NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046557346|ref|WP_065656759|]
View 

MULTISPECIES: 3'(2'),5'-bisphosphate nucleotidase CysQ [Rhizobium/Agrobacterium group]

Protein Classification

3'(2'),5'-bisphosphate nucleotidase CysQ( domain architecture ID 10787368)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 1-257 6.10e-107

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


:

Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 309.78  E-value: 6.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPE-TGAEFFL 79
Cdd:COG1218     4 LLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERkSWDRFWL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTG-EDNAAEKLAISGEgailsRHPIRARQR--GASPV 156
Cdd:COG1218    84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAaKGQGAFKETGGGE-----RQPIRVRDRppAEPLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 157 ALISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYA 236
Cdd:COG1218   159 VVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYN 238

                         250       260
                  ....*....|....*....|.
gi 1046557346 237 VRGDgedaLANPDFIAEGAMA 257
Cdd:COG1218   239 KKED----LLNPGFIASGDHA 255
 
Name Accession Description Interval E-value
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 1-257 6.10e-107

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 309.78  E-value: 6.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPE-TGAEFFL 79
Cdd:COG1218     4 LLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERkSWDRFWL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTG-EDNAAEKLAISGEgailsRHPIRARQR--GASPV 156
Cdd:COG1218    84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAaKGQGAFKETGGGE-----RQPIRVRDRppAEPLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 157 ALISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYA 236
Cdd:COG1218   159 VVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYN 238

                         250       260
                  ....*....|....*....|.
gi 1046557346 237 VRGDgedaLANPDFIAEGAMA 257
Cdd:COG1218   239 KKED----LLNPGFIASGDHA 255
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 1-252 2.30e-94

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: 277.57  E-value: 2.30e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGaEFFLV 80
Cdd:cd01638     1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWD-RFWLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  81 DPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGEDNA-AEKlaisgEGAILSRHPIRARQRGASPVALI 159
Cdd:cd01638    80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGgAYK-----NGRPGAVSLQARPPPLQPLRVVA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 160 SRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYavrg 239
Cdd:cd01638   155 SRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTY---- 230

                         250
                  ....*....|...
gi 1046557346 240 dGEDALANPDFIA 252
Cdd:cd01638   231 -NREDFLNPDFIA 242
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 1-254 6.19e-92

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: 271.63  E-value: 6.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILP-ETGAEFFL 79
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPrQTWQRFWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGEDNAAEKLAISGEGAilsRHPIRARQRGASPVA-L 158
Cdd:TIGR01331  81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQAL---KAPIHVRPWPSGPLLvV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 159 ISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYAVR 238
Cdd:TIGR01331 158 ISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237

                         250
                  ....*....|....*.
gi 1046557346 239 gdgeDALANPDFIAEG 254
Cdd:TIGR01331 238 ----ESFRNPNFVALG 249
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 1-250 1.33e-68

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 212.24  E-value: 1.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRaGPH---VSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGAEF 77
Cdd:PRK10931    1 MLEQICQLARNAGDAIMQVYD-GTKpldVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  78 FLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAP--------CRGQAWTGEDNaaeklaisgegailSRHPIRAR 149
Cdd:PRK10931   80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPvmnvmysaAEGKAWKEECG--------------VRKQIQVR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 150 qRGASPVALISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCE 229
Cdd:PRK10931  146 -DARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQ 224

                         250       260
                  ....*....|....*....|.
gi 1046557346 230 GRPLAYAVRgdgeDALANPDF 250
Cdd:PRK10931  225 GKTLDYTPR----ESFLNPGF 241
Inositol_P pfam00459
Inositol monophosphatase family;
1-239 4.70e-50

