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Conserved domains on  [gi|495162631|ref|WP_007887430|]
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MULTISPECIES: 3'(2'),5'-bisphosphate nucleotidase CysQ [Cronobacter]

Protein Classification

3'(2'),5'-bisphosphate nucleotidase CysQ( domain architecture ID 10793504)

3'(2'),5'-bisphosphate nucleotidase catalyzes the hydrolysis of the 2'- or 3'-phosphate from the appropriate nucleoside 2',5'- and 3',5'-bisphosphates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
1-247 0e+00

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


:

Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 524.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDVRQHWQRYW 80
Cdd:PRK10931   1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGKAWKEECGVRKQIQVRDARPPRVVISRSHGD 160
Cdd:PRK10931  81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 161 nAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTPRESFLNP 240
Cdd:PRK10931 161 -AELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFLNP 239

                 ....*..
gi 495162631 241 SFRVTIY 247
Cdd:PRK10931 240 GFRVSIY 246
 
Name Accession Description Interval E-value
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
1-247 0e+00

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 524.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDVRQHWQRYW 80
Cdd:PRK10931   1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGKAWKEECGVRKQIQVRDARPPRVVISRSHGD 160
Cdd:PRK10931  81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 161 nAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTPRESFLNP 240
Cdd:PRK10931 161 -AELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFLNP 239

                 ....*..
gi 495162631 241 SFRVTIY 247
Cdd:PRK10931 240 GFRVSIY 246
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
1-245 5.21e-134

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 377.96  E-value: 5.21e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYegHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEED-PPGWDVRQHWQRY 79
Cdd:COG1218    4 LLEAAIEIAREAGEAILEIY--RADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESaAIPYEERKSWDRF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  80 WLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEECGV-RKQIQVR---DARPPRVVI 154
Cdd:COG1218   82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQgAFKETGGGeRQPIRVRdrpPAEPLRVVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 155 SRSHGDnAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTaaghavavaagaqvHDWQGKTLDYTPR 234
Cdd:COG1218  162 SRSHRD-EETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTaagqaileaaggrvTDLDGKPLRYNKK 240
                        250
                 ....*....|.
gi 495162631 235 ESFLNPSFRVT 245
Cdd:COG1218  241 EDLLNPGFIAS 251
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
1-246 3.36e-128

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 362.92  E-value: 3.36e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631    1 MLEQICQLAREAGSAIMEVYegHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEED-PPGWDVRQHWQRY 79
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVY--QKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDaSIPLTPRQTWQRF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   80 WLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGKAWKEE-CG--VRKQIQVR--DARPPRVVI 154
Cdd:TIGR01331  79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREgDGqaLKAPIHVRpwPSGPLLVVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  155 SRSHgDNAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTPR 234
Cdd:TIGR01331 159 SRSH-AEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237
                         250
                  ....*....|..
gi 495162631  235 ESFLNPSFRVTI 246
Cdd:TIGR01331 238 ESFRNPNFVALG 249
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
1-244 6.34e-107

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 308.77  E-value: 6.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGHKPLEatQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDvRQHWQRYW 80
Cdd:cd01638    1 LLELLIRIAREAGDAILEVYRGGFTVE--RKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL-RLGWDRFW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEG-KAWKEECGVRKQIQVR--DARPPRVVISRS 157
Cdd:cd01638   78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGgGAYKNGRPGAVSLQARppPLQPLRVVASRS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 158 HGDnAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTpRESF 237
Cdd:cd01638  158 HPD-EELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-REDF 235

                 ....*..
gi 495162631 238 LNPSFRV 244
Cdd:cd01638  236 LNPDFIA 242
Inositol_P pfam00459
Inositol monophosphatase family;
1-207 1.61e-47

