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Conserved domains on  [gi|1955878209|ref|XP_038897109|]
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PAP-specific phosphatase HAL2-like [Benincasa hispida]

Protein Classification

FIG domain-containing protein( domain architecture ID 299)

FIG (FBPase/IMPase/glpX-like) domain-containing protein belongs to a superfamily of metal-dependent phosphatases with various substrates; such as fructose-1,6-bisphosphatase (both the major and the glpX-encoded variant), inositol-monophosphatases and inositol polyphosphatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIG super family cl00289
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 6-379 2.19e-166

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+.


The actual alignment was detected with superfamily member TIGR01330:

Pssm-ID: 469707 [Multi-domain]  Cd Length: 353  Bit Score: 469.35  E-value: 2.19e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   6 YSKELDMAVRVVHLACALCRRVQKGLLEAGNSQIKAKDDDSPVTIADWSVQATVSWILSEYFGSKNvsIVAEEDVQTLSn 85
Cdd:TIGR01330   2 LERELDVATQAVRLASLLTKKVQSELISHKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDP--IVGEEDSSGLS- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  86 pDSRSLLSAVVKTVNECLAEAPKYGLQSPARELGTSEILEAISRCNSTGGPTGRHWVLDPVDGTLGFVRGDQYAVALALI 165
Cdd:TIGR01330  79 -EADFTLGRVNELVNETLVYAKNYKKDDQFPLKSLEDVLQIIDFGNYEGGRKGRHWVLDPIDGTKGFLRGDQYAVCLALI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 166 ENGKVVLGVLGCPNYPLKKECfhyhykvstlklSQPCSDTLEKGCVIYAKKScSGAWMQPLVHGdkklewPNSASLIQVS 245
Cdd:TIGR01330 158 ENGKVVLGVIGCPNLPLSSYG------------AQNLKGSESKGCIFRAVRG-SGAFMYSLSSD------AESPTKVHVS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 246 SIDDPALATFCEPVEKRNSNHSFTAGLAYSVGLRKQPLRVYSMVKYAAIARGDAEIFMKFARTG-YREKIWDHAAGVIIV 324
Cdd:TIGR01330 219 SVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPIKLsYQEKIWDHAAGNVIV 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1955878209 325 EAAGGVVTDAGGRPLDFSKGVYLEgLDRGIIVCSGP-ILHEKIIGAVYASWDSSNL 379
Cdd:TIGR01330 299 EEAGGIVTDAMGKPLDFGKGRTLA-LDKGVIAASGPrVLHDLVVSTSCDSIQSRNA 353
 
Name Accession Description Interval E-value
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 6-379 2.19e-166

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: 469.35  E-value: 2.19e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   6 YSKELDMAVRVVHLACALCRRVQKGLLEAGNSQIKAKDDDSPVTIADWSVQATVSWILSEYFGSKNvsIVAEEDVQTLSn 85
Cdd:TIGR01330   2 LERELDVATQAVRLASLLTKKVQSELISHKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDP--IVGEEDSSGLS- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  86 pDSRSLLSAVVKTVNECLAEAPKYGLQSPARELGTSEILEAISRCNSTGGPTGRHWVLDPVDGTLGFVRGDQYAVALALI 165
Cdd:TIGR01330  79 -EADFTLGRVNELVNETLVYAKNYKKDDQFPLKSLEDVLQIIDFGNYEGGRKGRHWVLDPIDGTKGFLRGDQYAVCLALI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 166 ENGKVVLGVLGCPNYPLKKECfhyhykvstlklSQPCSDTLEKGCVIYAKKScSGAWMQPLVHGdkklewPNSASLIQVS 245
Cdd:TIGR01330 158 ENGKVVLGVIGCPNLPLSSYG------------AQNLKGSESKGCIFRAVRG-SGAFMYSLSSD------AESPTKVHVS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 246 SIDDPALATFCEPVEKRNSNHSFTAGLAYSVGLRKQPLRVYSMVKYAAIARGDAEIFMKFARTG-YREKIWDHAAGVIIV 324
Cdd:TIGR01330 219 SVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPIKLsYQEKIWDHAAGNVIV 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1955878209 325 EAAGGVVTDAGGRPLDFSKGVYLEgLDRGIIVCSGP-ILHEKIIGAVYASWDSSNL 379
Cdd:TIGR01330 299 EEAGGIVTDAMGKPLDFGKGRTLA-LDKGVIAASGPrVLHDLVVSTSCDSIQSRNA 353
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-372 1.42e-101

