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Conserved domains on  [gi|1123393974|gb|OKY19285|]
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3'(2'),5'-bisphosphate nucleotidase CysQ [Campylobacter jejuni]

Protein Classification

3'(2'),5'-bisphosphate nucleotidase CysQ( domain architecture ID 10108147)

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

CATH:  3.40.190.80|3.30.540.10
EC:  3.1.3.7
Gene Ontology:  GO:0008441|GO:0006790|GO:0000287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 8-243 3.09e-78

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: 235.97  E-value: 3.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILEERKNFKT-WEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEEcEELKTFWLID 84
Cdd:cd01638     2 LELLIRIAREAGDAILEVYRGGFTvERKEDGSPVTAADLAANAFIVEGLAALrpDIPVLSEESADDPLR-LGWDRFWLVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  85 PLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQID--QQEYEKNKYKALLSVNHLS 162
Cdd:cd01638    81 PLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSlqARPPPLQPLRVVASRSHPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 163 KEDEDF-AKEHQLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYSPLNYKSSPF 241
Cdd:cd01638   161 EELEALlAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDFLNPDF 240


                  ..
gi 1123393974 242 IC 243
Cdd:cd01638   241 IA 242
 
Name Accession Description Interval E-value
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 8-243 3.09e-78

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: 235.97  E-value: 3.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILEERKNFKT-WEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEEcEELKTFWLID 84
Cdd:cd01638     2 LELLIRIAREAGDAILEVYRGGFTvERKEDGSPVTAADLAANAFIVEGLAALrpDIPVLSEESADDPLR-LGWDRFWLVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  85 PLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQID--QQEYEKNKYKALLSVNHLS 162
Cdd:cd01638    81 PLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSlqARPPPLQPLRVVASRSHPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 163 KEDEDF-AKEHQLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYSPLNYKSSPF 241
Cdd:cd01638   161 EELEALlAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDFLNPDF 240


                  ..
gi 1123393974 242 IC 243
Cdd:cd01638   241 IA 242
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 4-248 1.86e-71

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 219.26  E-value: 1.86e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   4 LDKFLEIAINASNQASKAILE-ERKNFKTWEKEDKSPLTSADLASNKILNDILGS--TDIKILSEE-KLLSKEECEELKT 79
Cdd:COG1218     1 LEALLEAAIEIAREAGEAILEiYRADFEVEEKADDSPVTEADLAAHAIILAGLAAltPDIPVLSEEsAAIPYEERKSWDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  80 FWLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKND-----KPLQIDQQEyEKNKYKA 154
Cdd:COG1218    81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerQPIRVRDRP-PAEPLRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 155 LLSVNHLSKEDEDFAKEH-QLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYS- 232
Cdd:COG1218   160 VASRSHRDEETEALLARLgVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNk 239

                         250
                  ....*....|....*.
gi 1123393974 233 PLNYKSSPFICVSSRN 248
Cdd:COG1218   240 KEDLLNPGFIASGDHA 255
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 8-236 1.02e-40

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: 140.28  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILE-ERKNFKTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEE-KLLSKEECEELKTFWLI 83
Cdd:TIGR01331   2 LDDVIKIARAAGEEILPvYQKELAVAQKADNSPVTEADRAAHRFILEGLRALtpDIPVLSEEdASIPLTPRQTWQRFWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  84 DPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYK----NDKPLQIDQQEYEKNKYKALLSVN 159
Cdd:TIGR01331  82 DPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegdgQALKAPIHVRPWPSGPLLVVISRS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123393974 160 HLSKEDEDFAKEH-QLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSkkyilYSPLNY 236
Cdd:TIGR01331 162 HAEEKTTEYLANLgYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLD-----GSPLLY 234
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 8-233 1.50e-36

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 129.43  E-value: 1.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILE---ERKNFKTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEELKTFWL 82
Cdd:PRK10931    2 LEQICQLARNAGDAIMQvydGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLtpDIPVLSEEDPPAWEVRQHWQRYWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  83 IDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKgDIFYAHAKTKVYKNDKPLQIDQQEYEKNKYKALLSVNHLS 162
Cdd:PRK10931   82 VDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVM-NVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123393974 163 KEDEDFAK---EHQleAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYSP 233
Cdd:PRK10931  161 AELKEYLQqlgEHQ--TTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTP 232
Inositol_P pfam00459
Inositol monophosphatase family;
3-225 5.39e-36