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 158.28  E-value: 1.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631    1 MLEQICQLAREAGSAIMEVYegHKPLEATQKVDDS---PVTAADIAAHAVIVAGLKALTPQVPVLSEED--PPGWDVRQH 75
Cdd:pfam00459   5 VLKVAVELAAKAGEILREAF--SNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGgaKGDQTELTD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   76 WQRYWLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEEcgvrKQIQVRDARPPRVVI 154
Cdd:pfam00459  83 DGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKgAFLNG----QPLPVSRAPPLSEAL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495162631  155 S---------RSHGDNAELQDYLQQLGEHQTTSVGSS-LKFCLVAEGEAQLYPRFGPTNIWDT 207
Cdd:pfam00459 159 LvtlfgvssrKDTSEASFLAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDH 221
 
Name Accession Description Interval E-value
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
1-247 0e+00

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 524.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDVRQHWQRYW 80
Cdd:PRK10931   1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGKAWKEECGVRKQIQVRDARPPRVVISRSHGD 160
Cdd:PRK10931  81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 161 nAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTPRESFLNP 240
Cdd:PRK10931 161 -AELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFLNP 239

                 ....*..
gi 495162631 241 SFRVTIY 247
Cdd:PRK10931 240 GFRVSIY 246
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
1-245 5.21e-134

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 377.96  E-value: 5.21e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYegHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEED-PPGWDVRQHWQRY 79
Cdd:COG1218    4 LLEAAIEIAREAGEAILEIY--RADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESaAIPYEERKSWDRF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  80 WLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEECGV-RKQIQVR---DARPPRVVI 154
Cdd:COG1218   82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQgAFKETGGGeRQPIRVRdrpPAEPLRVVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 155 SRSHGDnAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTaaghavavaagaqvHDWQGKTLDYTPR 234
Cdd:COG1218  162 SRSHRD-EETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTaagqaileaaggrvTDLDGKPLRYNKK 240
                        250
                 ....*....|.
gi 495162631 235 ESFLNPSFRVT 245
Cdd:COG1218  241 EDLLNPGFIAS 251
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
1-246 3.36e-128

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 362.92  E-value: 3.36e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631    1 MLEQICQLAREAGSAIMEVYegHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEED-PPGWDVRQHWQRY 79
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVY--QKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDaSIPLTPRQTWQRF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   80 WLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGKAWKEE-CG--VRKQIQVR--DARPPRVVI 154
Cdd:TIGR01331  79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREgDGqaLKAPIHVRpwPSGPLLVVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  155 SRSHgDNAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTPR 234
Cdd:TIGR01331 159 SRSH-AEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237
                         250
                  ....*....|..
gi 495162631  235 ESFLNPSFRVTI 246
Cdd:TIGR01331 238 ESFRNPNFVALG 249
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
1-244 6.34e-107

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 308.77  E-value: 6.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGHKPLEatQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDvRQHWQRYW 80
Cdd:cd01638    1 LLELLIRIAREAGDAILEVYRGGFTVE--RKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL-RLGWDRFW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEG-KAWKEECGVRKQIQVR--DARPPRVVISRS 157
Cdd:cd01638   78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGgGAYKNGRPGAVSLQARppPLQPLRVVASRS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 158 HGDnAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPTNIWDTAAGHAVAVAAGAQVHDWQGKTLDYTpRESF 237
Cdd:cd01638  158 HPD-EELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-REDF 235

                 ....*..
gi 495162631 238 LNPSFRV 244
Cdd:cd01638  236 LNPDFIA 242
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
2-207 1.25e-53

Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.