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: 301.54  E-value: 1.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   9 ELDMAVRVVHLACALCRRVQKGLLEAGNSQikAKDDDSPVTIADWSVQATVSWILSEYFGSknVSIVAEEDVQTLsnpds 88
Cdd:cd01517     1 ELEVAILAVRAAASLTLPVFRNLGAGDVVW--KKSDKSPVTVADYGAQALITAALARLFPS--DPIVGEEDSAAL----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  89 rsllsavvktvneclaeapkyglqsparelgtseileaisrcnstggptGRHWVLDPVDGTLGFVRGDQYAVALALIENG 168
Cdd:cd01517    72 -------------------------------------------------GRFWVLDPIDGTKGFLRGDQFAVALALIEDG 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 169 KVVLGVLGCPNYPLKKEcfhyhykvstlklsqpcsdtlEKGCVIYAKKSCsGAWMQPLVHGdkklewpnSASLIQVSSID 248
Cdd:cd01517   103 EVVLGVIGCPNLPLDDG---------------------GGGDLFSAVRGQ-GAWLRPLDGS--------SLQPLSVRQLT 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 249 DPALATFCEPVEKRNSNHSFTAGLAYsVGLRKQPLRVYSMVKYAAIARGDAEIFMKFAR-TGYREKIWDHAAGVIIVEAA 327
Cdd:cd01517   153 NAARASFCESVESAHSSHRLQAAIKA-LGGTPQPVRLDSQAKYAAVARGAADFYLRLPLsMSYREKIWDHAAGVLIVEEA 231

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1955878209 328 GGVVTDAGGRPLDFSKGVYLeGLDRGIIVCSGpILHEKIIGAVYA 372
Cdd:cd01517   232 GGKVTDADGKPLDFGKGRKL-LNNGGLIAAPG-EIHEQVLEALRE 274
Inositol_P pfam00459
Inositol monophosphatase family;
44-374 3.64e-49

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 166.75  E-value: 3.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  44 DDSPVTIADWSVQATVSWILSEYFGSKnvsIVAEEDvqtlSNPDSRSLLSAVVKTVNECLAEApkygLQS--PARELGTS 121
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNK---LTIEEK----GKSGANDLVTAADKAAEELILEA----LAAlfPSHKIIGE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 122 EILEAISrcNSTGGPTGRHWVLDPVDGTLGFVRG-DQYAVALALIENGKVVLGVLGCPnyplkkecfhyhykvstlklsq 200
Cdd:pfam00459  70 EGGAKGD--QTELTDDGPTWIIDPIDGTKNFVHGiPQFAVSIGLAVNGEPVLGVIYQP---------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 201 pcsdtlEKGCVIYAKKSCsGAWM--QPL-VHGDKKLEWPNSASLIQVSSIDDPALATFCEPVEKRNSNHSFTaglaySVG 277
Cdd:pfam00459 126 ------FAGQLYSAAKGK-GAFLngQPLpVSRAPPLSEALLVTLFGVSSRKDTSEASFLAKLLKLVRAPGVR-----RVG 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 278 lrkqplrvYSMVKYAAIARGDAEIFMKFARtgyrEKIWDHAAGVIIVEAAGGVVTDAGGRPLDFskgvylegLDRGIIVC 357
Cdd:pfam00459 194 --------SAALKLAMVAAGKADAYIEFGR----LKPWDHAAGVAILREAGGVVTDADGGPFDL--------LAGRVIAA 253

                         330
                  ....*....|....*..
gi 1955878209 358 SGPILHEKIIGAVYASW 374
Cdd:pfam00459 254 NPKVLHELLAAALEEII 270
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 6-369 3.13e-43

