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Conserved domains on  [gi|71896857|ref|NP_001025939|]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
4-255 1.95e-138

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


The actual alignment was detected with superfamily member PRK14115:

Pssm-ID: 416258  Cd Length: 247  Bit Score: 388.83  E-value: 1.95e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    4 YKLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQS 83
Cdd:PRK14115   1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQMWLPVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   84 SWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEeiYNDRRYKccDVSQDNLPKAESLKDVLD 163
Cdd:PRK14115  81 SWRLNERHYGALQGLNKAETAAKYGDEQVKIWRRSYDVPPPALEKDDERYP--GHDPRYA--KLPEEELPLTESLKDTIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  164 RLLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGpHQFLGDQEAIQA 243
Cdd:PRK14115 157 RVLPYWNETIAPQLKSGKRVLIAAHGNSLRALVKYLDNISDEEILELNIPTGVPLVYELDENLKPIK-HYYLGDADEIAA 235
                        250
                 ....*....|..
gi 71896857  244 AIKKVEDQGKVK 255
Cdd:PRK14115 236 AAAAVANQGKAK 247
 
Name Accession Description Interval E-value
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-255 1.95e-138

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 388.83  E-value: 1.95e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    4 YKLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQS 83
Cdd:PRK14115   1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQMWLPVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   84 SWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEeiYNDRRYKccDVSQDNLPKAESLKDVLD 163
Cdd:PRK14115  81 SWRLNERHYGALQGLNKAETAAKYGDEQVKIWRRSYDVPPPALEKDDERYP--GHDPRYA--KLPEEELPLTESLKDTIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  164 RLLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGpHQFLGDQEAIQA 243
Cdd:PRK14115 157 RVLPYWNETIAPQLKSGKRVLIAAHGNSLRALVKYLDNISDEEILELNIPTGVPLVYELDENLKPIK-HYYLGDADEIAA 235
                        250
                 ....*....|..
gi 71896857  244 AIKKVEDQGKVK 255
Cdd:PRK14115 236 AAAAVANQGKAK 247
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
5-253 8.13e-132

phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are phosphoglycerate mutase (EC 5.4.2.1). This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate. The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have are phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (EC 5.4.2.4). This model is designated as a subfamily for this reason. The second and third paralogs in S. cerevisiae are somewhat divergent and apparently inactive (see PUBMED:9544241) but are also part of this subfamily phylogenetically.


Pssm-ID: 213596  Cd Length: 245  Bit Score: 372.13  E-value: 8.13e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857     5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:TIGR01258   2 KLVLVRHGESEWNALNLFTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDELDQLWIPVKKS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYKccDVSQDNLPKAESLKDVLDR 164
Cdd:TIGR01258  82 WRLNERHYGALQGLNKAETAAKYGEEQVNIWRRSFDVPPPPIDESDPRSPH--NDPRYA--HLDPKVLPLTESLKDTIAR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGPHqFLGDQEAIQAA 244
Cdd:TIGR01258 158 VLPYWNDEIAPDLLSGKRVLIVAHGNSLRALVKHLEGISDEEILELNIPTGIPLVYELDENLKPIKHY-YLGDPEAAAAA 236

                  ....*....
gi 71896857   245 IKKVEDQGK 253
Cdd:TIGR01258 237 AEAVANQGK 245
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];
5-237 1.08e-118

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];


Pssm-ID: 223661  Cd Length: 230  Bit Score: 338.48  E-value: 1.08e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:COG0588   3 KLVLLRHGQSEWNKENLFTGWVDVDLTEKGISEAKAAGKLLKEEGLEFDIAYTSVLKRAIKTLNIVLEESDQLWIPVIKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYKccDVSQDNLPKAESLKDVLDR 164
Cdd:COG0588  83 WRLNERHYGALQGLNKAETAAKYGEEQVLIWRRSYDIPPPKLEKDDERSPH--RDRRYA--HLDIGGLPLTESLKDTVER 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71896857 165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGPHqFLGD 237
Cdd:COG0588 159 VLPYWEDDIAPNLKSGKNVLIVAHGNSLRALIKYLEGISDEDILDLNIPTGIPLVYELDKNLKVISAY-YLGP 230
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
5-195 5.48e-47