Pssm-ID: 238815 [Multi-domain]  Cd Length: 238  Bit Score: 172.88  E-value: 1.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   2 LEQICQLAREAGSAIMEVYEGHKPLEATqKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDVRqHWQRYWL 81
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS-DGGRVWV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  82 VDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEECGVRKqiqVRDARPPRVVIS--RSH 158
Cdd:cd01637   79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKgAFLNGKKLPL---SKDTPLNDALLStnASM 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495162631 159 GDNAELQDYLQQLGEHQTT-SVGS-SLKFCLVAEGEAQLYPRFGPtNIWDT 207
Cdd:cd01637  156 LRSNRAAVLASLVNRALGIrIYGSaGLDLAYVAAGRLDAYLSSGL-NPWDY 205
Inositol_P pfam00459
Inositol monophosphatase family;
1-207 1.61e-47

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 158.28  E-value: 1.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631    1 MLEQICQLAREAGSAIMEVYegHKPLEATQKVDDS---PVTAADIAAHAVIVAGLKALTPQVPVLSEED--PPGWDVRQH 75
Cdd:pfam00459   5 VLKVAVELAAKAGEILREAF--SNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGgaKGDQTELTD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   76 WQRYWLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEEcgvrKQIQVRDARPPRVVI 154
Cdd:pfam00459  83 DGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKgAFLNG----QPLPVSRAPPLSEAL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495162631  155 S---------RSHGDNAELQDYLQQLGEHQTTSVGSS-LKFCLVAEGEAQLYPRFGPTNIWDT 207
Cdd:pfam00459 159 LvtlfgvssrKDTSEASFLAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDH 221
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
2-207 2.34e-43

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


Pssm-ID: 238814 [Multi-domain]  Cd Length: 184  Bit Score: 144.84  E-value: 2.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   2 LEQICQLAREAGSAIMEVYEGHKPLEATQ-KVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGW-DVRQHWQRY 79
Cdd:cd01636    1 LEELCRVAKEAGLAILKAFGRELSGKVKItKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEeVMGRRDEYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  80 WLVDPLDGTKEFLKRNGEFTVNIALIengkpvlgvvyapvlnVMYSAAEgkawkeecgvrkqiqvrdarpprvvisRSHG 159
Cdd:cd01636   81 WVIDPIDGTKNFINGLPFVAVVIAVY----------------VILILAE---------------------------PSHK 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495162631 160 DNAELQDYLQQLGEHQTTSVGS-SLKFCLVAEGEAQLYPRFGPT-NIWDT 207
Cdd:cd01636  118 RVDEKKAELQLLAVYRIRIVGSaVAKMCLVALGLADIYYEPGGKrRAWDV 167
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
1-206 1.93e-41

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 142.29  E-value: 1.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYeGHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDppGWDVRQHWQRYW 80
Cdd:COG0483    3 LLELALRAARAAGALILRRF-RELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEES--GASEGRDSGYVW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEEcgvrKQIQVRDARPPR---VVISR 156
Cdd:COG0483   80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGgAFLNG----RRLRVSARTDLEdalVATGF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495162631 157 SH-GDNAELQDYLQQLGEH--QTTSVGS-SLKFCLVAEGEAQLYPRFGpTNIWD 206
Cdd:COG0483  156 PYlRDDREYLAALAALLPRvrRVRRLGSaALDLAYVAAGRLDAFVEAG-LKPWD 208
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
31-206 3.80e-32

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 118.57  E-value: 3.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  31 KVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEED--PPGwdvrqhwqRYWLVDPLDGTKEFLkRNGEFTVNIALIENG 108
Cdd:cd01517   32 KSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDsaALG--------RFWVLDPIDGTKGFL-RGDQFAVALALIEDG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 109 KPVLGVVYAPVLNV-------MYSAAEGK-AW--KEECGVRKQIQVRDARPP--RVVIS---RSHGDNAELQDYLQQLGE 173
Cdd:cd01517  103 EVVLGVIGCPNLPLddggggdLFSAVRGQgAWlrPLDGSSLQPLSVRQLTNAarASFCEsveSAHSSHRLQAAIKALGGT 182
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495162631 174 HQTTSVGSSLKFCLVAEGEAQLYPRFG-----PTNIWD 206
Cdd:cd01517  183 PQPVRLDSQAKYAAVARGAADFYLRLPlsmsyREKIWD 220
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
1-206 2.68e-30