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 165.21  E-value: 4.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCS---PVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGAE- 76
Cdd:pfam00459   5 VLKVAVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDDg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  77 -FFLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTgednaaeklAISGEGAILSRHPIRARQRGASP 155
Cdd:pfam00459  85 pTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYS---------AAKGKGAFLNGQPLPVSRAPPLS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 156 VALI----SRSHCTAKTEAFVAEHGLKD-----CISVGSS-LKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRT 225
Cdd:pfam00459 156 EALLvtlfGVSSRKDTSEASFLAKLLKLvrapgVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVV 235

                         250
                  ....*....|....
gi 1046557346 226 LDCEGRPLAYAVRG 239
Cdd:pfam00459 236 TDADGGPFDLLAGR 249
 
Name Accession Description Interval E-value
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 1-257 6.10e-107

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 309.78  E-value: 6.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPE-TGAEFFL 79
Cdd:COG1218     4 LLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERkSWDRFWL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTG-EDNAAEKLAISGEgailsRHPIRARQR--GASPV 156
Cdd:COG1218    84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAaKGQGAFKETGGGE-----RQPIRVRDRppAEPLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 157 ALISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYA 236
Cdd:COG1218   159 VVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYN 238

                         250       260
                  ....*....|....*....|.
gi 1046557346 237 VRGDgedaLANPDFIAEGAMA 257
Cdd:COG1218   239 KKED----LLNPGFIASGDHA 255
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 1-252 2.30e-94

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: 277.57  E-value: 2.30e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGaEFFLV 80
Cdd:cd01638     1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWD-RFWLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  81 DPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGEDNA-AEKlaisgEGAILSRHPIRARQRGASPVALI 159
Cdd:cd01638    80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGgAYK-----NGRPGAVSLQARPPPLQPLRVVA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 160 SRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYavrg 239
Cdd:cd01638   155 SRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTY---- 230

                         250
                  ....*....|...
gi 1046557346 240 dGEDALANPDFIA 252
Cdd:cd01638   231 -NREDFLNPDFIA 242
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 1-254 6.19e-92

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: 271.63  E-value: 6.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILP-ETGAEFFL 79
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPrQTWQRFWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGEDNAAEKLAISGEGAilsRHPIRARQRGASPVA-L 158
Cdd:TIGR01331  81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQAL---KAPIHVRPWPSGPLLvV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 159 ISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYAVR 238
Cdd:TIGR01331 158 ISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237

                         250
                  ....*....|....*.
gi 1046557346 239 gdgeDALANPDFIAEG 254
Cdd:TIGR01331 238 ----ESFRNPNFVALG 249
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 1-250 1.33e-68

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 212.24  E-value: 1.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRaGPH---VSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGAEF 77
Cdd:PRK10931    1 MLEQICQLARNAGDAIMQVYD-GTKpldVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  78 FLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAP--------CRGQAWTGEDNaaeklaisgegailSRHPIRAR 149
Cdd:PRK10931   80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPvmnvmysaAEGKAWKEECG--------------VRKQIQVR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 150 qRGASPVALISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCE 229
Cdd:PRK10931  146 -DARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQ 224

                         250       260
                  ....*....|....*....|.
gi 1046557346 230 GRPLAYAVRgdgeDALANPDF 250
Cdd:PRK10931  225 GKTLDYTPR----ESFLNPGF 241
Inositol_P pfam00459
Inositol monophosphatase family;
1-239 4.70e-50

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 165.21  E-value: 4.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCS---PVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGAE- 76
Cdd:pfam00459   5 VLKVAVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDDg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  77 -FFLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTgednaaeklAISGEGAILSRHPIRARQRGASP 155
Cdd:pfam00459  85 pTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYS---------AAKGKGAFLNGQPLPVSRAPPLS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 156 VALI----SRSHCTAKTEAFVAEHGLKD-----CISVGSS-LKFCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRT 225
Cdd:pfam00459 156 EALLvtlfGVSSRKDTSEASFLAKLLKLvrapgVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVV 235

                         250
                  ....*....|....
gi 1046557346 226 LDCEGRPLAYAVRG 239
Cdd:pfam00459 236 TDADGGPFDLLAGR 249
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 1-233 8.09e-40