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 153.77  E-value: 5.48e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857      5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALG-FEFDLVFTSILRRSIQTAWLVLEEMGQewvpiqs 83
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGL------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857     84 sWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPiteshpyyeeiyndrrykccdvsqdnLPKAESLKDVLD 163
Cdd:smart00855  74 -PGLRERDFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPPA--------------------------PPGGESLADLVE 126
                          170       180       190
                   ....*....|....*....|....*....|..
gi 71896857    164 RLLPYWNEKIVPELKSGKKILISAHGNSSRAL 195
Cdd:smart00855 127 RVEPALDELIATADASGQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
5-228 2.58e-45

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718  Cd Length: 153  Bit Score: 149.01  E-value: 2.58e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMgqEWVPIQSS 84
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEEL--PGLPVEVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  85 WRLNErhygaliglnraemalnhgeeqvkiwrrsydvtpppiteshpyyeeiyndrrykccdvsqdnlpkaeslkdvlDR 164
Cdd:cd07067  79 PRLRE-------------------------------------------------------------------------AR 85
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71896857 165 LLPYWNEKIVPElkSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRP 228
Cdd:cd07067  86 VLPALEELIAPH--DGKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISVLELDENGGG 147
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
6-225 1.07e-33

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 395236 [Multi-domain]  Cd Length: 194  Bit Score: 120.78  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857     6 LVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKalGFEFDLVFTSILRRSIQTAWLVLEEMGqewVPIQSSW 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEALG---LPVEIDP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    86 RLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPiteshpyyeeiyndrrykccdvsqdnlpkAESLKDVLDRL 165
Cdd:pfam00300  76 RLREIDFGDWEGLTFAEIAERYPEEYDAWLADPADYRPPG-----------------------------GESLADVRARV 126
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71896857   166 LPYWnEKIVPELKsGKKILISAHGNSSRALLKHLEGISDKDIMNVTLP-TGVpVLLELDEN 225
Cdd:pfam00300 127 RAAL-EELAARHP-GGTVLVVSHGGVIRALLAHLLGLPLEALRRFPLDnASL-SILEFDGG 184
 
Name Accession Description Interval E-value
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-255 1.95e-138

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 388.83  E-value: 1.95e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    4 YKLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQS 83
Cdd:PRK14115   1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQMWLPVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   84 SWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEeiYNDRRYKccDVSQDNLPKAESLKDVLD 163
Cdd:PRK14115  81 SWRLNERHYGALQGLNKAETAAKYGDEQVKIWRRSYDVPPPALEKDDERYP--GHDPRYA--KLPEEELPLTESLKDTIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  164 RLLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGpHQFLGDQEAIQA 243
Cdd:PRK14115 157 RVLPYWNETIAPQLKSGKRVLIAAHGNSLRALVKYLDNISDEEILELNIPTGVPLVYELDENLKPIK-HYYLGDADEIAA 235
                        250
                 ....*....|..
gi 71896857  244 AIKKVEDQGKVK 255
Cdd:PRK14115 236 AAAAVANQGKAK 247
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
5-253 8.13e-132

phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are phosphoglycerate mutase (EC 5.4.2.1). This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate. The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have are phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (EC 5.4.2.4). This model is designated as a subfamily for this reason. The second and third paralogs in S. cerevisiae are somewhat divergent and apparently inactive (see PUBMED:9544241) but are also part of this subfamily phylogenetically.