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 128.62  E-value: 5.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   3 NLDKFLEIAINASNQASKAILEERKNFKTWEKEDKS----PLTSADLASNKILNDILGST--DIKILSEEKLlSKEECEE 76
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSgandLVTAADKAAEELILEALAALfpSHKIIGEEGG-AKGDQTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  77 LK---TFWLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQIDQQEYEKNKY- 152
Cdd:pfam00459  80 LTddgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 153 ---KALLSVNHLSKEDEDFAKE---HQLEAINIGS-GLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFS 225
Cdd:pfam00459 160 vtlFGVSSRKDTSEASFLAKLLklvRAPGVRRVGSaALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDAD 239
 
Name Accession Description Interval E-value
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 8-243 3.09e-78

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: 235.97  E-value: 3.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILEERKNFKT-WEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEEcEELKTFWLID 84
Cdd:cd01638     2 LELLIRIAREAGDAILEVYRGGFTvERKEDGSPVTAADLAANAFIVEGLAALrpDIPVLSEESADDPLR-LGWDRFWLVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  85 PLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQID--QQEYEKNKYKALLSVNHLS 162
Cdd:cd01638    81 PLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSlqARPPPLQPLRVVASRSHPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 163 KEDEDF-AKEHQLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYSPLNYKSSPF 241
Cdd:cd01638   161 EELEALlAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDFLNPDF 240


                  ..
gi 1123393974 242 IC 243
Cdd:cd01638   241 IA 242
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 4-248 1.86e-71

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 219.26  E-value: 1.86e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   4 LDKFLEIAINASNQASKAILE-ERKNFKTWEKEDKSPLTSADLASNKILNDILGS--TDIKILSEE-KLLSKEECEELKT 79
Cdd:COG1218     1 LEALLEAAIEIAREAGEAILEiYRADFEVEEKADDSPVTEADLAAHAIILAGLAAltPDIPVLSEEsAAIPYEERKSWDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  80 FWLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKND-----KPLQIDQQEyEKNKYKA 154
Cdd:COG1218    81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerQPIRVRDRP-PAEPLRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 155 LLSVNHLSKEDEDFAKEH-QLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYS- 232
Cdd:COG1218   160 VASRSHRDEETEALLARLgVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNk 239

                         250
                  ....*....|....*.
gi 1123393974 233 PLNYKSSPFICVSSRN 248
Cdd:COG1218   240 KEDLLNPGFIASGDHA 255
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 8-236 1.02e-40

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: 140.28  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILE-ERKNFKTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEE-KLLSKEECEELKTFWLI 83
Cdd:TIGR01331   2 LDDVIKIARAAGEEILPvYQKELAVAQKADNSPVTEADRAAHRFILEGLRALtpDIPVLSEEdASIPLTPRQTWQRFWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  84 DPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYK----NDKPLQIDQQEYEKNKYKALLSVN 159
Cdd:TIGR01331  82 DPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegdgQALKAPIHVRPWPSGPLLVVISRS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123393974 160 HLSKEDEDFAKEH-QLEAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSkkyilYSPLNY 236
Cdd:TIGR01331 162 HAEEKTTEYLANLgYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLD-----GSPLLY 234
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 8-233 1.50e-36

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 129.43  E-value: 1.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILE---ERKNFKTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEELKTFWL 82
Cdd:PRK10931    2 LEQICQLARNAGDAIMQvydGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLtpDIPVLSEEDPPAWEVRQHWQRYWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  83 IDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKgDIFYAHAKTKVYKNDKPLQIDQQEYEKNKYKALLSVNHLS 162
Cdd:PRK10931   82 VDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVM-NVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123393974 163 KEDEDFAK---EHQleAINIGSGLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFSKKYILYSP 233
Cdd:PRK10931  161 AELKEYLQqlgEHQ--TTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTP 232
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 8-225 3.54e-36

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: 128.20  E-value: 3.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILEERKNFKTWE--KEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEElKTFWLI 83
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELTVEtkKGDGDLVTEADLAAEELIVDVLKALfpDDGILGEEGGGSGNVSDG-GRVWVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  84 DPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQIDQqeyEKNKYKALLSVN-HLS 162
Cdd:cd01637    80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSK---DTPLNDALLSTNaSML 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123393974 163 KEDEDFAKEHQLEAI----NIGS-GLKFCAILEARAGVYKRFEkLNIWDIVAGDFLINQNGGFMGDFS 225
Cdd:cd01637   157 RSNRAAVLASLVNRAlgirIYGSaGLDLAYVAAGRLDAYLSSG-LNPWDYAAGALIVEEAGGIVTDLD 223
Inositol_P pfam00459
Inositol monophosphatase family;
3-225 5.39e-36