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: 138.44  E-value: 8.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPH-VSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGilPETGAEFFL 79
Cdd:COG0483     3 LLELALRAARAAGALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASE--GRDSGYVWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTgednaaeklAISGEGAILSRHPIRARQRGASPVALI 159
Cdd:COG0483    81 IDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFT---------AARGGGAFLNGRRLRVSARTDLEDALV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 160 S---RSHCTAKTEAFVAEHGLKDCISV----GSSLKFCMLAEGAADIYprFSRTMM-WDTAAGDAVLRAAGGRTLDCEGR 231
Cdd:COG0483   152 AtgfPYLRDDREYLAALAALLPRVRRVrrlgSAALDLAYVAAGRLDAF--VEAGLKpWDIAAGALIVREAGGVVTDLDGE 229


                  ..
gi 1046557346 232 PL 233
Cdd:COG0483   230 PL 231
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 3-240 2.76e-38

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: 133.98  E-value: 2.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   3 DILTKAALDAGQAIMAVHRAGPHVSYK-DDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPeTGAEFFLVD 81
Cdd:cd01637     2 ELALKAVREAGALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS-DGGRVWVID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  82 PLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGEDnaaeklaisGEGAILSRHPIRARQRGASPVALIS- 160
Cdd:cd01637    81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGR---------GKGAFLNGKKLPLSKDTPLNDALLSt 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 161 ----RSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRFsRTMMWDTAAGDAVLRAAGGRTLDCEGRPLAYA 236
Cdd:cd01637   152 nasmLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSS-GLNPWDYAAGALIVEEAGGIVTDLDGEPLDTL 230


                  ....
gi 1046557346 237 VRGD 240
Cdd:cd01637   231 NRSG 234
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 1-252 3.57e-35

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: 127.04  E-value: 3.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHR---AGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVssgilpETGAEF 77
Cdd:cd01517     1 ELEVAILAVRAAASLTLPVFRnlgAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS------AALGRF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  78 FLVDPLDGTKEFISGkDDFTVNIALIRNGVPVAGVVYAPcrgqAWTGEDNAAEKL--AISGEGA------ILSRHPIRAR 149
Cdd:cd01517    75 WVLDPIDGTKGFLRG-DQFAVALALIEDGEVVLGVIGCP----NLPLDDGGGGDLfsAVRGQGAwlrpldGSSLQPLSVR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 150 QRGASPV-----ALISRSHCTAKTEAFVAEHGLKDCISVGSSLKFCMLAEGAADIYPRF-----SRTMMWDTAAGDAVLR 219
Cdd:cd01517   150 QLTNAARasfceSVESAHSSHRLQAAIKALGGTPQPVRLDSQAKYAAVARGAADFYLRLplsmsYREKIWDHAAGVLIVE 229

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1046557346 220 AAGGRTLDCEGRPLAYavrGDGEDALANPDFIA 252
Cdd:cd01517   230 EAGGKVTDADGKPLDF---GKGRKLLNNGGLIA 259
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 1-238 1.21e-28

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: 108.78  E-value: 1.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIM-AVHRAGPHVSYKDDCS-PVTEADQRAEAIILAALAAHFPDIPVVAEEavsSGILPETGAEF- 77
Cdd:cd01639     1 LLNIAIEAARKAGEILLeAYEKLGLNVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEE---SGAAGGLTDEPt 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  78 FLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTgednaaeklAISGEGAILSRHPIRARQRGASPVA 157
Cdd:cd01639    78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFT---------AVRGQGAFLNGRRIRVSGRKELKDA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 158 LI-----SRSHCTAKTEAFVAEHGLKDCI----SVGS-SLKFCMLAEGAADIY------PrfsrtmmWDTAAGDAVLRAA 221
Cdd:cd01639   149 LVatgfpYDRGDNFDRYLNNFAKLLAKAVrgvrRLGSaALDLAYVAAGRLDGYwerglkP-------WDVAAGALIVREA 221