Pssm-ID: 213596  Cd Length: 245  Bit Score: 372.13  E-value: 8.13e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857     5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:TIGR01258   2 KLVLVRHGESEWNALNLFTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDELDQLWIPVKKS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYKccDVSQDNLPKAESLKDVLDR 164
Cdd:TIGR01258  82 WRLNERHYGALQGLNKAETAAKYGEEQVNIWRRSFDVPPPPIDESDPRSPH--NDPRYA--HLDPKVLPLTESLKDTIAR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGPHqFLGDQEAIQAA 244
Cdd:TIGR01258 158 VLPYWNDEIAPDLLSGKRVLIVAHGNSLRALVKHLEGISDEEILELNIPTGIPLVYELDENLKPIKHY-YLGDPEAAAAA 236

                  ....*....
gi 71896857   245 IKKVEDQGK 253
Cdd:TIGR01258 237 AEAVANQGK 245
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
16-256 5.16e-127

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 359.74  E-value: 5.16e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   16 WNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSSWRLNERHYGAL 95
Cdd:PTZ00123   1 WNKENRFTGWTDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEELGQLHVPVIKSWRLNERHYGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   96 IGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYKccDVSQDNLPKAESLKDVLDRLLPYWNEKIVP 175
Cdd:PTZ00123  81 QGLNKSETAEKHGEEQVKIWRRSYDIPPPPLEKSDERYPG--NDPVYK--DIPKDALPNTECLKDTVERVLPYWEDHIAP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  176 ELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGpHQFLGDQEAIQAAIKKVEDQGKVK 255
Cdd:PTZ00123 157 DILAGKKVLVAAHGNSLRALVKYLDKMSEEDILELNIPTGVPLVYELDENLKPIK-KYYLLDEEELKAKMEAVANQGKAK 235

                 .
gi 71896857  256 S 256
Cdd:PTZ00123 236 S 236
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];
5-237 1.08e-118

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];


Pssm-ID: 223661  Cd Length: 230  Bit Score: 338.48  E-value: 1.08e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:COG0588   3 KLVLLRHGQSEWNKENLFTGWVDVDLTEKGISEAKAAGKLLKEEGLEFDIAYTSVLKRAIKTLNIVLEESDQLWIPVIKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYKccDVSQDNLPKAESLKDVLDR 164
Cdd:COG0588  83 WRLNERHYGALQGLNKAETAAKYGEEQVLIWRRSYDIPPPKLEKDDERSPH--RDRRYA--HLDIGGLPLTESLKDTVER 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71896857 165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGPHqFLGD 237
Cdd:COG0588 159 VLPYWEDDIAPNLKSGKNVLIVAHGNSLRALIKYLEGISDEDILDLNIPTGIPLVYELDKNLKVISAY-YLGP 230
gpmA PRK14120
phosphoglyceromutase; Provisional
1-253 4.86e-110

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 317.37  E-value: 4.86e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    1 MTKYKLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVP 80
Cdd:PRK14120   2 MMTYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANLALDAADRLWIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   81 IQSSWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYKCCDVSqdnlPKAESLKD 160
Cdd:PRK14120  82 VRRSWRLNERHYGALQGKDKAETKAEYGEEQFMLWRRSYDTPPPPIEDGSEYSQD--NDPRYADLGVG----PRTECLKD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  161 VLDRLLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRPLGPHQFLGDQEA 240
Cdd:PRK14120 156 VVARFLPYWEDDIVPDLKAGKTVLIAAHGNSLRALVKHLDGISDEDIAGLNIPTGIPLVYELDEDFKPLNPGGTYLDPEA 235
                        250
                 ....*....|...
gi 71896857  241 IQAAIKKVEDQGK 253
Cdd:PRK14120 236 AAAGAAAVANQGK 248
gpmA PRK14117
phosphoglyceromutase; Provisional
5-226 4.63e-93