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 113.02  E-value: 2.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGhKPLEATQK---VDdsPVTAADIAAHAVIVAGLKALTPQVPVLSEE--------DPPg 69
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEK-LGLNVEEKgspVD--LVTEVDKAVEKLIIEILKKAYPDHGFLGEEsgaaggltDEP- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  70 wdvrqhwqrYWLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEEcgvrKQIQVRDAR 148
Cdd:cd01639   77 ---------TWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQgAFLNG----RRIRVSGRK 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495162631 149 PPR---VVISRSHGDNAELQDYLQQLGE------HQTTSVGS-SLKFCLVAEGEAQLYPRFGpTNIWD 206
Cdd:cd01639  144 ELKdalVATGFPYDRGDNFDRYLNNFAKllakavRGVRRLGSaALDLAYVAAGRLDGYWERG-LKPWD 210
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
7-148 3.89e-25

Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate fructose-1,6-bisphosphate, inositol monophospate, 3'-phosphoadenosine-5'-phosphate, or similar substrates.


Pssm-ID: 238819 [Multi-domain]  Cd Length: 248  Bit Score: 99.25  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   7 QLAREAGSAIMEVYEghKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDppGWDvRQHWQRYWLVDPLD 86
Cdd:cd01641    7 ELADAAGQITLPYFR--TRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEF--GNE-GGDAGYVWVLDPID 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495162631  87 GTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGKAWKEECGVRKQIQVRDAR 148
Cdd:cd01641   82 GTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVRACA 143
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
7-206 3.53e-24

Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate inositol monophosphate or similar substrates.


Pssm-ID: 238821 [Multi-domain]  Cd Length: 242  Bit Score: 96.64  E-value: 3.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   7 QLAREAGSAIMEVYEGHkpLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEE---DPPGWDvrqhwqRYWLVD 83
Cdd:cd01643    6 AIAQEAGDRALADFGNS--LSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEgggIFPSSG------WYWVID 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  84 PLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK-AWKEecGVRKQIQVRDARP-PRVVISRSH--G 159
Cdd:cd01643   78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGgAFLN--GKPLALHPPLQLPdCNVGFNRSSraS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495162631 160 DNAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYPRFGPtNIWD 206
Cdd:cd01643  156 ARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATP-KIWD 201
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
7-231 4.60e-21

3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.


Pssm-ID: 273558 [Multi-domain]  Cd Length: 353  Bit Score: 90.31  E-value: 4.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631    7 QLAREAGSAIMEVYEG---HKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGW------------- 70
Cdd:TIGR01330  11 QAVRLASLLTKKVQSElisHKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSGLseadftlgrvnel 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   71 --DVRQHWQ-------------------------------RYWLVDPLDGTKEFLkRNGEFTVNIALIENGKPVLGVVYA 117
Cdd:TIGR01330  91 vnETLVYAKnykkddqfplksledvlqiidfgnyeggrkgRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIGC 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  118 PVLNVMYSAAEGKAWKEECG-----VRK----------------QIQVRDARPPRVVI--------SRSHGDNAELQDYL 168
Cdd:TIGR01330 170 PNLPLSSYGAQNLKGSESKGcifraVRGsgafmyslssdaesptKVHVSSVKDTKDAIfcegvekgHSSHDEQTAIANKL 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495162631  169 QQlgEHQTTSVGSSLKFCLVAEGEAQLYPRFgPTN------IWDTAAGHAVAVAAGAQVHDWQGKTLDY 231
Cdd:TIGR01330 250 GI--SKSPLRLDSQAKYAALARGDADVYLRL-PIKlsyqekIWDHAAGNVIVEEAGGIVTDAMGKPLDF 315
PRK10757 PRK10757
inositol-1-monophosphatase;
1-130 7.49e-19

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 82.93  E-value: 7.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMEVYEGHKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDppGWDVRQHWQRYW 80
Cdd:PRK10757   4 MLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES--GELEGEDQDVQW 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK 130
Cdd:PRK10757  82 VIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQ 131
PLN02911 PLN02911
inositol-phosphate phosphatase
2-121 1.19e-16