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 128.62  E-value: 5.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   3 NLDKFLEIAINASNQASKAILEERKNFKTWEKEDKS----PLTSADLASNKILNDILGST--DIKILSEEKLlSKEECEE 76
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSgandLVTAADKAAEELILEALAALfpSHKIIGEEGG-AKGDQTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  77 LK---TFWLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQIDQQEYEKNKY- 152
Cdd:pfam00459  80 LTddgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 153 ---KALLSVNHLSKEDEDFAKE---HQLEAINIGS-GLKFCAILEARAGVYKRFEKLNIWDIVAGDFLINQNGGFMGDFS 225
Cdd:pfam00459 160 vtlFGVSSRKDTSEASFLAKLLklvRAPGVRRVGSaALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDAD 239
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 5-224 2.25e-35

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: 126.50  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   5 DKFLEIAINASNQASKAILE--ERKNFKTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEELktF 80
Cdd:COG0483     1 HPLLELALRAARAAGALILRrfRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAfpDHGILGEESGASEGRDSGY--V 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  81 WLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQIDQQEYEKNkykALLSVNH 160
Cdd:COG0483    79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLED---ALVATGF 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123393974 161 lSKEDEDFAKEHQLEAI--------NIGS-GLKFCAILEARAGVYkrFE-KLNIWDIVAGDFLINQNGGFMGDF 224
Cdd:COG0483   156 -PYLRDDREYLAALAALlprvrrvrRLGSaALDLAYVAAGRLDAF--VEaGLKPWDIAAGALIVREAGGVVTDL 226
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 30-232 1.25e-30

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: 114.72  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  30 KTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEEkllskeECEELKTFWLIDPLDGTSGFLKGsDEFCVMISLVH 107
Cdd:cd01517    28 VVWKKSDKSPVTVADYGAQALITAALARLfpSDPIVGEE------DSAALGRFWVLDPIDGTKGFLRG-DQFAVALALIE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 108 DNRPVLSLIQNP-------SKGDIFYAHAKTKVY-----KNDKPLQIDQQEYEKNKYKALLSVNHLSKEDEDFAKEHQLE 175
Cdd:cd01517   101 DGEVVLGVIGCPnlplddgGGGDLFSAVRGQGAWlrpldGSSLQPLSVRQLTNAARASFCESVESAHSSHRLQAAIKALG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123393974 176 ----AINIGSGLKFCAILEARAGVYKRF-----EKLNIWDIVAGDFLINQNGGFMGDFSKKYILYS 232
Cdd:cd01517   181 gtpqPVRLDSQAKYAAVARGAADFYLRLplsmsYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFG 246
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 7-227 1.24e-23

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: 95.30  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   7 FLEIAINASNQASKAILEERKNFKTwEKEDKS----PLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEELKtf 80
Cdd:cd01639     1 LLNIAIEAARKAGEILLEAYEKLGL-NVEEKGspvdLVTEVDKAVEKLIIEILKKAypDHGFLGEESGAAGGLTDEPT-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  81 WLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAhAKTK-VYKNDKPLQI-DQQEYEknkyKALLSV 158
Cdd:cd01639    78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTA-VRGQgAFLNGRRIRVsGRKELK----DALVAT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 159 NHLSKEDEDFAKE----HQLEAINI------GS-GLKFCAILEARAGVYkrFE-KLNIWDIVAGDFLINQNGGFMGDFSK 226
Cdd:cd01639   153 GFPYDRGDNFDRYlnnfAKLLAKAVrgvrrlGSaALDLAYVAAGRLDGY--WErGLKPWDVAAGALIVREAGGLVTDFDG 230


                  .
gi 1123393974 227 K 227
Cdd:cd01639   231 G 231
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 8-224 1.59e-15

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: 72.43  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILEERKNFKTWE----KEDKSPLTSADLASNKILNDILGST--DIKILSEE-KLLSKEECEELKTF 80
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFGRELSGKvkitKSDNDPVTTADVAAETLIRNMLKSSfpDVKIVGEEsGVAEEVMGRRDEYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  81 WLIDPLDGTSGFLKGSDEFCVMISLvhdnrpvlsliqnpskgdifyahaktkvykndkplqidqqeyeknkYKALLSVN- 159
Cdd:cd01636    81 WVIDPIDGTKNFINGLPFVAVVIAV----------------------------------------------YVILILAEp 114

