLQRAFAPGDTFSDAALAALGKALDLPGQGLANPDWLQPAQSRPPRRKLQQAPRYHGHEIPAQDGGAGFFKANDHRLLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 241 GKQALLRNHRKSLVHDHYFEAPSTRAFGKDVMVHRGLFDNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:NF041304 241 GKQALLREHRKELVHENYFQAPSTRALGKDVMVHRGLFDFHAGIPENSLAAIDRAYAQGYRTLELDVEVSADGVPVLMHD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 321 FSIGRMAGDPQNRLVSQVPFAELREMPLVIRNPSDGNYVKTDQTIAGVEQMLEHVLKKPEPMSVALDCKENTGEAVAMLL 400
Cdd:NF041304 321 FTIGRTLDDPQNRLVAQVPFAELRDQPLVIRNPVDGNFVKTDQRIASIEQMLEHVLQTKPGMSVVLDCKENTAEDVALLL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 401 MRRPDLRKAAAIKVYAKYYTGGFDQFLSNLYKHYQINPLHSQDAPRRAALDRLLAKINVVPVLSQGMLNDERLRGFFRSN 480
Cdd:NF041304 401 MRRPQLRPIAAIKVYSKAYKGGFDQFFSNLCKHLQINPLHSQDEPRRAKLRRDLSKINVVPVLSQGMIEDPQLRDFFPGK 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 481 EQGAAGLADTAMQWLDSWTKMRPVIVEAVATD-DSDAGKAMEIARTRMRQPDSAYAKAAYSVSYRYEDFSVPRANHDKDY 559
Cdd:NF041304 481 DDGAEGLADTATQWMQSWNGMHPVIAEAMVTDpDSDAGKAMQLARARLRQPGSGYEKAAFSAAYRYEDFSLPRSDGDRDY 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 560 YVYRNFGELQKLTNEDFGVKRTTAGAFRDDGESLLTDQPEAELLAILENRTLARGHTGNELDVPPETPIDINRDAEIVKQ 639
Cdd:NF041304 561 FTWGNFGEINPVPESGFEPKRGTAGAFRDQGESVLTDQPDEEVLALRENRTLPRGHTGMELDVPPDTPIDTNRDAEIVQL 640

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374634320 640 RTQQFQASSIPADPNHIAAVREGKQHDRTVDLINDPAAARALDKRAEALGLLTDKYRGAPVTHYLNEQAKQTETD 714
Cdd:NF041304 641 RRQEFMAAKQPLDPVHVAAVREGARLDRGASLQLDPAARRAIDKRAESLGLLTDRYRGAPVSHYLNEQAKQTEPE 715
 
Name Accession Description Interval E-value
AvrBs2 NF041304
type III secretion system effector avirulence protein AvrBs2;
1-714 0e+00

type III secretion system effector avirulence protein AvrBs2;