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 77.45  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   2 LEQICQLAREAGSAIMEVYEGH--KPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDppGWDVRQHWQRY 79
Cdd:PLN02911  33 LDRFVDVAHKLADAAGEVTRKYfrTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEH--GLRCGEGSSDY 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495162631  80 -WLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLN 121
Cdd:PLN02911 111 vWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLK 153
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
27-240 1.48e-16

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 76.98  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  27 EATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDVRQHWQRY-------------------------Wl 81
Cdd:cd01640   32 GKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVdldeeileescpspskdlpeedlgvW- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  82 VDPLDGTKEFLKRNGEF-TVNIALIENGKPVLGVVYAPVlnVMYSAAEGkAWKEEC--GVR------KQIQVRDARPpRV 152
Cdd:cd01640  111 VDPLDATQEYTEGLLEYvTVLIGVAVKGKPIAGVIHQPF--YEKTAGAG-AWLGRTiwGLSglgahsSDFKEREDAG-KI 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631 153 VISRSH-GDNAELQDYLQQLGEHQTTSVGSSLKFCLVAEGEAQLYpRF--GPTNIWDTAAGHAVAVAAGAQVHDWQGKTL 229
Cdd:cd01640  187 IVSTSHsHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAY-VHstGGIKKWDICAPEAILRALGGDMTDLHGEPL 265
                        250
                 ....*....|.
gi 495162631 230 DYTPRESFLNP 240
Cdd:cd01640  266 SYSKAVKPVNK 276
PLN02553 PLN02553
inositol-phosphate phosphatase
9-130 1.39e-15

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 73.96  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   9 AREAGSAIMEVYEGHKPLEATQKVDdsPVTAADIAAHAVIVAGLKALTPQVPVLSEE-----------DPPGWdvrqhwq 77
Cdd:PLN02553  18 AKAAGQIIRKGFYQTKHVEHKGQVD--LVTETDKACEDLIFNHLKQAFPSHKFIGEEttaasggteltDEPTW------- 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495162631  78 rywLVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVVYAPVLNVMYSAAEGK 130
Cdd:PLN02553  89 ---IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGK 138
PLN02737 PLN02737
inositol monophosphatase family protein
2-115 9.32e-07

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 49.03  E-value: 9.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   2 LEQICQLAREAGS-AIMEVYEghKPLEATQKVDDSPVTAADIAAHAVIVAGLKALTPQVPVLSEEDPPGWDVRQHWqrYW 80
Cdd:PLN02737  79 LLAVAELAAKTGAeVVMEAVN--KPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDY--LW 154
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495162631  81 LVDPLDGTKEFLKRNGEFTVNIALIENGKPVLGVV 115
Cdd:PLN02737 155 CIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATV 189
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
1-191 2.38e-06

Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.


Pssm-ID: 238773 [Multi-domain]  Cd Length: 257  Bit Score: 47.37  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631   1 MLEQICQLAREAGSAIMevyeghkPLEATQK--------VDDSPVTAADIAAHAVIVAGLKALTPqVPVLSEE------- 65
Cdd:cd01515    1 WLEIARNIAKEIEKAIK-------PLFGTEDasevvkigADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEigvidng 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162631  66 DPPGWDVrqhwqrywLVDPLDGTKEFLKRNGEFTVNIALIENGK--PVLGVVYAPVLNVMYSAAEGK-AWKEecgvRKQI 142
Cdd:cd01515   73 DEPEYTV--------VLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKgAYLN----GKRI 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495162631 143 QVRDARPP-RVVISRSHGDNAELQDYLQQLGEHQTTSVGS-SLKFCLVAEG 191
Cdd:cd01515  141 KVSDFSSLkSISVSYYIYGKNHDRTFKICRKVRRVRIFGSvALELCYVASG 191
 
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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