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 151.08  E-value: 3.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   6 YSKELDMAVRVVHLACALCRRVQkglleAGNSQIKAKDDDSPVTIADWSVQATVSWILSEYFGskNVSIVAEEDVQTLSN 85
Cdd:COG1218     1 LEALLEAAIEIAREAGEAILEIY-----RADFEVEEKADDSPVTEADLAAHAIILAGLAALTP--DIPVLSEESAAIPYE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  86 PDSRSllsavvktvneclaeapkyglqsparelgtseileaiSRCnstggptgrhWVLDPVDGTLGFVRG-DQYAVALAL 164
Cdd:COG1218    74 ERKSW-------------------------------------DRF----------WLVDPLDGTKEFIKRnGEFTVNIAL 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 165 IENGKVVLGVLGCPNyplKKECFhyhykvstlklsqpcsdtlekgcviYAKKScSGAWMQPLVHGDKKlewpnsaslIQV 244
Cdd:COG1218   107 IEDGRPVLGVVYAPA---LGRLY-------------------------YAAKG-QGAFKETGGGERQP---------IRV 148

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 245 SSIDDPALATFCEpvekrNSNHSFTAGLAYSVGLR-KQPLRVYSMVKYAAIARGDAEIFMKFARTgyreKIWDHAAGVII 323
Cdd:COG1218   149 RDRPPAEPLRVVA-----SRSHRDEETEALLARLGvAELVSVGSSLKFCLVAEGEADLYPRLGPT----MEWDTAAGQAI 219

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1955878209 324 VEAAGGVVTDAGGRPLDFSKGvylEGLDRGIIVCSGPilHEKIIGA 369
Cdd:COG1218   220 LEAAGGRVTDLDGKPLRYNKK---EDLLNPGFIASGD--HAAILAA 260
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 139-342 5.60e-14

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 70.88  E-value: 5.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 139 RHWVLDPVDGTLGFV-RGDQYAVALALIENGKVVLGVLgcpnyplkkecfhyhYKvstlklsqPCSDTLEKGCVIYAKKS 217
Cdd:PRK10931   78 RYWLVDPLDGTKEFIkRNGEFTVNIALIEQGKPVLGVV---------------YA--------PVMNVMYSAAEGKAWKE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 218 CSGAWMQplvhgdkklewpnsaslIQVSSIDDPALAtfcepVEKRNSNHSFTAGLAySVGlRKQPLRVYSMVKYAAIARG 297
Cdd:PRK10931  135 ECGVRKQ-----------------IQVRDARPPLVV-----ISRSHADAELKEYLQ-QLG-EHQTTSIGSSLKFCLVAEG 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1955878209 298 DAEIFMKFARTgyreKIWDHAAGVIIVEAAGGVVTDAGGRPLDFS 342
Cdd:PRK10931  191 QAQLYPRFGPT----NIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
 
Name Accession Description Interval E-value
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 6-379 2.19e-166

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: 469.35  E-value: 2.19e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   6 YSKELDMAVRVVHLACALCRRVQKGLLEAGNSQIKAKDDDSPVTIADWSVQATVSWILSEYFGSKNvsIVAEEDVQTLSn 85
Cdd:TIGR01330   2 LERELDVATQAVRLASLLTKKVQSELISHKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDP--IVGEEDSSGLS- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  86 pDSRSLLSAVVKTVNECLAEAPKYGLQSPARELGTSEILEAISRCNSTGGPTGRHWVLDPVDGTLGFVRGDQYAVALALI 165
Cdd:TIGR01330  79 -EADFTLGRVNELVNETLVYAKNYKKDDQFPLKSLEDVLQIIDFGNYEGGRKGRHWVLDPIDGTKGFLRGDQYAVCLALI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 166 ENGKVVLGVLGCPNYPLKKECfhyhykvstlklSQPCSDTLEKGCVIYAKKScSGAWMQPLVHGdkklewPNSASLIQVS 245
Cdd:TIGR01330 158 ENGKVVLGVIGCPNLPLSSYG------------AQNLKGSESKGCIFRAVRG-SGAFMYSLSSD------AESPTKVHVS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 246 SIDDPALATFCEPVEKRNSNHSFTAGLAYSVGLRKQPLRVYSMVKYAAIARGDAEIFMKFARTG-YREKIWDHAAGVIIV 324
Cdd:TIGR01330 219 SVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPIKLsYQEKIWDHAAGNVIV 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1955878209 325 EAAGGVVTDAGGRPLDFSKGVYLEgLDRGIIVCSGP-ILHEKIIGAVYASWDSSNL 379
Cdd:TIGR01330 299 EEAGGIVTDAMGKPLDFGKGRTLA-LDKGVIAASGPrVLHDLVVSTSCDSIQSRNA 353
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-372 1.42e-101