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 273.44  E-value: 4.63e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:PRK14117   3 KLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTTNLALEASDQLWVPVEKS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYyeEIYNDRRYKCCDVSQdnLPKAESLKDVLDR 164
Cdd:PRK14117  83 WRLNERHYGGLTGKNKAEAAEQFGDEQVHIWRRSYDVLPPAMAKDDEY--SAHTDRRYASLDDSV--IPDAENLKVTLER 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71896857  165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENL 226
Cdd:PRK14117 159 ALPFWEDKIAPALKDGKNVFVGAHGNSIRALVKHIKGLSDDEIMDVEIPNFPPLVFEFDEKL 220
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
5-227 3.46e-92

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 271.08  E-value: 3.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:PRK14118   2 ELVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEAGYEFDIAFTSVLTRAIKTCNIVLEESNQLWIPQVKN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYyeEIYNDRRYkcCDVSQDNLPKAESLKDVLDR 164
Cdd:PRK14118  82 WRLNERHYGALQGLDKKATAEQYGDEQVHIWRRSYDTLPPDLDPQDPN--SAHNDRRY--AHLPADVVPDAENLKVTLER 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71896857  165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLR 227
Cdd:PRK14118 158 VLPFWEDQIAPALLSGKRVLVAAHGNSLRALAKHIEGISDADIMDLEIPTGQPLVYKLDDNLK 220
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
5-226 3.45e-86

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 255.99  E-value: 3.45e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:PRK14116   3 KLVLIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTLHYALEESDQLWIPETKT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHPYYEEiyNDRRYkcCDVSQDNLPKAESLKDVLDR 164
Cdd:PRK14116  83 WRLNERHYGALQGLNKKETAEKYGDEQVHIWRRSYDVLPPLLDADDEGSAA--KDRRY--ANLDPRIIPGGENLKVTLER 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71896857  165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENL 226
Cdd:PRK14116 159 VIPFWEDHIAPDLLDGKNVIIAAHGNSLRALTKYIENISDEDIMNLEMATGEPVVYDFDEKL 220
gpmA PRK14119
phosphoglyceromutase; Provisional
5-226 8.04e-86

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 255.20  E-value: 8.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSS 84
Cdd:PRK14119   3 KLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESKQQWIPVYKS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   85 WRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPITESHpyYEEIYNDRRYKCCDvsQDNLPKAESLKDVLDR 164
Cdd:PRK14119  83 WRLNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYDVKPPAETEEQ--REAYLADRRYNHLD--KRMMPYSESLKDTLVR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71896857  165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENL 226
Cdd:PRK14119 159 VIPFWTDHISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDIINYEIKTGAPLVYELTDDL 220
PRK01295 PRK01295
phosphoglyceromutase; Provisional
6-223 1.18e-65

phosphoglyceromutase; Provisional


Pssm-ID: 167205  Cd Length: 206  Bit Score: 203.00  E-value: 1.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    6 LVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQSSW 85
Cdd:PRK01295   5 LVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELGQPGLETIRDQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   86 RLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPpiteshpyyeeiyndrrykccdvsqdnlpKAESLKDVLDRL 165
Cdd:PRK01295  85 ALNERDYGDLSGLNKDDARAKWGEEQVHIWRRSYDVPPP-----------------------------GGESLKDTGARV 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 71896857  166 LPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELD 223
Cdd:PRK01295 136 LPYYLQEILPRVLRGERVLVAAHGNSLRALVMVLDGLTPEQILKLELATGVPIVYRLN 193
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
5-224 6.30e-63

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 196.87  E-value: 6.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALgfEFDLVFTSILRRSIQTAWLVL------------- 71
Cdd:PRK01112   3 LLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIKDL--PIDCIFTSTLVRSLMTALLAMtnhssgkipyivh 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   72 EEMGQEW-------------VPIQSSWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPppiteshpyyeeiyn 138
Cdd:PRK01112  81 EEDDKKWmsriysdeepeqmIPLFQSSALNERMYGELQGKNKAETAEKFGEEQVKLWRRSYKTAP--------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  139 drrykccdvsqdnlPKAESLKDVLDRLLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPV 218
Cdd:PRK01112 146 --------------PQGESLEDTGQRTLPYFQNRILPHLQQGKNVFVSAHGNSLRSLIMDLEKLSEEEVLSLELPTGKPI 211