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 160 HLSKEDEDFAKEHQLE----AINIGSGLKFCAILEARAGVYKRFE-KLNIWDIVAGDFLINQNGGFMGDF 224
Cdd:cd01636   115 SHKRVDEKKAELQLLAvyriRIVGSAVAKMCLVALGLADIYYEPGgKRRAWDVAASAAIVREAGGIMTDW 184
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 34-129 7.03e-15

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: 71.90  E-value: 7.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  34 KEDKSPLTSADLASNKILNDILGST--DIKILSEEKllsKEECEELKTFWLIDPLDGTSGFLKGSDEFCVMISLVHDNRP 111
Cdd:cd01641    29 KADFSPVTEADRAAEAAMRELIAAAfpDHGILGEEF---GNEGGDAGYVWVLDPIDGTKSFIRGLPVWGTLIALLHDGRP 105

                          90
                  ....*....|....*...
gi 1123393974 112 VLSLIQNPSKGDIFYAHA 129
Cdd:cd01641   106 VLGVIDQPALGERWIGAR 123
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 33-219 7.25e-15

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: 71.60  E-value: 7.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  33 EKEDKSPLTSADLASNKILNDILGST--DIKILSEEKL---LSKEECeelktfWLIDPLDGTSGFLKGSDEFCVMISLVH 107
Cdd:cd01643    27 TKADGSLVTAADRWVEQLIRARLAAQfpDDGVLGEEGGgifPSSGWY------WVIDPIDGTTNFARGIPIWAISIALLY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 108 DNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQIDQQEYEKNkykallsVNHLSKEDEDFAKEHQLEAIN--------- 178
Cdd:cd01643   101 RGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPD-------CNVGFNRSSRASARAVLRVILrrfpgkirm 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1123393974 179 IGSG-LKFCAILEARAGVYkrFEKL-NIWDIVAGdFLINQNGG 219
Cdd:cd01643   174 LGSAsLNLASVAAGQTLGY--VEATpKIWDIAAA-WVILREAG 213
PLN02911 PLN02911
inositol-phosphate phosphatase
 4-119 3.06e-13

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 67.82  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   4 LDKFLEIAINASNQASKAILEE-RKNFKTWEKEDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEEcEELKTF 80
Cdd:PLN02911   33 LDRFVDVAHKLADAAGEVTRKYfRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENfpSHAIFGEEHGLRCGE-GSSDYV 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1123393974  81 WLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNP 119
Cdd:PLN02911  112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQP 150
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 8-234 2.43e-11

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: 62.34  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILEER-KNFKTWEKEDKS---PLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEELKTF- 80
Cdd:cd01640     6 LAVAEKAGGIARDVVKKGRlLILLVEGKTKEGandFKTLADRLSQRVIKHSLQKQfpKLKIIGEEDNEFENQEDESRDVd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  81 ------------------------WlIDPLDGTSGFLKGSDEFC-VMISLVHDNRPVLSLIQNPskgdiFYahaktkvyk 135
Cdd:cd01640    86 ldeeileescpspskdlpeedlgvW-VDPLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQP-----FY--------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 136 ndkplqiDQQEYEKNKYKALL-SVNHLSKEDEDFA------------------KEHQLEAINI--------GSGLKFCAI 188
Cdd:cd01640   151 -------EKTAGAGAWLGRTIwGLSGLGAHSSDFKeredagkiivstshshsvKEVQLITAGNkdevlragGAGYKVLQV 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1123393974 189 LEARAGVY---KRFEKLniWDIVAGDFLINQNGGFMGDFSKKYILYSPL 234
Cdd:cd01640   224 LEGLADAYvhsTGGIKK--WDICAPEAILRALGGDMTDLHGEPLSYSKA 270
PLN02553 PLN02553
inositol-phosphate phosphatase
 4-227 5.14e-11