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: 301.54  E-value: 1.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   9 ELDMAVRVVHLACALCRRVQKGLLEAGNSQikAKDDDSPVTIADWSVQATVSWILSEYFGSknVSIVAEEDVQTLsnpds 88
Cdd:cd01517     1 ELEVAILAVRAAASLTLPVFRNLGAGDVVW--KKSDKSPVTVADYGAQALITAALARLFPS--DPIVGEEDSAAL----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  89 rsllsavvktvneclaeapkyglqsparelgtseileaisrcnstggptGRHWVLDPVDGTLGFVRGDQYAVALALIENG 168
Cdd:cd01517    72 -------------------------------------------------GRFWVLDPIDGTKGFLRGDQFAVALALIEDG 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 169 KVVLGVLGCPNYPLKKEcfhyhykvstlklsqpcsdtlEKGCVIYAKKSCsGAWMQPLVHGdkklewpnSASLIQVSSID 248
Cdd:cd01517   103 EVVLGVIGCPNLPLDDG---------------------GGGDLFSAVRGQ-GAWLRPLDGS--------SLQPLSVRQLT 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 249 DPALATFCEPVEKRNSNHSFTAGLAYsVGLRKQPLRVYSMVKYAAIARGDAEIFMKFAR-TGYREKIWDHAAGVIIVEAA 327
Cdd:cd01517   153 NAARASFCESVESAHSSHRLQAAIKA-LGGTPQPVRLDSQAKYAAVARGAADFYLRLPLsMSYREKIWDHAAGVLIVEEA 231

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1955878209 328 GGVVTDAGGRPLDFSKGVYLeGLDRGIIVCSGpILHEKIIGAVYA 372
Cdd:cd01517   232 GGKVTDADGKPLDFGKGRKL-LNNGGLIAAPG-EIHEQVLEALRE 274
Inositol_P pfam00459
Inositol monophosphatase family;
44-374 3.64e-49

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 166.75  E-value: 3.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  44 DDSPVTIADWSVQATVSWILSEYFGSKnvsIVAEEDvqtlSNPDSRSLLSAVVKTVNECLAEApkygLQS--PARELGTS 121
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNK---LTIEEK----GKSGANDLVTAADKAAEELILEA----LAAlfPSHKIIGE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 122 EILEAISrcNSTGGPTGRHWVLDPVDGTLGFVRG-DQYAVALALIENGKVVLGVLGCPnyplkkecfhyhykvstlklsq 200
Cdd:pfam00459  70 EGGAKGD--QTELTDDGPTWIIDPIDGTKNFVHGiPQFAVSIGLAVNGEPVLGVIYQP---------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 201 pcsdtlEKGCVIYAKKSCsGAWM--QPL-VHGDKKLEWPNSASLIQVSSIDDPALATFCEPVEKRNSNHSFTaglaySVG 277
Cdd:pfam00459 126 ------FAGQLYSAAKGK-GAFLngQPLpVSRAPPLSEALLVTLFGVSSRKDTSEASFLAKLLKLVRAPGVR-----RVG 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 278 lrkqplrvYSMVKYAAIARGDAEIFMKFARtgyrEKIWDHAAGVIIVEAAGGVVTDAGGRPLDFskgvylegLDRGIIVC 357
Cdd:pfam00459 194 --------SAALKLAMVAAGKADAYIEFGR----LKPWDHAAGVAILREAGGVVTDADGGPFDL--------LAGRVIAA 253