Pssm-ID: 469201  Cd Length: 716  Bit Score: 1348.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320   1 MRIGPLQPSVAHTAAPALPTHTSAISPTQVPHMPGNTPPLRERPRRRAGNMPPLVPLNGSAMTGRPALVALDSEFSEQRL 80
Cdd:NF041304   1 MRIAPLQPAATHTAAPATPTHTSASTPTQVPHAPGSNPPLRPRPRRRAAGAPPLVPLPDSAMTGKPALVALDGEFSEQRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  81 AEVQARQITVQTLQTKLATHLAQAGTAPKPDSIAARFAAGTLEPVYLDTAAFNAMSRGLPARARAAAGPVLIDAQQGRII 160
Cdd:NF041304  81 AEVQARQITVQALQSKLATHLAQAGTALKPDSIAARFAAGTLQPVYLDTAAFRAMARSLPGRARAAAGPVLVDAQQGRII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 161 FNLQRAFAPGDTFSDAALAALGKQLNLSGHGLATPNWLQPAAGTPGRRKLQQAARYHGHEVPARDGGAGFFKANDHRLLE 240
Cdd:NF041304 161 FDLQRAFAPGDTFSDAALAALGKALDLPGQGLANPDWLQPAQSRPPRRKLQQAPRYHGHEIPAQDGGAGFFKANDHRLLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 241 GKQALLRNHRKSLVHDHYFEAPSTRAFGKDVMVHRGLFDNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:NF041304 241 GKQALLREHRKELVHENYFQAPSTRALGKDVMVHRGLFDFHAGIPENSLAAIDRAYAQGYRTLELDVEVSADGVPVLMHD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 321 FSIGRMAGDPQNRLVSQVPFAELREMPLVIRNPSDGNYVKTDQTIAGVEQMLEHVLKKPEPMSVALDCKENTGEAVAMLL 400
Cdd:NF041304 321 FTIGRTLDDPQNRLVAQVPFAELRDQPLVIRNPVDGNFVKTDQRIASIEQMLEHVLQTKPGMSVVLDCKENTAEDVALLL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 401 MRRPDLRKAAAIKVYAKYYTGGFDQFLSNLYKHYQINPLHSQDAPRRAALDRLLAKINVVPVLSQGMLNDERLRGFFRSN 480
Cdd:NF041304 401 MRRPQLRPIAAIKVYSKAYKGGFDQFFSNLCKHLQINPLHSQDEPRRAKLRRDLSKINVVPVLSQGMIEDPQLRDFFPGK 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 481 EQGAAGLADTAMQWLDSWTKMRPVIVEAVATD-DSDAGKAMEIARTRMRQPDSAYAKAAYSVSYRYEDFSVPRANHDKDY 559
Cdd:NF041304 481 DDGAEGLADTATQWMQSWNGMHPVIAEAMVTDpDSDAGKAMQLARARLRQPGSGYEKAAFSAAYRYEDFSLPRSDGDRDY 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 560 YVYRNFGELQKLTNEDFGVKRTTAGAFRDDGESLLTDQPEAELLAILENRTLARGHTGNELDVPPETPIDINRDAEIVKQ 639
Cdd:NF041304 561 FTWGNFGEINPVPESGFEPKRGTAGAFRDQGESVLTDQPDEEVLALRENRTLPRGHTGMELDVPPDTPIDTNRDAEIVQL 640

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374634320 640 RTQQFQASSIPADPNHIAAVREGKQHDRTVDLINDPAAARALDKRAEALGLLTDKYRGAPVTHYLNEQAKQTETD 714
Cdd:NF041304 641 RRQEFMAAKQPLDPVHVAAVREGARLDRGASLQLDPAARRAIDKRAESLGLLTDRYRGAPVSHYLNEQAKQTEPE 715
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 274-516 4.36e-45

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: 161.41  E-value: 4.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  274 HRGLFDNHagiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQnrLVSQVPFAELREMPL--VIR 351
Cdd:pfam03009   1 HRGASGSY---PENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG--YVRDLTLEELKRLDIgaGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  352 NPSDGNYVKT---DQTIAGVEQMLEHVLKKPEPMSVALDCKEntGEAVAMLLMRRPDLR--KAAAIKVYAKYYTGGFDQF 426
Cdd:pfam03009  76 GPLSGERVPFptlEEVLEFDWDVGFNIEIKIKPYVEAIAPEE--GLIVKDLLLSVDEILakKADPRRVIFSSFNPDELKR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  427 LSNLYKHYQINPLHSQDAPRRAALD-RLLAKINVVPVLSQGMLNDERLRGFF-RSNEQGAAGLADTAMQWlDSWTKMRPV 504
Cdd:pfam03009 154 LRELAPKLPLVFLSSGRAYAEADLLeRAAAFAGAPALLGEVALVDEALPDLVkRAHARGLVVHVWTVNNE-DEMKRLLEL 232

                         250
                  ....*....|..
gi 374634320  505 IVEAVATDDSDA 516
Cdd:pfam03009 233 GVDGVITDRPDT 244
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 271-514 1.02e-30