                         250
                  ....*....|....*..
gi 1046557346 222 GGRTLDCEGRPLAYAVR 238
Cdd:cd01639   222 GGLVTDFDGGPFDLMSG 238
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 2-249 1.51e-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: 100.79  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   2 IDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAvssGILPETGAEFFLVD 81
Cdd:cd01641     2 LAFALELADAAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEF---GNEGGDAGYVWVLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  82 PLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWtgednaaekLAISGEGAILSR---HPIRARQRGASPVAL 158
Cdd:cd01641    79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERW---------IGARGGGTFLNGaggRPLRVRACADLAEAV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 159 IS-------RSHCTAKTEAFVAEHGLkdCISVGSSLKFCMLAEGAADIyprfsrtMM------WDTAAGDAVLRAAGGRT 225
Cdd:cd01641   150 LSttdphffTPGDRAAFERLARAVRL--TRYGGDCYAYALVASGRVDL-------VVeaglkpYDVAALIPIIEGAGGVI 220

                         250       260
                  ....*....|....*....|....
gi 1046557346 226 LDCEGRPLayavRGDGEDALANPD 249
Cdd:cd01641   221 TDWDGGPL----TGGSGRVVAAGD 240
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 34-235 6.00e-24

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: 97.78  E-value: 6.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  34 PVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGAEFFL------------------------VDPLDGTKEF 89
Cdd:cd01640    41 FKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVDLdeeileescpspskdlpeedlgvwVDPLDATQEY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  90 ISGKDDF-TVNIALIRNGVPVAGVVYAPCRGQ-AWTGEDNAAEKLAISGEGAILSRHPirarQRGASPVALISRSHCTAK 167
Cdd:cd01640   121 TEGLLEYvTVLIGVAVKGKPIAGVIHQPFYEKtAGAGAWLGRTIWGLSGLGAHSSDFK----EREDAGKIIVSTSHSHSV 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046557346 168 TEAFVAEHGLKDCI--SVGSSLKFCMLAEGAADIYpRFSR--TMMWDTAAGDAVLRAAGGRTLDCEGRPLAY 235
Cdd:cd01640   197 KEVQLITAGNKDEVlrAGGAGYKVLQVLEGLADAY-VHSTggIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 29-252 2.31e-20

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: 87.01  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  29 KDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEavSSGILPETGAeFFLVDPLDGTKEFISGKDDFTVNIALIRNGVP 108
Cdd:cd01643    28 KADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE--GGGIFPSSGW-YWVIDPIDGTTNFARGIPIWAISIALLYRGEP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 109 VAGVVYAPCRGQAWTgednaaeklAISGEGAILSRHPIRARQRGASPVALISRSHCTAKTEAFVAEHGLKD------CIS 182
Cdd:cd01643   105 VFGVIALPALNQTFV---------AFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASARAVLRVILRRfpgkirMLG 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046557346 183 VgSSLKFCMLAEGAADIYprFSRTM-MWDTAAGDAVLRAAGGRTLDCEGRPLAYAVRGDGEDalANPDFIA 252
Cdd:cd01643   176 S-ASLNLASVAAGQTLGY--VEATPkIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYLSA--GFPTLIA 241
PLN02553 PLN02553
inositol-phosphate phosphatase
 8-233 5.54e-20

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 86.28  E-value: 5.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   8 AALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVS-SGILPETGAEFFLVDPLDGT 86
Cdd:PLN02553   17 AAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAaSGGTELTDEPTWIVDPLDGT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  87 KEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTgednaaeklAISGEGAILSRHPIRARQRGASPVALISRSHCTA 166
Cdd:PLN02553   97 TNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFT---------AVKGKGAFLNGKPIKASSQSELGKALLATEVGTK 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046557346 167 KTEAFVAE--HGLKDCISVGSSLK--------FCMLAEGAADIYPRFSRTMMWDTAAGDAVLRAAGGRTLDCEGRPL 233
Cdd:PLN02553  168 RDKATVDAttNRINALLYKVRSLRmsgscalnLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPF 244
PLN02911 PLN02911
inositol-phosphate phosphatase
 2-247 4.17e-18