                         330
                  ....*....|....*..
gi 1955878209 358 SGPILHEKIIGAVYASW 374
Cdd:pfam00459 254 NPKVLHELLAAALEEII 270
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 6-369 3.13e-43

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 151.08  E-value: 3.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   6 YSKELDMAVRVVHLACALCRRVQkglleAGNSQIKAKDDDSPVTIADWSVQATVSWILSEYFGskNVSIVAEEDVQTLSN 85
Cdd:COG1218     1 LEALLEAAIEIAREAGEAILEIY-----RADFEVEEKADDSPVTEADLAAHAIILAGLAALTP--DIPVLSEESAAIPYE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  86 PDSRSllsavvktvneclaeapkyglqsparelgtseileaiSRCnstggptgrhWVLDPVDGTLGFVRG-DQYAVALAL 164
Cdd:COG1218    74 ERKSW-------------------------------------DRF----------WLVDPLDGTKEFIKRnGEFTVNIAL 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 165 IENGKVVLGVLGCPNyplKKECFhyhykvstlklsqpcsdtlekgcviYAKKScSGAWMQPLVHGDKKlewpnsaslIQV 244
Cdd:COG1218   107 IEDGRPVLGVVYAPA---LGRLY-------------------------YAAKG-QGAFKETGGGERQP---------IRV 148

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 245 SSIDDPALATFCEpvekrNSNHSFTAGLAYSVGLR-KQPLRVYSMVKYAAIARGDAEIFMKFARTgyreKIWDHAAGVII 323
Cdd:COG1218   149 RDRPPAEPLRVVA-----SRSHRDEETEALLARLGvAELVSVGSSLKFCLVAEGEADLYPRLGPT----MEWDTAAGQAI 219

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1955878209 324 VEAAGGVVTDAGGRPLDFSKGvylEGLDRGIIVCSGPilHEKIIGA 369
Cdd:COG1218   220 LEAAGGRVTDLDGKPLRYNKK---EDLLNPGFIASGD--HAAILAA 260
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 10-370 7.18e-28

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: 109.93  E-value: 7.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  10 LDMAVRVVHLAcalcRRVQKGLLEAGNSQIKAKDDDSPVTIADWSVQATVSWILSEYFGskNVSIVAEEDVQTlsnpdsr 89
Cdd:COG0483     4 LELALRAARAA----GALILRRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFP--DHGILGEESGAS------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  90 sllsavvktvneclaeapkyglqsparelgtseileaisrcnsTGGPTGRHWVLDPVDGTLGFVRG-DQYAVALALIENG 168
Cdd:COG0483    71 -------------------------------------------EGRDSGYVWVIDPIDGTTNFVHGlPLFAVSIALVRDG 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 169 KVVLGVLgcpnY-PLKKECFHYhykvstlklsqpcsdtlEKGcviyakkscSGAWMqplvhGDKKlewpnsaslIQVSSI 247
Cdd:COG0483   108 EPVAGVV----YdPALGELFTA-----------------ARG---------GGAFL-----NGRR---------LRVSAR 143

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 248 DDPALATFCEPVEKRNSNHSFTAGLAysvGLRKQPLRVYSM----VKYAAIARGDAEIFMkfartGYREKIWDHAAGVII 323
Cdd:COG0483   144 TDLEDALVATGFPYLRDDREYLAALA---ALLPRVRRVRRLgsaaLDLAYVAAGRLDAFV-----EAGLKPWDIAAGALI 215

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1955878209 324 VEAAGGVVTDAGGRPLDfskgvylegLDRGIIVCSGPILHEKIIGAV 370
Cdd:COG0483   216 VREAGGVVTDLDGEPLD---------LGSGSLVAANPALHDELLALL 253
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 9-343 2.20e-25