                 ....*.
gi 71896857  219 LLELDE 224
Cdd:PRK01112 212 VYEWTG 217
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
5-195 5.48e-47

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 153.77  E-value: 5.48e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857      5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALG-FEFDLVFTSILRRSIQTAWLVLEEMGQewvpiqs 83
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGL------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857     84 sWRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPiteshpyyeeiyndrrykccdvsqdnLPKAESLKDVLD 163
Cdd:smart00855  74 -PGLRERDFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPPA--------------------------PPGGESLADLVE 126
                          170       180       190
                   ....*....|....*....|....*....|..
gi 71896857    164 RLLPYWNEKIVPELKSGKKILISAHGNSSRAL 195
Cdd:smart00855 127 RVEPALDELIATADASGQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
5-228 2.58e-45

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718  Cd Length: 153  Bit Score: 149.01  E-value: 2.58e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMgqEWVPIQSS 84
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEEL--PGLPVEVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  85 WRLNErhygaliglnraemalnhgeeqvkiwrrsydvtpppiteshpyyeeiyndrrykccdvsqdnlpkaeslkdvlDR 164
Cdd:cd07067  79 PRLRE-------------------------------------------------------------------------AR 85
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71896857 165 LLPYWNEKIVPElkSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRP 228
Cdd:cd07067  86 VLPALEELIAPH--DGKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISVLELDENGGG 147
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
5-228 1.42e-38

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716  Cd Length: 153  Bit Score: 131.77  E-value: 1.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQeWVPIQSS 84
Cdd:cd07040   1 VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFE-GLPVEVD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  85 WRlnerhygaliglnraemalnhgeeqvkiwrrsydvtpppiteshpyyeeiyndrrykccdvsqdnlpkaeslkdvlDR 164
Cdd:cd07040  80 PR----------------------------------------------------------------------------AR 83
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71896857 165 LLPYWNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDENLRP 228
Cdd:cd07040  84 VLNALLELLARHLLDGKNVLIVSHGGTIRALLAALLGLSDEEILSLNLPNGSILVLELDECGGK 147
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
6-225 1.07e-33

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 395236 [Multi-domain]  Cd Length: 194  Bit Score: 120.78  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857     6 LVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKalGFEFDLVFTSILRRSIQTAWLVLEEMGqewVPIQSSW 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEALG---LPVEIDP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    86 RLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPiteshpyyeeiyndrrykccdvsqdnlpkAESLKDVLDRL 165
Cdd:pfam00300  76 RLREIDFGDWEGLTFAEIAERYPEEYDAWLADPADYRPPG-----------------------------GESLADVRARV 126
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71896857   166 LPYWnEKIVPELKsGKKILISAHGNSSRALLKHLEGISDKDIMNVTLP-TGVpVLLELDEN 225
Cdd:pfam00300 127 RAAL-EELAARHP-GGTVLVVSHGGVIRALLAHLLGLPLEALRRFPLDnASL-SILEFDGG 184
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
5-225 1.02e-31

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 223483 [Multi-domain]  Cd Length: 208  Bit Score: 116.05  E-value: 1.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQEWVPIQss 84
Cdd:COG0406   4 RLYLVRHGETEWNVEGRLQGWTDSPLTEEGRAQAEALAERLAARDIGFDAIYSSPLKRAQQTAEPLAEELGLPLEVDD-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857  85 wRLNERHYGALIGLNRAEMALNHGEEQVKIWRRSYDVTPPPiteshpyyeeiyndrrykccdvsqdnlpkAESLKDVLDR 164
Cdd:COG0406  82 -RLREIDFGDWEGLTIDELAEEPPEELAAWLADPYLAPPPG-----------------------------GESLADVSKR 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71896857 165 LLPYWNEkiVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMNVTLPTGVPVLLELDEN 225
Cdd:COG0406 132 VVAALAE--LLRSPPGNNVLVVSHGGVIRALLAYLLGLDLEELWRLRLDNASVTVLEFDDG 190
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
5-94 1.26e-10