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: 120.87  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 271 VMVHRGlfDNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQNrlVSQVPFAELREMPLVi 350
Cdd:cd08566    2 VVAHRG--GWGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGK--VSDLTLAEIRKLRLK- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 351 rnpsDGNYVKTDQTIAGVEQMLEHVLKKpepMSVALDCKENTGEAVAMLLMRRPDLRKaAAIKVYAKYYTGGFDQfLSNL 430
Cdd:cd08566   77 ----DGDGEVTDEKVPTLEEALAWAKGK---ILLNLDLKDADLDEVIALVKKHGALDQ-VIFKSYSEEQAKELRA-LAPE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 431 YKHYQINPLHSQDAprrAALDRLLAKINVVP-VLSQGMLNDERLRGFFRSNE-----------QGAAGLADTAMQWLDSW 498
Cdd:cd08566  148 VMLMPIVRDAEDLD---EEEARAIDALNLLAfEITFDDLDLPPLFDELLRALgirvwvntlgdDDTAGLDRALSDPREVW 224

                        250
                 ....*....|....*.
gi 374634320 499 TKMRPVIVEAVATDDS 514
Cdd:cd08566  225 GELVDAGVDVIQTDRP 240
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
274-398 8.01e-18

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 83.38  E-value: 8.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLfdnHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAELREmplvIRNP 353
Cdd:COG0584    8 HRGA---SGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTN--GTGRVADLTLAELRQ----LDAG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 374634320 354 SDGNYvkTDQTIAGVEQMLEHVlkkPEPMSVALDCKENTGEAVAM 398
Cdd:COG0584   79 SGPDF--AGERIPTLEEVLELV---PGDVGLNIEIKSPPAAEPDL 118
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 271-320 3.90e-08

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 54.95  E-value: 3.90e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 374634320 271 VMVHRGlfdnhAG--IPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:PRK09454  10 IVAHRG-----GGklAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHD 56
 
Name Accession Description Interval E-value
AvrBs2 NF041304
type III secretion system effector avirulence protein AvrBs2;
1-714 0e+00

type III secretion system effector avirulence protein AvrBs2;


Pssm-ID: 469201  Cd Length: 716  Bit Score: 1348.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320   1 MRIGPLQPSVAHTAAPALPTHTSAISPTQVPHMPGNTPPLRERPRRRAGNMPPLVPLNGSAMTGRPALVALDSEFSEQRL 80
Cdd:NF041304   1 MRIAPLQPAATHTAAPATPTHTSASTPTQVPHAPGSNPPLRPRPRRRAAGAPPLVPLPDSAMTGKPALVALDGEFSEQRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  81 AEVQARQITVQTLQTKLATHLAQAGTAPKPDSIAARFAAGTLEPVYLDTAAFNAMSRGLPARARAAAGPVLIDAQQGRII 160
Cdd:NF041304  81 AEVQARQITVQALQSKLATHLAQAGTALKPDSIAARFAAGTLQPVYLDTAAFRAMARSLPGRARAAAGPVLVDAQQGRII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 161 FNLQRAFAPGDTFSDAALAALGKQLNLSGHGLATPNWLQPAAGTPGRRKLQQAARYHGHEVPARDGGAGFFKANDHRLLE 240
Cdd:NF041304 161 FDLQRAFAPGDTFSDAALAALGKALDLPGQGLANPDWLQPAQSRPPRRKLQQAPRYHGHEIPAQDGGAGFFKANDHRLLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 241 GKQALLRNHRKSLVHDHYFEAPSTRAFGKDVMVHRGLFDNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:NF041304 241 GKQALLREHRKELVHENYFQAPSTRALGKDVMVHRGLFDFHAGIPENSLAAIDRAYAQGYRTLELDVEVSADGVPVLMHD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 321 FSIGRMAGDPQNRLVSQVPFAELREMPLVIRNPSDGNYVKTDQTIAGVEQMLEHVLKKPEPMSVALDCKENTGEAVAMLL 400
Cdd:NF041304 321 FTIGRTLDDPQNRLVAQVPFAELRDQPLVIRNPVDGNFVKTDQRIASIEQMLEHVLQTKPGMSVVLDCKENTAEDVALLL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 401 MRRPDLRKAAAIKVYAKYYTGGFDQFLSNLYKHYQINPLHSQDAPRRAALDRLLAKINVVPVLSQGMLNDERLRGFFRSN 480
Cdd:NF041304 401 MRRPQLRPIAAIKVYSKAYKGGFDQFFSNLCKHLQINPLHSQDEPRRAKLRRDLSKINVVPVLSQGMIEDPQLRDFFPGK 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 481 EQGAAGLADTAMQWLDSWTKMRPVIVEAVATD-DSDAGKAMEIARTRMRQPDSAYAKAAYSVSYRYEDFSVPRANHDKDY 559
Cdd:NF041304 481 DDGAEGLADTATQWMQSWNGMHPVIAEAMVTDpDSDAGKAMQLARARLRQPGSGYEKAAFSAAYRYEDFSLPRSDGDRDY 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 560 YVYRNFGELQKLTNEDFGVKRTTAGAFRDDGESLLTDQPEAELLAILENRTLARGHTGNELDVPPETPIDINRDAEIVKQ 639
Cdd:NF041304 561 FTWGNFGEINPVPESGFEPKRGTAGAFRDQGESVLTDQPDEEVLALRENRTLPRGHTGMELDVPPDTPIDTNRDAEIVQL 640