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: 102.69  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209   9 ELDMAVRVVHLACALCRRVQKGLLEagnsqIKAKDDDSPVTIADwsvqATVSWILSEYFGS--KNVSIVAEEDVQtlsnp 86
Cdd:cd01638     1 LLELLIRIAREAGDAILEVYRGGFT-----VERKEDGSPVTAAD----LAANAFIVEGLAAlrPDIPVLSEESAD----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  87 dsrsllsavvktvneclaeapkyglqSPARElgtseileaisrcnstggPTGRHWVLDPVDGTLGFVRG-DQYAVALALI 165
Cdd:cd01638    67 --------------------------DPLRL------------------GWDRFWLVDPLDGTREFIKGnGEFAVNIALV 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 166 ENGKVVLGVLGCPnyplkkecfhyhykvstlklsqpcsdtlEKGCVIYAKKScSGAWMQPLvhgdkklewPNSASLIQVS 245
Cdd:cd01638   103 EDGRPVLGVVYAP----------------------------ALGELYYALRG-GGAYKNGR---------PGAVSLQARP 144

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 246 SIDDPALATfcepVEKRNSNHSFTAGLAysVGLRKQPLRVYSMVKYAAIARGDAEIFMKFARTgyreKIWDHAAGVIIVE 325
Cdd:cd01638   145 PPLQPLRVV----ASRSHPDEELEALLA--ALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPT----MEWDTAAGDAVLR 214

                         330
                  ....*....|....*...
gi 1955878209 326 AAGGVVTDAGGRPLDFSK 343
Cdd:cd01638   215 AAGGAVSDLDGSPLTYNR 232
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 138-344 1.46e-19

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: 86.60  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 138 GRHWVLDPVDGTLGFVRG-DQYAVALALIENGKVVLGVLGCpnyPLKKECFHYhykvstlklsqpcsdtlEKGCviyakk 216
Cdd:cd01637    74 GRVWVIDPIDGTTNFVAGlPNFAVSIALYEDGKPVLGVIYD---PMLDELYYA-----------------GRGK------ 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 217 scsGAWMqplvhGDKKLEWPNSASLiqvssiDDPALATfcepvekrNSNHSFTAGLAYSVGLRKQPLRVYSM----VKYA 292
Cdd:cd01637   128 ---GAFL-----NGKKLPLSKDTPL------NDALLST--------NASMLRSNRAAVLASLVNRALGIRIYgsagLDLA 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1955878209 293 AIARGDAEIFMKFartgyREKIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKG 344
Cdd:cd01637   186 YVAAGRLDAYLSS-----GLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNR 232
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 131-347 2.74e-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: 74.68  E-value: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 131 NSTGGPTGRHWVLDPVDGTLGFVRGDQY-AVALALIENGKVVLGVLgcpNYPLKKECFHyhykvstlklsqpcsdtlekg 209
Cdd:cd01643    64 GGIFPSSGWYWVIDPIDGTTNFARGIPIwAISIALLYRGEPVFGVI---ALPALNQTFV--------------------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 210 cviyakkscsGAWMQPLVHGDKKLEWPNSASLiqvssiddPALATFCepvekrNSNHSFTAGLAYSVGLRKQP--LRVYS 287
Cdd:cd01643   120 ----------AFKGGGAFLNGKPLALHPPLQL--------PDCNVGF------NRSSRASARAVLRVILRRFPgkIRMLG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955878209 288 MVKY--AAIARGdaeifmkfaRT-GYRE---KIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKGVYL 347
Cdd:cd01643   176 SASLnlASVAAG---------QTlGYVEatpKIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYL 232
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 38-364 7.98e-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: 73.44  E-value: 7.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  38 QIKAKDDDSPVTIADWSvqatvswilseyfgsknvsivAEEDVqtlsnpdsRSLLSAvvktvneclaEAPKYGLqspARE 117
Cdd:cd01641    25 QVETKADFSPVTEADRA---------------------AEAAM--------RELIAA----------AFPDHGI---LGE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 118 LGTSEileaisrcnstGGPTGRHWVLDPVDGTLGFVRG-DQYAVALALIENGKVVLGVLgcpNYPLKKECFhyhykvstl 196
Cdd:cd01641    63 EFGNE-----------GGDAGYVWVLDPIDGTKSFIRGlPVWGTLIALLHDGRPVLGVI---DQPALGERW--------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 197 klsqpCSDTlekgcviyakkscSGAWMQPLVHGDKklewpnsaslIQVSSIDDPALATFcepvekrnsnhSFTAGLAYSV 276
Cdd:cd01641   120 -----IGAR-------------GGGTFLNGAGGRP----------LRVRACADLAEAVL-----------STTDPHFFTP 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 277 GLRKQPLRVYSMVK----------YAAIARGDAEIFMKFARtgyreKIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKGVy 346
Cdd:cd01641   161 GDRAAFERLARAVRltryggdcyaYALVASGRVDLVVEAGL-----KPYDVAALIPIIEGAGGVITDWDGGPLTGGSGR- 234