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966  Cd Length: 199  Bit Score: 59.29  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    5 KLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALgfEFDLVFTSILRRSIQTAWLVLEEMGqewVPIQSS 84
Cdd:PRK15004   2 RLWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDV--PFDLVLCSELERAQHTARLVLSDRQ---LPVHII 76
                         90
                 ....*....|
gi 71896857   85 WRLNERHYGA 94
Cdd:PRK15004  77 PELNEMFFGD 86
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
6-124 1.11e-09

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 58.07  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    6 LVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGfEFDLVFTSILRRSIQTAWLVLEEMGqewVPIQSSW 85
Cdd:PRK07238 174 LLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALG---LDVTVDD 249
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71896857   86 RLNERHYGALIGLNRAEMALNHGEEQVKiWRRSYDVTPP 124
Cdd:PRK07238 250 DLIETDFGAWEGLTFAEAAERDPELHRA-WLADTSVAPP 287
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
5-77 2.34e-09

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 224973  Cd Length: 163  Bit Score: 54.99  E-value: 2.34e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71896857   5 KLVLLRHGEGAWNKENRFCSwvDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWLVLEEMGQE 77
Cdd:COG2062   3 RLYLMRHGKAEWAAPGIADF--DRPLTERGRKEAELVAAWLAGQGVEPDLVLVSPAVRARQTAEIVAEHLGEK 73
PRK13462 PRK13462
acid phosphatase; Provisional
1-78 9.83e-08

acid phosphatase; Provisional


Pssm-ID: 139587  Cd Length: 203  Bit Score: 50.99  E-value: 9.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    1 MTKYKLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFDLVFTSILRRSIQTAWL----VLEEMGQ 76
Cdd:PRK13462   3 VRNHRLLLLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLagltVDEVSGL 82

                 ....
gi 71896857   77 --EW 78
Cdd:PRK13462  83 laEW 86
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
8-118 1.45e-07

phosphoglycerate mutase GpmB;


Pssm-ID: 179583  Cd Length: 215  Bit Score: 50.50  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    8 LLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEFdlVFTSILRRSIQTAWLVLEEMGqewVPIQSSWRL 87
Cdd:PRK03482   6 LVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITH--IISSDLGRTRRTAEIIAQACG---CDIIFDPRL 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 71896857   88 NERHYGALigLNRAEMALNHGEEQvkiWRRS 118
Cdd:PRK03482  81 RELNMGVL--EKRHIDSLTEEEEG---WRRQ 106
PRK13463 PRK13463
phosphoserine phosphatase 1;
3-209 9.12e-06

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 45.43  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857    3 KYKLVLLRHGEGAWNKENRFCSWVDQKLSSDGIKEAQNCGRQLKALGFEfdLVFTSILRRSIQTAWLVleeMGQEWVPIQ 82
Cdd:PRK13463   2 KTTVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIH--AIYSSPSERTLHTAELI---KGERDIPII 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71896857   83 SSWRLNERHYGALIGLNRAEMALNHGEEQVKIWrrsydvtpppiTESHPYYEEiyndrrykccdvsqdnlpKAESLKDVL 162
Cdd:PRK13463  77 ADEHFYEINMGIWEGQTIDDIERQYPDDIQLFW-----------NEPHLFQST------------------SGENFEAVH 127
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 71896857  163 DRLLPywNEKIVPELKSGKKILISAHGNSSRALLKHLEGISDKDIMN 209
Cdd:PRK13463 128 KRVIE--GMQLLLEKHKGESILIVSHAAAAKLLVGHFAGIEIENVWD 172
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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