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 61.24  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   4 LDKFLEIAINASNQASKAIleeRKNFKTWEK-EDK---SPLTSADLASNKILNDILGST--DIKILSEE-------KLLS 70
Cdd:PLN02553    7 LEQFLEVAVDAAKAAGQII---RKGFYQTKHvEHKgqvDLVTETDKACEDLIFNHLKQAfpSHKFIGEEttaasggTELT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  71 KEECeelktfWLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQIDQQEyekN 150
Cdd:PLN02553   84 DEPT------WIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQS---E 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 151 KYKALLSVNHLSKEDedfakEHQLEA----IN-----------IGS-GLKFCAILEARAGVykrFEKLNI---WDIVAGD 211
Cdd:PLN02553  155 LGKALLATEVGTKRD-----KATVDAttnrINallykvrslrmSGScALNLCGVACGRLDI---FYEIGFggpWDVAAGA 226

                         250
                  ....*....|....*.
gi 1123393974 212 FLINQNGGFMGDFSKK 227
Cdd:PLN02553  227 VIVKEAGGLVFDPSGG 242
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 7-223 2.40e-10

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: 59.31  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   7 FLEIAINASNQASKAIleerKNFKTWEKEDKSPLTSAD---------LASNKILNDILGSTDIKILSEEkLLSKEECEEL 77
Cdd:cd01515     1 WLEIARNIAKEIEKAI----KPLFGTEDASEVVKIGADgtptklidkVAEDAAIEILKKLGSVNIVSEE-IGVIDNGDEP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  78 KTFWLIDPLDGTSGFLKGSDEF--CVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKplQIDQQEYEKNKYKAL 155
Cdd:cd01515    76 EYTVVLDPLDGTYNAINGIPFYsvSVAVFKIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGK--RIKVSDFSSLKSISV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1123393974 156 LSVNHLSKEDEDFAKEHQLEAINI-GS-GLKFCAILEAR--AGVYKRfEKLNIWDIVAGDFLINQNGGFMGD 223
Cdd:cd01515   154 SYYIYGKNHDRTFKICRKVRRVRIfGSvALELCYVASGAldAFVDVR-ENLRLVDIAAGYLIAEEAGGIVTD 224
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
6-142 6.61e-10

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 58.00  E-value: 6.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   6 KFLEIAINASNQASKAIL------EERKNFKTweKEDKSPLTSADLASNKILNDILGSTD--IKILSEEKLLSKEECEEL 77
Cdd:PRK12676    5 EWLEICDDMAKEVEKAIMplfgtpDAGETVGM--GADGTPTKLIDKVAEDIILEVLKPLGrcVNIISEELGEIVGNGPEY 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123393974  78 KTFwlIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLQI 142
Cdd:PRK12676   83 TVV--LDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKV 145
PRK10757 PRK10757
inositol-1-monophosphatase;
8-224 1.42e-07

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 50.96  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   8 LEIAINASNQASKAILeerKNFKTWEKEDKSPLTSADLASN------KILNDILGSTDIK--ILSEEKllSKEECEELKT 79
Cdd:PRK10757    5 LNIAVRAARKAGNLIA---KNYETPDAVEASQKGSNDFVTNvdkaaeAVIIDTIRKSYPQhtIITEES--GELEGEDQDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  80 FWLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGDIFYAHAKTKVYKNDKPLqidQQEYEKNKYKALLSVN 159
Cdd:PRK10757   80 QWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRL---RGSTARDLDGTILATG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974 160 HLSKededfAKEHQLEAINIGSGL-KFCAILEaRAG-------------VYKRFE-KLNIWDIVAGDFLINQNGGFMGDF 224
Cdd:PRK10757  157 FPFK-----AKQHATTYINIVGKLfTECADFR-RTGsaaldlayvaagrVDGFFEiGLKPWDFAAGELLVREAGGIVSDF 230
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 7-114 1.31e-03

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: 38.97  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974   7 FLEIAINASNQASKAILEerKNFKTWEK----EDKSPLTSADLASNKILNDILGST--DIKILSEEKLLSKEECEElKTF 80
Cdd:cd01642     1 MLEVLEKITKEIILLLNE--KNRQGLVKlirgAGGDVTRVADLKAEEIILKLLREEgvFGQIISEESGEIRKGSGE-YIA 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1123393974  81 wLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLS 114
Cdd:cd01642    78 -VLDPLDGSTNYLSGIPFYSVSVALADPRSKVKA 110
PLN02737 PLN02737
inositol monophosphatase family protein
 81-144 1.48e-03

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 39.40  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123393974  81 WLIDPLDGTSGFLKGSDEFCVMISLVHDNRPVLSLIQNPSKGD------IFYAHAKTKVYKNDKPLQIDQ 144
Cdd:PLN02737  154 WCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPmcwntrTFSASAGGGAFCNGQKIHVSQ 223
 
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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