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 81.69  E-value: 4.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   2 IDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEavsSGI-LPETGAEFFLV 80
Cdd:PLN02911   37 VDVAHKLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEE---HGLrCGEGSSDYVWV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  81 -DPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGednaaeklaISGEGAILSRHPIRARqrgasPVALI 159
Cdd:PLN02911  114 lDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVG---------VAGRATTLNGEEISTR-----SCASL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 160 SRSHCTAKTEAFVAEHGLKDCISVGSSLK----------FCMLAEGAADIYPRfSRTMMWDTAAGDAVLRAAGGRTLDCE 229
Cdd:PLN02911  180 KDAYLYTTSPHMFSGDAEDAFARVRDKVKvplygcdcyaYGLLASGHVDLVVE-SGLKPYDYLALVPVVEGAGGVITDWK 258

                         250
                  ....*....|....*...
gi 1046557346 230 GRPLAYAVRGDGEDALAN 247
Cdd:PLN02911  259 GRKLRWEPSPGSLATSFN 276
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 3-227 8.46e-17

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: 75.89  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   3 DILTKAALDAGQAIMAV---HRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAVSSGILPETGAEFF- 78
Cdd:cd01636     2 EELCRVAKEAGLAILKAfgrELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  79 LVDPLDGTKEFISGKDDFTVNIALIRngvpvagvvyapcrgqawtgednaaeklAISGEGAILSRHPIRARQRGASPVAL 158
Cdd:cd01636    82 VIDPIDGTKNFINGLPFVAVVIAVYV----------------------------ILILAEPSHKRVDEKKAELQLLAVYR 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046557346 159 ISRshctakteafvaehglkdcisVGS-SLKFCMLAEGAADIYPRFS-RTMMWDTAAGDAVLRAAGGRTLD 227
Cdd:cd01636   134 IRI---------------------VGSaVAKMCLVALGLADIYYEPGgKRRAWDVAASAAIVREAGGIMTD 183
PLN02737 PLN02737
inositol monophosphatase family protein
 1-232 4.58e-14

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 70.98  E-value: 4.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAGPHVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEAvssGILPETGAEF-FL 79
Cdd:PLN02737   79 LLAVAELAAKTGAEVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG---GVIGDSSSDYlWC 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  80 VDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRG-QAWTGEDNAAeklaISGEGAILSRHPIRARQRGASPVAL 158
Cdd:PLN02737  156 IDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGpMCWNTRTFSA----SAGGGAFCNGQKIHVSQTDKVERSL 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 159 ISRSHCTAKTEAFVAEHGL-KDCISV--------GSSLKFCMLAEGAADIYPRFsRTMMWDTAAGDAVLRAAGGRTLDCE 229
Cdd:PLN02737  232 LVTGFGYEHDDAWATNIELfKEFTDVsrgvrrlgAAAVDMCHVALGIVEAYWEY-RLKPWDMAAGVLIVEEAGGTVTRMD 310


                  ...
gi 1046557346 230 GRP 232
Cdd:PLN02737  311 GGK 313
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
59-233 9.15e-10

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 57.61  E-value: 9.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  59 VVAEEAvssGILPETGAEF-FLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTgednaaeklAISGE 137
Cdd:PRK12676   67 IISEEL---GEIVGNGPEYtVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYE---------AIPGK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 138 GAILSRHPIRarqrgASPVALISRSHCTAKTEAFVAEHGLKDCISV-------GSSLKFCMLAEGA----ADIYPRFSRT 206
Cdd:PRK12676  135 GAYLNGKPIK-----VSKTSELNESAVSIYGYRRGKERTVKLGRKVrrvrilgAIALELCYVASGRldafVDVRNYLRVT 209

