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Conserved domains on  [gi|2082271904|ref|XP_042914040|]
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uncharacterized protein CHLRE_36g759647v5 [Chlamydomonas reinhardtii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 155-424 7.00e-56

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02605:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 245  Bit Score: 184.86  E-value: 7.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 155 MVVSDLDGTMVGDD---AATGAFKSWWEDAGALAGGVLVYNTGRSLGSFLELLrsKAGCMAVPDALILAVGTCVYlrhps 231
Cdd:cd02605     1 LLVSDLDETLVGHDtnlQALERLQDLLEQLTADNDVILVYATGRSPESVLELI--KEVMLPKPDFIISDVGTEIY----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 232 ggpADAAAGWREDRDWAAQLDASWN--LKVARDACYKALaevgkdamHFRPAEEQNDHKVTCGVADAAAGGVVARVNSEL 309
Cdd:cd02605    74 ---YGESGYLEPDTYWNEVLSEGWErfLFEAIADLFKQL--------KPQSELEQNPHKISFYLDPQNDAAVIEQLEEML 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 310 AAAGVSANVITSgHGGWKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWA 389
Cdd:cd02605   143 LKAGLTVRIIYS-SGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWA 221

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2082271904 390 QQRqaaeaplpsgkHRLLQATKKEALGILEGLEHF 424
Cdd:cd02605   222 DRV-----------TRSRLAKGPYAGGILEGLAHF 245
CBM_21 super family cl23798
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 54-136 9.81e-05

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


The actual alignment was detected with superfamily member smart01066:

Pssm-ID: 474061 [Multi-domain]  Cd Length: 83  Bit Score: 40.80  E-value: 9.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904   54 IKLFYRT-----GWDKAVAHGSLAGAAWTDFPLVKSAGAPNRWLVADIPVGAAPSsngqplLEFVVADAAkQQWDKPQaG 128
Cdd:smart01066   4 VTVYYNGllatsGAKNVYLHYGFGENNWTDVPDVRMEKTGEGWVKATIPVKEAYK------LNFCFKDGA-GNWDNNG-G 75


                   ....*...
gi 2082271904  129 GNYVVDSP 136
Cdd:smart01066  76 ANYHFEIG 83
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 155-424 7.00e-56

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 184.86  E-value: 7.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 155 MVVSDLDGTMVGDD---AATGAFKSWWEDAGALAGGVLVYNTGRSLGSFLELLrsKAGCMAVPDALILAVGTCVYlrhps 231
Cdd:cd02605     1 LLVSDLDETLVGHDtnlQALERLQDLLEQLTADNDVILVYATGRSPESVLELI--KEVMLPKPDFIISDVGTEIY----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 232 ggpADAAAGWREDRDWAAQLDASWN--LKVARDACYKALaevgkdamHFRPAEEQNDHKVTCGVADAAAGGVVARVNSEL 309
Cdd:cd02605    74 ---YGESGYLEPDTYWNEVLSEGWErfLFEAIADLFKQL--------KPQSELEQNPHKISFYLDPQNDAAVIEQLEEML 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 310 AAAGVSANVITSgHGGWKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWA 389
Cdd:cd02605   143 LKAGLTVRIIYS-SGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWA 221

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2082271904 390 QQRqaaeaplpsgkHRLLQATKKEALGILEGLEHF 424
Cdd:cd02605   222 DRV-----------TRSRLAKGPYAGGILEGLAHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 152-426 8.46e-52

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 174.38  E-value: 8.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 152 RPVMVVSDLDGTMV-GDDAATGAFKSWWEDAGALAGgvLVYNTGRSLGSFLELLRSKAgcMAVPDALILAVGTCVYLRHP 230
Cdd:pfam05116   1 PPLLLVSDLDNTLVdGDNEALARLNQLLEAYRPDVG--LVFATGRSLDSAKELLKEKP--LPTPDYLITSVGTEIYYGPS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 231 SggpadaaagwREDRDWAAQLDASWNlkvaRDACYKALAEVGKDAMhfRPAEEQNDHKVTCGVADAAAGGVVARVNSELA 310
Cdd:pfam05116  77 L----------VPDQSWQEHLDYHWD----RQAVVEALAKFPGLTL--QPEEEQRPHKVSYFLDPEAAAAVLAELEQLLR 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 311 AAGVSANVITSGHggwKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWAQ 390
Cdd:pfam05116 141 KRGLDVKVIYSSG---RDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYL 217