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374634320 640 RTQQFQASSIPADPNHIAAVREGKQHDRTVDLINDPAAARALDKRAEALGLLTDKYRGAPVTHYLNEQAKQTETD 714
Cdd:NF041304 641 RRQEFMAAKQPLDPVHVAAVREGARLDRGASLQLDPAARRAIDKRAESLGLLTDRYRGAPVSHYLNEQAKQTEPE 715
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 274-516 4.36e-45

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: 161.41  E-value: 4.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  274 HRGLFDNHagiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQnrLVSQVPFAELREMPL--VIR 351
Cdd:pfam03009   1 HRGASGSY---PENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG--YVRDLTLEELKRLDIgaGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  352 NPSDGNYVKT---DQTIAGVEQMLEHVLKKPEPMSVALDCKEntGEAVAMLLMRRPDLR--KAAAIKVYAKYYTGGFDQF 426
Cdd:pfam03009  76 GPLSGERVPFptlEEVLEFDWDVGFNIEIKIKPYVEAIAPEE--GLIVKDLLLSVDEILakKADPRRVIFSSFNPDELKR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320  427 LSNLYKHYQINPLHSQDAPRRAALD-RLLAKINVVPVLSQGMLNDERLRGFF-RSNEQGAAGLADTAMQWlDSWTKMRPV 504
Cdd:pfam03009 154 LRELAPKLPLVFLSSGRAYAEADLLeRAAAFAGAPALLGEVALVDEALPDLVkRAHARGLVVHVWTVNNE-DEMKRLLEL 232

                         250
                  ....*....|..
gi 374634320  505 IVEAVATDDSDA 516
Cdd:pfam03009 233 GVDGVITDRPDT 244
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 271-514 1.02e-30

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: 120.87  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 271 VMVHRGlfDNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQNrlVSQVPFAELREMPLVi 350
Cdd:cd08566    2 VVAHRG--GWGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGK--VSDLTLAEIRKLRLK- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 351 rnpsDGNYVKTDQTIAGVEQMLEHVLKKpepMSVALDCKENTGEAVAMLLMRRPDLRKaAAIKVYAKYYTGGFDQfLSNL 430
Cdd:cd08566   77 ----DGDGEVTDEKVPTLEEALAWAKGK---ILLNLDLKDADLDEVIALVKKHGALDQ-VIFKSYSEEQAKELRA-LAPE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 431 YKHYQINPLHSQDAprrAALDRLLAKINVVP-VLSQGMLNDERLRGFFRSNE-----------QGAAGLADTAMQWLDSW 498
Cdd:cd08566  148 VMLMPIVRDAEDLD---EEEARAIDALNLLAfEITFDDLDLPPLFDELLRALgirvwvntlgdDDTAGLDRALSDPREVW 224