                         330
                  ....*....|....*...
gi 1955878209 347 legldrgIIVCSGPILHE 364
Cdd:cd01641   235 -------VVAAGDAELHE 245
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 139-342 5.60e-14

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 70.88  E-value: 5.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 139 RHWVLDPVDGTLGFV-RGDQYAVALALIENGKVVLGVLgcpnyplkkecfhyhYKvstlklsqPCSDTLEKGCVIYAKKS 217
Cdd:PRK10931   78 RYWLVDPLDGTKEFIkRNGEFTVNIALIEQGKPVLGVV---------------YA--------PVMNVMYSAAEGKAWKE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 218 CSGAWMQplvhgdkklewpnsaslIQVSSIDDPALAtfcepVEKRNSNHSFTAGLAySVGlRKQPLRVYSMVKYAAIARG 297
Cdd:PRK10931  135 ECGVRKQ-----------------IQVRDARPPLVV-----ISRSHADAELKEYLQ-QLG-EHQTTSIGSSLKFCLVAEG 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1955878209 298 DAEIFMKFARTgyreKIWDHAAGVIIVEAAGGVVTDAGGRPLDFS 342
Cdd:PRK10931  191 QAQLYPRFGPT----NIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
142-374 6.65e-09

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 57.43  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 142 VLDPVDGTLGFVRG-DQYAVALALienGKVVLGVLGCPNYPLKKecfhyhYKVSTLKLSqpCSDTLEKGCVIYAKKScSG 220
Cdd:PRK14076   85 VLDPIDGTYNALKDiPIYSASIAI---AKIDGFDKKIKEFIGKN------LTINDLEVG--VVKNIATGDTYYAEKG-EG 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 221 AWMqpLVHGDKKLEWPNSASLIQVSSIDdpalatfcepvekrnsnhSFTAGLAYSV-----GLRKQPLRVY-SMV-KYAA 293
Cdd:PRK14076  153 AYL--LKKGEKKKIEISNISNLKDASIG------------------LFAYGLSLDTlkfikDRKVRRIRLFgSIAlEMCY 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 294 IARGDAEIFMKFARTgyrEKIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKGVYleglDRGIIVCSGPILHEKIIGAVYAS 373
Cdd:PRK14076  213 VASGALDAFINVNET---TRLCDIAAGYVICKEAGGIITNKNGKPLNMKLDIN----EKTSVICSNEILHKKLVGIFGNK 285


                  .
gi 1955878209 374 W 374
Cdd:PRK14076  286 W 286
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
142-367 6.79e-08

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 52.99  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 142 VLDPVDGTLGFVRGDQ-YAVALALIENGKVVLGvlgcpnyplkkecfhYHYKVSTlklsqpcsdtlekGCVIYAKKScSG 220
Cdd:PRK12676   85 VLDPLDGTYNAINGIPfYAISIAVFKGGKPVYG---------------YVYNLAT-------------GDFYEAIPG-KG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 221 AWMQplvhgDKKlewpnsaslIQVSSIDDpaLATFCEpvekrnSNHSFTAGLAYSVGLRKQPLRVYSM----VKYAAIAR 296
Cdd:PRK12676  136 AYLN-----GKP---------IKVSKTSE--LNESAV------SIYGYRRGKERTVKLGRKVRRVRILgaiaLELCYVAS 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955878209 297 GDAEIFMKFARTgyrEKIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKGVyLEGLDrgIIVCSGPILHEKII 367
Cdd:PRK12676  194 GRLDAFVDVRNY---LRVTDIAAGKLICEEAGGIVTDEDGNELKLPLNV-TERTN--LIAANGEELHKKIL 258
PLN02737 PLN02737
inositol monophosphatase family protein
 310-367 1.92e-07

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 52.49  E-value: 1.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1955878209 310 YREKIWDHAAGVIIVEAAGGVVTDAGGRPldFSkgVYleglDRGIIVCSGpILHEKII 367
Cdd:PLN02737  285 YRLKPWDMAAGVLIVEEAGGTVTRMDGGK--FS--VF----DRSVLVSNG-VLHPKLL 333
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 135-366 8.42e-07

histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273949 [Multi-domain]  Cd Length: 251  Bit Score: 49.61  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 135 GPTGRH-WVLDPVDGTLGFVRGDQYAVAL-ALIENGKVVLGVLgcpNYPLKKECFhyhykvstlklsqpcsdtlekgcvi 212
Cdd:TIGR02067  70 EGDAERvWVLDPIDGTKSFIRGVPVWGTLiALVEGGMPVLGVI---FQPATGERW------------------------- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 213 YAKKScSGAWmqplvhgdkklewpNSASLIQVSSIDDPALATFcepvekrnsnHSFTAGLAYSVGLRKQPLRVYSMVK-- 290
Cdd:TIGR02067 122 WAAGG-GAAF--------------LGGRRLRVSSCANLSDAVL----------FTTSPDLLDDPGNRPAFERLRRAARlt 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 291 --------YAAIARGDAEIFMKFARtgyreKIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKgvylegldrGIIVCSGPIL 362
Cdd:TIGR02067 177 ryggdcyaYLMVAGGAVDIVVEPGL-----SPWDIAALIPVIEEAGGCFTDWDGKPAPDGG---------GAVAAGNAML 242


                  ....
gi 1955878209 363 HEKI 366
Cdd:TIGR02067 243 HDEA 246
PLN02911 PLN02911
inositol-phosphate phosphatase
 38-369 8.17e-06

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 47.02  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209  38 QIKAKDDDSPVTIADWSVQATVSWILSEYFGSKnvSIVAEEdvqtlsnpdsrsllsavvktvneclaeapkYGLQSPAre 117
Cdd:PLN02911   60 EIIDKEDLSPVTIADRAAEEAMRSIILENFPSH--AIFGEE------------------------------HGLRCGE-- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 118 lGTSEILeaisrcnstggptgrhWVLDPVDGTLGFVRGDQ-YAVALALIENGKVVLGVLGCPnyPLKKECFHYHYKVSTL 196
Cdd:PLN02911  106 -GSSDYV----------------WVLDPIDGTKSFITGKPlFGTLIALLYKGKPVLGIIDQP--VLKERWVGVAGRATTL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 197 KlSQPCSdtlekgcviyaKKSCsgawmqplvhgdkklewpnsasliqvSSIDDPALATfcepvekrNSNHSFT--AGLAY 274
Cdd:PLN02911  167 N-GEEIS-----------TRSC--------------------------ASLKDAYLYT--------TSPHMFSgdAEDAF 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955878209 275 SvglrkqplRVYSMVK----------YAAIARGDAEIFMKfarTGYreKIWDHAAGVIIVEAAGGVVTDAGGRPLDFSKG 344
Cdd:PLN02911  201 A--------RVRDKVKvplygcdcyaYGLLASGHVDLVVE---SGL--KPYDYLALVPVVEGAGGVITDWKGRKLRWEPS 267

                         330       340
                  ....*....|....*....|....*
gi 1955878209 345 VYLEGLDRGIIVCSGPILHEKIIGA 369
Cdd:PLN02911  268 PGSLATSFNVVAAGDARLHKQALDI 292
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 289-334 3.50e-04

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: 41.22  E-value: 3.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1955878209 289 VKYAAIARGDAEIFMkfaRTGYREKIWDHAAGVIIVEAAGGVVTDA 334
Cdd:cd01636   142 AKMCLVALGLADIYY---EPGGKRRAWDVAASAAIVREAGGIMTDW 184
 
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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