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2082271904 391 QrQAAEaplpsgKHRLLQATKKEALGILEGLEHFGF 426
Cdd:pfam05116 218 E-NARD------NPRIYFASGRCAGGILEGIRHFGL 246
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 153-426 1.87e-38

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 139.18  E-value: 1.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 153 PVMVVSDLDGTMV----GDDAATGAFKSWWEDAGAlAGGVLVYNTGRSLGSFLELLRSKAgcMAVPDALILAVGTCVYLr 228
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRG-EDSLLVYSTGRSPHSYKELQKQKP--LLTPDIWVTSVGSEIYY- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 229 hpsgGPADAAagwreDRDWAAQLDASWNlkvaRDAcykALAE-VGKDAMHFRPAEEQNDHKVTCGVADAAAGGVVARVNS 307
Cdd:TIGR01485  77 ----GGAEVP-----DQHWAEYLSEKWQ----RDI---VVAItDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTE 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 308 ELAAAGVSANVITSGHggwKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENL-AIVVGNAQPDLR 386
Cdd:TIGR01485 141 MLKETGLDVKLIYSSG---KDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVrGVIVSNAQEELL 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2082271904 387 TWAQQrqaaeaplpSGKHRLLQATKKEALGILEGLEHFGF 426
Cdd:TIGR01485 218 QWYDE---------NAKDKIYHASERCAGGIIEAIAHFDL 248
PLN02382 PLN02382
probable sucrose-phosphatase
 148-425 7.91e-29

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 117.01  E-value: 7.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 148 RLAARP-VMVVSDLDGTMV--GDDAATG--AFKSWWEDAGAlAGGVLVYNTGRSLGSFLELLRSKAgcMAVPDALILAVG 222
Cdd:PLN02382    3 RLSGSPrLMIVSDLDHTMVdhHDPENLSllRFNALWEAEYR-HDSLLVFSTGRSPTLYKELRKEKP--LLTPDITIMSVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 223 T-CVYlrhpsgGPAdaaagWREDRDWAAQLDASWNlkvaRDACYKALAEVGKdaMHFRPAEEQNDHKVTCGVADAAAGGV 301
Cdd:PLN02382   80 TeIAY------GES-----MVPDHGWVEYLNKKWD----REIVVEETSKFPE--LKLQPETEQRPHKVSFYVDKKKAQEV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 302 VARVNSELAAAGVSANVITSGHggwKYMDVVPIRAGKLEALNHVRRHF---GFSVASTVACGDSGNDILMLSGENL-AIV 377
Cdd:PLN02382  143 IKELSERLEKRGLDVKIIYSGG---IDLDVLPQGAGKGQALAYLLKKLkaeGKAPVNTLVCGDSGNDAELFSVPDVyGVM 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2082271904 378 VGNAQPDLRTWAQQRQaaeaplpSGKHRLLQATKKEALGILEGLEHFG 425
Cdd:PLN02382  220 VSNAQEELLQWYAENA-------KDNPKIIHATERCAAGIIQAIGHFN 260
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 155-424 6.07e-19

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 84.42  E-value: 6.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 155 MVVSDLDGTMVGDDAA-TGAFKSWWEDAGAlAGGVLVYNTGRSLGSFLELLRSkagcMAVPDALILAVGTCVYlrhpsgg 233
Cdd:COG0561     4 LIALDLDGTLLNDDGEiSPRTKEALRRLRE-KGIKVVIATGRPLRSALPLLEE----LGLDDPLITSNGALIY------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 234 padaaagwreDRDWAAQLDASWNLKVARDACykalaevgkdamhfrpaeeqndhkvtcgvadaaaggvvarvnSELAAAG 313
Cdd:COG0561    72 ----------DPDGEVLYERPLDPEDVREIL------------------------------------------ELLREHG 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 314 VSANVITSGHGGWkyMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLrtwaqqRQ 393
Cdd:COG0561   100 LHLQVVVRSGPGF--LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEV------KA 171

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2082271904 394 AAEAPLPSGkhrllqatkkEALGILEGLEHF 424
Cdd:COG0561   172 AADYVTGSN----------DEDGVAEALEKL 192
CBM_25 smart01066
Carbohydrate binding domain;
54-136 9.81e-05

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 40.80  E-value: 9.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904   54 IKLFYRT-----GWDKAVAHGSLAGAAWTDFPLVKSAGAPNRWLVADIPVGAAPSsngqplLEFVVADAAkQQWDKPQaG 128
Cdd:smart01066   4 VTVYYNGllatsGAKNVYLHYGFGENNWTDVPDVRMEKTGEGWVKATIPVKEAYK------LNFCFKDGA-GNWDNNG-G 75


                   ....*...
gi 2082271904  129 GNYVVDSP 136
Cdd:smart01066  76 ANYHFEIG 83
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 155-424 7.00e-56

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 184.86  E-value: 7.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 155 MVVSDLDGTMVGDD---AATGAFKSWWEDAGALAGGVLVYNTGRSLGSFLELLrsKAGCMAVPDALILAVGTCVYlrhps 231
Cdd:cd02605     1 LLVSDLDETLVGHDtnlQALERLQDLLEQLTADNDVILVYATGRSPESVLELI--KEVMLPKPDFIISDVGTEIY----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 232 ggpADAAAGWREDRDWAAQLDASWN--LKVARDACYKALaevgkdamHFRPAEEQNDHKVTCGVADAAAGGVVARVNSEL 309
Cdd:cd02605    74 ---YGESGYLEPDTYWNEVLSEGWErfLFEAIADLFKQL--------KPQSELEQNPHKISFYLDPQNDAAVIEQLEEML 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 310 AAAGVSANVITSgHGGWKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWA 389
Cdd:cd02605   143 LKAGLTVRIIYS-SGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWA 221

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2082271904 390 QQRqaaeaplpsgkHRLLQATKKEALGILEGLEHF 424
Cdd:cd02605   222 DRV-----------TRSRLAKGPYAGGILEGLAHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 152-426 8.46e-52

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 174.38  E-value: 8.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 152 RPVMVVSDLDGTMV-GDDAATGAFKSWWEDAGALAGgvLVYNTGRSLGSFLELLRSKAgcMAVPDALILAVGTCVYLRHP 230
Cdd:pfam05116   1 PPLLLVSDLDNTLVdGDNEALARLNQLLEAYRPDVG--LVFATGRSLDSAKELLKEKP--LPTPDYLITSVGTEIYYGPS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 231 SggpadaaagwREDRDWAAQLDASWNlkvaRDACYKALAEVGKDAMhfRPAEEQNDHKVTCGVADAAAGGVVARVNSELA 310
Cdd:pfam05116  77 L----------VPDQSWQEHLDYHWD----RQAVVEALAKFPGLTL--QPEEEQRPHKVSYFLDPEAAAAVLAELEQLLR 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 311 AAGVSANVITSGHggwKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWAQ 390
Cdd:pfam05116 141 KRGLDVKVIYSSG---RDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYL 217

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2082271904 391 QrQAAEaplpsgKHRLLQATKKEALGILEGLEHFGF 426
Cdd:pfam05116 218 E-NARD------NPRIYFASGRCAGGILEGIRHFGL 246
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 153-426 1.87e-38

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 139.18  E-value: 1.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 153 PVMVVSDLDGTMV----GDDAATGAFKSWWEDAGAlAGGVLVYNTGRSLGSFLELLRSKAgcMAVPDALILAVGTCVYLr 228
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRG-EDSLLVYSTGRSPHSYKELQKQKP--LLTPDIWVTSVGSEIYY- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 229 hpsgGPADAAagwreDRDWAAQLDASWNlkvaRDAcykALAE-VGKDAMHFRPAEEQNDHKVTCGVADAAAGGVVARVNS 307
Cdd:TIGR01485  77 ----GGAEVP-----DQHWAEYLSEKWQ----RDI---VVAItDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTE 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 308 ELAAAGVSANVITSGHggwKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENL-AIVVGNAQPDLR 386
Cdd:TIGR01485 141 MLKETGLDVKLIYSSG---KDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVrGVIVSNAQEELL 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2082271904 387 TWAQQrqaaeaplpSGKHRLLQATKKEALGILEGLEHFGF 426
Cdd:TIGR01485 218 QWYDE---------NAKDKIYHASERCAGGIIEAIAHFDL 248
PLN02382 PLN02382
probable sucrose-phosphatase
 148-425 7.91e-29

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 117.01  E-value: 7.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 148 RLAARP-VMVVSDLDGTMV--GDDAATG--AFKSWWEDAGAlAGGVLVYNTGRSLGSFLELLRSKAgcMAVPDALILAVG 222
Cdd:PLN02382    3 RLSGSPrLMIVSDLDHTMVdhHDPENLSllRFNALWEAEYR-HDSLLVFSTGRSPTLYKELRKEKP--LLTPDITIMSVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 223 T-CVYlrhpsgGPAdaaagWREDRDWAAQLDASWNlkvaRDACYKALAEVGKdaMHFRPAEEQNDHKVTCGVADAAAGGV 301
Cdd:PLN02382   80 TeIAY------GES-----MVPDHGWVEYLNKKWD----REIVVEETSKFPE--LKLQPETEQRPHKVSFYVDKKKAQEV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 302 VARVNSELAAAGVSANVITSGHggwKYMDVVPIRAGKLEALNHVRRHF---GFSVASTVACGDSGNDILMLSGENL-AIV 377
Cdd:PLN02382  143 IKELSERLEKRGLDVKIIYSGG---IDLDVLPQGAGKGQALAYLLKKLkaeGKAPVNTLVCGDSGNDAELFSVPDVyGVM 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2082271904 378 VGNAQPDLRTWAQQRQaaeaplpSGKHRLLQATKKEALGILEGLEHFG 425
Cdd:PLN02382  220 VSNAQEELLQWYAENA-------KDNPKIIHATERCAAGIIQAIGHFN 260
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 155-424 6.07e-19

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 84.42  E-value: 6.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 155 MVVSDLDGTMVGDDAA-TGAFKSWWEDAGAlAGGVLVYNTGRSLGSFLELLRSkagcMAVPDALILAVGTCVYlrhpsgg 233
Cdd:COG0561     4 LIALDLDGTLLNDDGEiSPRTKEALRRLRE-KGIKVVIATGRPLRSALPLLEE----LGLDDPLITSNGALIY------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 234 padaaagwreDRDWAAQLDASWNLKVARDACykalaevgkdamhfrpaeeqndhkvtcgvadaaaggvvarvnSELAAAG 313
Cdd:COG0561    72 ----------DPDGEVLYERPLDPEDVREIL------------------------------------------ELLREHG 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 314 VSANVITSGHGGWkyMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLrtwaqqRQ 393
Cdd:COG0561   100 LHLQVVVRSGPGF--LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEV------KA 171

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2082271904 394 AAEAPLPSGkhrllqatkkEALGILEGLEHF 424
Cdd:COG0561   172 AADYVTGSN----------DEDGVAEALEKL 192
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 156-391 1.87e-16

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 77.89  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 156 VVSDLDGTMVGDDAAtgaFKSWWEDAGALAGGV---LVYNTGRSLgSFLELLRSKAGcmaVPDALILAVGTCVYlrHPSG 232
Cdd:TIGR01482   1 IASDIDGTLTDPNRA---INESALEAIRKAESKgipVVLVTGNSV-QFARALAKLIG---TPDPVIAENGGEIS--YNEG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 233 GpadaaagwreDRDWAAQLDASWNLkvaRDACYKAlaeVGKDAMHFRPAEEQNDHKVtcgvadaAAGGVVARVNSELAAA 312
Cdd:TIGR01482  72 L----------DDIFLAYLEEEWFL---DIVIAKT---FPFSRLKVQYPRRASLVKM-------RYGIDVDTVREIIKEL 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082271904 313 GVSANVITSGhggwKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWAQQ 391
Cdd:TIGR01482 129 GLNLVAVDSG----FDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADY 203
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 155-378 1.03e-10

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 60.86  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 155 MVVSDLDGTMVGDDAAT---GAFKSWWEdaGALAGGVLVYNTGRSLGSFLELLRSkagcMAVPDALILAVGTCVYLrhpS 231
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHElspETIEALER--LREAGVKVVIVTGRSLAEIKELLKQ----LNLPLPLIAENGALIFY---P 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 232 GGPAdaaagWREDRDwAAQLDASWNLKVArDACYKALAEVGKDAMHFRPAEEQNDHKVTCGVADAAAGGVVARVNsELAA 311
Cdd:TIGR01484  72 GEIL-----YIEPSD-VFEEILGIKFEEI-GAELKSLSEHYVGTFIEDKAIAVAIHYVGAELGQELDSKMRERLE-KIGR 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2082271904 312 AGVSANVITSGHGGWkymDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVV 378
Cdd:TIGR01484 144 NDLELEAIYSGKTDL---EVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 328-425 6.91e-10

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 58.77  E-value: 6.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 328 YMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWAQqrqaaeaplpsgkhrll 407
Cdd:cd07517   132 STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIAD----------------- 194

                          90
                  ....*....|....*....
gi 2082271904 408 QATKK-EALGILEGLEHFG 425
Cdd:cd07517   195 YVTKDvDEDGILKALKHFG 213
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 316-385 8.78e-10

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 57.59  E-value: 8.78e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 316 ANVITSGHGgwkYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDL 385
Cdd:cd07518    97 LRAVTSGFG---SIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEV 163
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 316-385 6.87e-08

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 53.40  E-value: 6.87e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 316 ANVITSGHGGWKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDL 385
Cdd:pfam08282 166 GSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 317-386 3.73e-07

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 51.06  E-value: 3.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904 317 NVITSGhggWKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLR 386
Cdd:cd07516   166 SVVRSA---PFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVK 232
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 325-389 1.08e-06

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 49.57  E-value: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2082271904 325 GWKYMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWA 389
Cdd:TIGR00099 176 GPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALA 240
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 335-393 4.64e-05

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 44.44  E-value: 4.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2082271904 335 RAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVgNAQPDLRTWAQQRQ 393
Cdd:COG0560   153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAADRER 210
CBM_25 smart01066
Carbohydrate binding domain;
54-136 9.81e-05

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 40.80  E-value: 9.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082271904   54 IKLFYRT-----GWDKAVAHGSLAGAAWTDFPLVKSAGAPNRWLVADIPVGAAPSsngqplLEFVVADAAkQQWDKPQaG 128
Cdd:smart01066   4 VTVYYNGllatsGAKNVYLHYGFGENNWTDVPDVRMEKTGEGWVKATIPVKEAYK------LNFCFKDGA-GNWDNNG-G 75


                   ....*...
gi 2082271904  129 GNYVVDSP 136
Cdd:smart01066  76 ANYHFEIG 83
PRK15126 PRK15126
HMP-PP phosphatase;
329-386 7.24e-04

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 41.22  E-value: 7.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2082271904 329 MDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLR 386
Cdd:PRK15126  180 LEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLR 237
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 328-390 1.31e-03

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 40.45  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2082271904 328 YMDVVPIRAGKLEALNHVRRHFGFSVASTVACGDSGNDILMLSGENLAIVVGNAQPDLRTWAQ 390
Cdd:PRK10513  187 FLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQ 249
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 335-369 3.01e-03

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 3.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2082271904 335 RAGKLEALNHVRRHFGFSVASTVACGDSGNDILML 369
Cdd:cd07500   135 AQRKAETLQELAARLGIPLEQTVAVGDGANDLPML 169
 
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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