                        250
                 ....*....|....*.
gi 374634320 499 TKMRPVIVEAVATDDS 514
Cdd:cd08566  225 GELVDAGVDVIQTDRP 240
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
274-398 8.01e-18

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 83.38  E-value: 8.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLfdnHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAELREmplvIRNP 353
Cdd:COG0584    8 HRGA---SGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTN--GTGRVADLTLAELRQ----LDAG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 374634320 354 SDGNYvkTDQTIAGVEQMLEHVlkkPEPMSVALDCKENTGEAVAM 398
Cdd:COG0584   79 SGPDF--AGERIPTLEEVLELV---PGDVGLNIEIKSPPAAEPDL 118
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 274-412 2.40e-15

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: 76.21  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLFDNHAGIPENSLASIDHAYEQGYrNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAELREMPLvirnp 353
Cdd:cd08585    9 HRGLHDRDAGIPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTG--VEGRVEELTAAELRALRL----- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 354 sdgnyVKTDQTIAGVEQMLEhVLKKPEPMSVALD-CKENTGEAVAMLLMRRPDLRKAAAI 412
Cdd:cd08585   81 -----LGTDEHIPTLDEVLE-LVAGRVPLLIELKsCGGGDGGLERRVLAALKDYKGPAAI 134
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 274-400 1.17e-13

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function is not elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4.


Pssm-ID: 176517 [Multi-domain]  Cd Length: 264  Bit Score: 71.48  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLfdnHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAELREMPL---VI 350
Cdd:cd08575    6 HRGG---AAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTG--GSGLVSDLTYAELPPLDAgygYT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 374634320 351 RNPSDGNYVKTDqtiaGVEQM--LEHVLKKPEPMSVALDCK-ENTGEAVAMLL 400
Cdd:cd08575   81 FDGGKTGYPRGG----GDGRIptLEEVFKAFPDTPINIDIKsPDAEELIAAVL 129
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 274-412 5.33e-13

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: 69.59  E-value: 5.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGlfdNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPqnRLVSQVPFAELREMPLVIRNP 353
Cdd:cd08573    4 HRG---AGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGT--GLVAELTWEELRKLNAAAKHR 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374634320 354 SDGNY--VKTDQTIAGVEQMLEHVLKkpepmsVALDCKENTGEAVAM---LLMRRPDLRKAAAI 412
Cdd:cd08573   79 LSSRFpgEKIPTLEEAVKECLENNLR------MIFDVKSNSSKLVDAlknLFKKYPGLYDKAIV 136
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 274-400 1.13e-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: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 65.03  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGlFDNHAgiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDpqNRLVSQVPFAELREMPLVIRNp 353
Cdd:cd08582    4 HRG-ASAEA--PENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG--DGAVSDLTLAELRKLDIGSWK- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 374634320 354 sdgNYVKTDQTIAGVEQMLEHVLKKPEPMSVALDCKENTGEAVAMLL 400
Cdd:cd08582   78 ---GESYKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEEELL 121
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 271-374 6.05e-11

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: 63.43  E-value: 6.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 271 VMVHRGLfdnhAGI-PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPqnRLVSQVPFAELREMPLV 349
Cdd:cd08561    1 VIAHRGG----AGLaPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGT--GPVADLTLAELRRLDAG 74

                         90       100
                 ....*....|....*....|....*....
gi 374634320 350 IRNPSDGN----YVKTDQTIAGVEQMLEH 374
Cdd:cd08561   75 YHFTDDGGrtypYRGQGIRIPTLEELFEA 103
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 274-378 1.02e-10

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: 62.19  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLFDNHagiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDpqNRLVSQVPFAELREmpLVIRNP 353
Cdd:cd08563    6 HRGYSGTA---PENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNG--KGYVKDLTLEELKK--LDAGSW 78

                         90       100
                 ....*....|....*....|....*
gi 374634320 354 SDGNYvkTDQTIAGVEQMLEHVLKK 378
Cdd:cd08563   79 FDEKF--TGEKIPTLEEVLDLLKDK 101
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 274-343 1.79e-10

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: 61.58  E-value: 1.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGlfdNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAEL 343
Cdd:cd08581    4 HRG---YPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTG--VEGLLHELEDAEL 68
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 274-320 1.92e-10

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: 60.74  E-value: 1.92e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 374634320 274 HRGlFDNHAgiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:cd08556    4 HRG-ASGEA--PENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD 47
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 271-325 2.16e-10

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: 61.47  E-value: 2.16e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 374634320 271 VMVHRGLfdnhAGI-PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGR 325
Cdd:cd08562    1 IIAHRGA----SSLaPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDR 52
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 271-348 3.44e-10

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: 60.64  E-value: 3.44e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374634320 271 VMVHRGlfDNHAGiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAELREMPL 348
Cdd:cd08579    1 IIAHRG--VSSNG-VENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAG--VNKKVWDLTLEELKKLTI 73
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 274-436 5.64e-10

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: 61.08  E-value: 5.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGlfdnHAGI-PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGdpQNRLVSQVPFAELremPLVIRN 352
Cdd:cd08612   32 HRG----GSGEnLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCG--VDKLVSDLNYADL---PPYLEK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 353 ------PSDGNYVK-TDQTIAgveqMLEHVLKK-PE-PMSValDCKENTGEAVAM------------------------- 398
Cdd:cd08612  103 levtfsPGDYCVPKgSDRRIP----LLEEVFEAfPDtPINI--DIKVENDELIKKvsdlvrkykreditvwgsfndeivk 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 374634320 399 -LLMRRPDLR----KAAAIKVYAKYYTgGFDQFLSNLYKHYQI 436
Cdd:cd08612  177 kCHKENPNIPlffsLKRVLLLLLLYYT-GLLPFIPIKESFLEI 218
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 271-356 1.19e-09

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: 59.73  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 271 VMVHRGLFDN--------HAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMH-DFSIGRMAGDPQNRLVSQVPFA 341
Cdd:cd08605    2 VIGHRGLGMNrashqpsvGPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHdDFIVVERGGEVESSRIRDLTLA 81

                         90
                 ....*....|....*
gi 374634320 342 ELREMPLVIRNPSDG 356
Cdd:cd08605   82 ELKALGPQAESTKTS 96
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 274-389 2.66e-09

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase.


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 58.00  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLfdnHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQNrlvsqvpfaelremplvIRNP 353
Cdd:cd08570    4 HRGY---KAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGL-----------------IIDD 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 374634320 354 SDGNYVKTDQTI-AGVEQMLE-----HVLKKPEP--MSVALDCK 389
Cdd:cd08570   64 STWDELSHLRTIeEPHQPMPTlkdvlEWLVEHELpdVKLMLDIK 107
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 274-346 4.84e-09

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: 58.06  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 274 HRGLFDNH-----AGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSI--------GRMAGDPQNRLVSQVPF 340
Cdd:cd08572    5 HRGLGKNYasgslAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvseksktGSDEGELIEVPIHDLTL 84


                 ....*.
gi 374634320 341 AELREM 346
Cdd:cd08572   85 EQLKEL 90
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 271-320 3.90e-08

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 54.95  E-value: 3.90e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 374634320 271 VMVHRGlfdnhAG--IPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:PRK09454  10 IVAHRG-----GGklAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHD 56
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 285-325 1.00e-07

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


Pssm-ID: 176516 [Multi-domain]  Cd Length: 252  Bit Score: 53.85  E-value: 1.00e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 374634320 285 PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGR 325
Cdd:cd08574   15 PENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRR 55
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 274-348 5.34e-07

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: 51.91  E-value: 5.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374634320 274 HRGL----FDNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIgRMAgdPQNRLVSQvPFaELREMPL 348
Cdd:cd08607    5 HRGAgnsyTAASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTL-RVS--LKSKGDSD-RD-DLLEVPV 78
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 285-325 1.15e-06

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: 51.03  E-value: 1.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 374634320 285 PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGR 325
Cdd:cd08610   36 PENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKR 76
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 270-320 4.49e-06

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: 48.85  E-value: 4.49e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 374634320 270 DVMVHRGLfdnHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:cd08567    2 DLQGHRGA---RGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHD 49
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 271-389 5.65e-06

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: 48.60  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 271 VMVHRGLFDNHAG-----IPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQNRLVSQVPFAELRE 345
Cdd:cd08606    4 VIGHRGLGKNTAErkslqLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETGTDVPIHDLTLEQFLHLSR 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 374634320 346 MPLVIRNPSDGNYVKT-DQTIAGVEQMLEHVLKK-PEPMSVALDCK 389
Cdd:cd08606   84 MKYTVDFKKKGFKGNSrGHSIQAPFTTLEELLKKlPKSVGFNIELK 129
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 287-391 6.99e-06

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 48.07  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 287 NSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFS------IGRMAGDPQNRLvsqvPFAELREMPLVirnpsdGNYvk 360
Cdd:cd08583   16 NSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWDesllkqLGLPTSKNTKPL----SYEEFKSKKIY------GKY-- 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 374634320 361 tdqTIAGVEQMLEHVLKKPEpMSVALDCKEN 391
Cdd:cd08583   84 ---TPMDFKDVIDLLKKYPD-VYIVTDTKQD 110
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 274-345 7.03e-06

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: 47.68  E-value: 7.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374634320 274 HRGLfdnHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQNrlVSQVPFAELRE 345
Cdd:cd08568    5 HRGY---RAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLK--VKELTYKELKK 71
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 285-325 1.53e-05

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 47.92  E-value: 1.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 374634320 285 PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGR 325
Cdd:cd08608   15 PENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRR 55
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 269-320 2.16e-05

Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), GlpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ, which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein, protein D (HPD), from Haemophilus influenza Type b and nontypeable strains, which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria.


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 47.00  E-value: 2.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 374634320 269 KDVMVHRGlfdNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:cd08600    1 KIIIAHRG---ASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHD 49
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 285-325 2.67e-05

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: 46.84  E-value: 2.67e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 374634320 285 PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGR 325
Cdd:cd08609   40 PENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLR 80
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 271-326 2.78e-05

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: 46.50  E-value: 2.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 374634320 271 VMVHRGlfdNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRM 326
Cdd:cd08559    3 VIAHRG---ASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRT 55
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 271-346 2.69e-04

Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 43.46  E-value: 2.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374634320 271 VMVHRGLfDNHAgiPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQNRLVSQVPFAELREM 346
Cdd:cd08601    3 VIAHRGA-SGYA--PEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPGPVKDYTLAEIKQL 75
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 274-319 2.74e-04

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 43.47  E-value: 2.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 374634320 274 HRGlfdNHAGIPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMH 319
Cdd:cd08580    6 HRG---GTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYR 48
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 285-381 1.10e-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: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374634320 285 PENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHDFSIGRMAGDPQN-------RLVSQVPFAELREMPLVIRNPSDGn 357
Cdd:cd08555   12 QENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILPptleevlELIADYLKNPDYTIILSLEIKQDS- 90

                         90       100
                 ....*....|....*....|....
gi 374634320 358 yvktDQTIAGVEQMLEHVLKKPEP 381
Cdd:cd08555   91 ----PEYDEFLAKVLKELRVYFDY 110
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 261-320 3.43e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 40.43  E-value: 3.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374634320 261 APSTRAFGKDVMVHRGLfdnhAG-IPENSLASIDHAYEQGYRNLELDVEVSADGVPVLMHD 320
Cdd:PRK11143  19 AAAADSAEKIVIAHRGA----SGyLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHD 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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