                         170       180
                  ....*....|....*....|....*..
gi 1046557346 207 mmwDTAAGDAVLRAAGGRTLDCEGRPL 233
Cdd:PRK12676  210 ---DIAAGKLICEEAGGIVTDEDGNEL 233
PRK10757 PRK10757
inositol-1-monophosphatase;
1-230 8.22e-08

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 52.12  E-value: 8.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAImAVHRAGP---HVSYKDDCSPVTEADQRAEAIILAALAAHFPDIPVVAEEavsSGILPETGAEF 77
Cdd:PRK10757    4 MLNIAVRAARKAGNLI-AKNYETPdavEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEE---SGELEGEDQDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  78 -FLVDPLDGTKEFISGKDDFTVNIALIRNGVPVAGVVYAPCRGQAWTGEDNAAEKL---------AISGEGAILSR-HPI 146
Cdd:PRK10757   80 qWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLngyrlrgstARDLDGTILATgFPF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 147 RARQRGASPVALISR--SHCTakteafvaehglkDCISVGSS-LKFCMLAEGAADIYprFSRTMM-WDTAAGDAVLRAAG 222
Cdd:PRK10757  160 KAKQHATTYINIVGKlfTECA-------------DFRRTGSAaLDLAYVAAGRVDGF--FEIGLKpWDFAAGELLVREAG 224


                  ....*...
gi 1046557346 223 GRTLDCEG 230
Cdd:PRK10757  225 GIVSDFTG 232
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 59-233 5.36e-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: 46.60  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  59 VVAEE--AVSSGILPETgaeFFLVDPLDGTKEFISGKDDFTVNIALIRN--GVPVAGVVYAPCrgqawTGEdnaaEKLAI 134
Cdd:cd01515    61 IVSEEigVIDNGDEPEY---TVVLDPLDGTYNAINGIPFYSVSVAVFKIdkSDPYYGYVYNLA-----TGD----LYYAI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 135 SGEGAILSRHPIRAR-QRGASPVALISRSHCTAKTEAFVAEHGLKDCISVGS-SLKFCMLAEGAADIYPRFSRTM-MWDT 211
Cdd:cd01515   129 KGKGAYLNGKRIKVSdFSSLKSISVSYYIYGKNHDRTFKICRKVRRVRIFGSvALELCYVASGALDAFVDVRENLrLVDI 208

                         170       180
                  ....*....|....*....|..
gi 1046557346 212 AAGDAVLRAAGGRTLDCEGRPL 233
Cdd:cd01515   209 AAGYLIAEEAGGIVTDENGKEL 230
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 1-214 3.30e-05

Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.


Pssm-ID: 238820 [Multi-domain]  Cd Length: 244  Bit Score: 43.98  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346   1 MIDILTKAALDAGQAIMAVHRAG--PHVSYKDDcSPVTEADQRAEAIILAALAAHFPDIPVVAEEavSSGILPETGAEFF 78
Cdd:cd01642     1 MLEVLEKITKEIILLLNEKNRQGlvKLIRGAGG-DVTRVADLKAEEIILKLLREEGVFGQIISEE--SGEIRKGSGEYIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346  79 LVDPLDGTKEFISGKDDFTVNIALIRNGVPV-AGVVYAPCRGQAWTG-EDNAAEKLAISGEGaiLSRHPIRARqrgASPV 156
Cdd:cd01642    78 VLDPLDGSTNYLSGIPFYSVSVALADPRSKVkAATLDNFVSGEGGLKvYSPPTRFSYISVPK--LGPPLVPEV---PSKI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046557346 157 ALISRSHCTAKTEAFVAEHGLKdCISVGS-SLKFCMLAEGAADIY-PRFSRTMMWDTAAG 214
Cdd:cd01642   153 GIYEGSSRNPEKFLLLSRNGLK-FRSLGSaALELAYTCEGSFVLFlDLRGKLRNFDVAAA 211
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH