|
Name |
Accession |
Description |
Interval |
E-value |
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
3-335 |
5.52e-134 |
|
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: 385.76 E-value: 5.52e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 3 YEKELAAAKKAVSLAARLSQEVQKSLLQSD---VRSKSDKSPVTAADYGSQAVISHVLERELHPEPLylVAEENAEDLHK 79
Cdd:TIGR01330 2 LERELDVATQAVRLASLLTKKVQSELISHKdstVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPI--VGEEDSSGLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 80 NGaeEFLESITKLVNNALASDDSYAN----SSLSMDDVRKAIDHGRSQGGSSGRHWILDPVDGTRGFVKGEEYAVALALL 155
Cdd:TIGR01330 80 AD--FTLGRVNELVNETLVYAKNYKKddqfPLKSLEDVLQIIDFGNYEGGRKGRHWVLDPIDGTKGFLRGDQYAVCLALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 156 VEGKVVLGVMACPKL-------ENHKSSSS-GCLFFATVGEGAYVQSLEGDSHPPQKVQVSNIENPEEATFVESSHKPIP 227
Cdd:TIGR01330 158 ENGKVVLGVIGCPNLplssygaQNLKGSESkGCIFRAVRGSGAFMYSLSSDAESPTKVHVSSVKDTKDAIFCEGVEKGHS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 228 IH---SSIANKLGIKAPPLRIHSQVKYAALARGDAEIYLRFTLKG-YREFIWNHAAGAIITTEAGGVVCDADGNPLDFSR 303
Cdd:TIGR01330 238 SHdeqTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPIKLsYQEKIWDHAAGNVIVEEAGGIVTDAMGKPLDFGK 317
|
330 340 350
....*....|....*....|....*....|....
gi 1032280832 304 GNHLEHKTGIVVSTKN--LMPRLLKAIRESIEEE 335
Cdd:TIGR01330 318 GRTLALDKGVIAASGPrvLHDLVVSTSCDSIQSR 351
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
6-330 |
6.06e-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: 298.46 E-value: 6.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 6 ELAAAKKAVSLAARLSQEVQKSLLQSDVR-SKSDKSPVTAADYGSQAVISHVLERELHPEPLylVAEENAEDLhkngaee 84
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGAGDVVwKKSDKSPVTVADYGAQALITAALARLFPSDPI--VGEEDSAAL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 85 flesitklvnnalasddsyansslsmddvrkaidhgrsqggssGRHWILDPVDGTRGFVKGEEYAVALALLVEGKVVLGV 164
Cdd:cd01517 72 -------------------------------------------GRFWVLDPIDGTKGFLRGDQFAVALALIEDGEVVLGV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 165 MACPKLeNHKSSSSGCLFFATVGEGAYVQSLEGdsHPPQKVQVSNIENPEEATF---VESSHKPIPIHSSIaNKLGIKAP 241
Cdd:cd01517 109 IGCPNL-PLDDGGGGDLFSAVRGQGAWLRPLDG--SSLQPLSVRQLTNAARASFcesVESAHSSHRLQAAI-KALGGTPQ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 242 PLRIHSQVKYAALARGDAEIYLRFTLK-GYREFIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHLEHKTGIVVSTKNL 320
Cdd:cd01517 185 PVRLDSQAKYAAVARGAADFYLRLPLSmSYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIAAPGEI 264
|
330
....*....|
gi 1032280832 321 MPRLLKAIRE 330
Cdd:cd01517 265 HEQVLEALRE 274
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
3-307 |
3.74e-58 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 188.83 E-value: 3.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 3 YEKELAAAKKAVSLAARLSQEVQKSLLqsDVRSKSDKSPVTAADYGSQAVISHVLeRELHPE-PLylVAEENAEDLhkng 81
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRADF--EVEEKADDSPVTEADLAAHAIILAGL-AALTPDiPV--LSEESAAIP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 82 aeeflesitklvnnalasddsyansslsmDDVRKaidhgrsqggSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKV 160
Cdd:COG1218 72 -----------------------------YEERK----------SWDRFWLVDPLDGTKEFIKRnGEFTVNIALIEDGRP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 161 VLGVMACPKLenhkssssGCLFFATVGEGAYVQSlegDSHPPQKVQVSNIENPEEATFVESSHKPIPIHSSIANKLGIkA 240
Cdd:COG1218 113 VLGVVYAPAL--------GRLYYAAKGQGAFKET---GGGERQPIRVRDRPPAEPLRVVASRSHRDEETEALLARLGV-A 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032280832 241 PPLRIHSQVKYAALARGDAEIYLRFTLKGyrefIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHL 307
Cdd:COG1218 181 ELVSVGSSLKFCLVAEGEADLYPRLGPTM----EWDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDL 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
38-333 |
5.88e-57 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 186.01 E-value: 5.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 38 DKSPVTAADYGSQAVISHVLERELHPEplyLVAEENAedlhKNGAEEFLESITKLVNNALASD--DSYANSS-LSMDDVR 114
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNK---LTIEEKG----KSGANDLVTAADKAAEELILEAlaALFPSHKiIGEEGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 115 KAidhGRSQGGSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKVVLGVMACPKLENhkssssgcLFFATVGEGAYVq 193
Cdd:pfam00459 74 KG---DQTELTDDGPTWIIDPIDGTKNFVHGiPQFAVSIGLAVNGEPVLGVIYQPFAGQ--------LYSAAKGKGAFL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 194 slegDSHPPQKVQVSNI-ENPEEATFVESSHKPIPIHSSIANKLGIK-APPLRIH--SQVKYAALARGDAEIYLRFTlkg 269
Cdd:pfam00459 142 ----NGQPLPVSRAPPLsEALLVTLFGVSSRKDTSEASFLAKLLKLVrAPGVRRVgsAALKLAMVAAGKADAYIEFG--- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032280832 270 yREFIWNHAAGAIITTEAGGVVCDADGNPLDfsrgnhLEHKTGIVVSTKNLMPRLLKAIRESIE 333
Cdd:pfam00459 215 -RLKPWDHAAGVAILREAGGVVTDADGGPFD------LLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
32-302 |
1.40e-16 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 78.20 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 32 DVRSKSDKSPVTAADYGSQAVISHVLEReLHPEpLYLVAEENAEDLhkngaeeflesitklvnnalasddsyansslsmd 111
Cdd:PRK10931 27 DVASKADDSPVTAADIAAHTVIKDGLRT-LTPD-IPVLSEEDPPAW---------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 112 DVRKaidHGRsqggssgRHWILDPVDGTRGFVKGE-EYAVALALLVEGKVVLGVMACPKLENHKSSSSGCLFFATVGEGA 190
Cdd:PRK10931 71 EVRQ---HWQ-------RYWLVDPLDGTKEFIKRNgEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 191 YVQSLegDSHPPQKVqVSNIENPEEatfVESSHKPIPIHSSIAnklgikapplrIHSQVKYAALARGDAEIYLRFTLKGy 270
Cdd:PRK10931 141 QIQVR--DARPPLVV-ISRSHADAE---LKEYLQQLGEHQTTS-----------IGSSLKFCLVAEGQAQLYPRFGPTN- 202
|
250 260 270
....*....|....*....|....*....|..
gi 1032280832 271 refIWNHAAGAIITTEAGGVVCDADGNPLDFS 302
Cdd:PRK10931 203 ---IWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
3-335 |
5.52e-134 |
|
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: 385.76 E-value: 5.52e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 3 YEKELAAAKKAVSLAARLSQEVQKSLLQSD---VRSKSDKSPVTAADYGSQAVISHVLERELHPEPLylVAEENAEDLHK 79
Cdd:TIGR01330 2 LERELDVATQAVRLASLLTKKVQSELISHKdstVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPI--VGEEDSSGLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 80 NGaeEFLESITKLVNNALASDDSYAN----SSLSMDDVRKAIDHGRSQGGSSGRHWILDPVDGTRGFVKGEEYAVALALL 155
Cdd:TIGR01330 80 AD--FTLGRVNELVNETLVYAKNYKKddqfPLKSLEDVLQIIDFGNYEGGRKGRHWVLDPIDGTKGFLRGDQYAVCLALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 156 VEGKVVLGVMACPKL-------ENHKSSSS-GCLFFATVGEGAYVQSLEGDSHPPQKVQVSNIENPEEATFVESSHKPIP 227
Cdd:TIGR01330 158 ENGKVVLGVIGCPNLplssygaQNLKGSESkGCIFRAVRGSGAFMYSLSSDAESPTKVHVSSVKDTKDAIFCEGVEKGHS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 228 IH---SSIANKLGIKAPPLRIHSQVKYAALARGDAEIYLRFTLKG-YREFIWNHAAGAIITTEAGGVVCDADGNPLDFSR 303
Cdd:TIGR01330 238 SHdeqTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPIKLsYQEKIWDHAAGNVIVEEAGGIVTDAMGKPLDFGK 317
|
330 340 350
....*....|....*....|....*....|....
gi 1032280832 304 GNHLEHKTGIVVSTKN--LMPRLLKAIRESIEEE 335
Cdd:TIGR01330 318 GRTLALDKGVIAASGPrvLHDLVVSTSCDSIQSR 351
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
6-330 |
6.06e-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: 298.46 E-value: 6.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 6 ELAAAKKAVSLAARLSQEVQKSLLQSDVR-SKSDKSPVTAADYGSQAVISHVLERELHPEPLylVAEENAEDLhkngaee 84
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGAGDVVwKKSDKSPVTVADYGAQALITAALARLFPSDPI--VGEEDSAAL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 85 flesitklvnnalasddsyansslsmddvrkaidhgrsqggssGRHWILDPVDGTRGFVKGEEYAVALALLVEGKVVLGV 164
Cdd:cd01517 72 -------------------------------------------GRFWVLDPIDGTKGFLRGDQFAVALALIEDGEVVLGV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 165 MACPKLeNHKSSSSGCLFFATVGEGAYVQSLEGdsHPPQKVQVSNIENPEEATF---VESSHKPIPIHSSIaNKLGIKAP 241
Cdd:cd01517 109 IGCPNL-PLDDGGGGDLFSAVRGQGAWLRPLDG--SSLQPLSVRQLTNAARASFcesVESAHSSHRLQAAI-KALGGTPQ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 242 PLRIHSQVKYAALARGDAEIYLRFTLK-GYREFIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHLEHKTGIVVSTKNL 320
Cdd:cd01517 185 PVRLDSQAKYAAVARGAADFYLRLPLSmSYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIAAPGEI 264
|
330
....*....|
gi 1032280832 321 MPRLLKAIRE 330
Cdd:cd01517 265 HEQVLEALRE 274
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
3-307 |
3.74e-58 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 188.83 E-value: 3.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 3 YEKELAAAKKAVSLAARLSQEVQKSLLqsDVRSKSDKSPVTAADYGSQAVISHVLeRELHPE-PLylVAEENAEDLhkng 81
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRADF--EVEEKADDSPVTEADLAAHAIILAGL-AALTPDiPV--LSEESAAIP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 82 aeeflesitklvnnalasddsyansslsmDDVRKaidhgrsqggSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKV 160
Cdd:COG1218 72 -----------------------------YEERK----------SWDRFWLVDPLDGTKEFIKRnGEFTVNIALIEDGRP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 161 VLGVMACPKLenhkssssGCLFFATVGEGAYVQSlegDSHPPQKVQVSNIENPEEATFVESSHKPIPIHSSIANKLGIkA 240
Cdd:COG1218 113 VLGVVYAPAL--------GRLYYAAKGQGAFKET---GGGERQPIRVRDRPPAEPLRVVASRSHRDEETEALLARLGV-A 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032280832 241 PPLRIHSQVKYAALARGDAEIYLRFTLKGyrefIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHL 307
Cdd:COG1218 181 ELVSVGSSLKFCLVAEGEADLYPRLGPTM----EWDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDL 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
38-333 |
5.88e-57 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 186.01 E-value: 5.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 38 DKSPVTAADYGSQAVISHVLERELHPEplyLVAEENAedlhKNGAEEFLESITKLVNNALASD--DSYANSS-LSMDDVR 114
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNK---LTIEEKG----KSGANDLVTAADKAAEELILEAlaALFPSHKiIGEEGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 115 KAidhGRSQGGSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKVVLGVMACPKLENhkssssgcLFFATVGEGAYVq 193
Cdd:pfam00459 74 KG---DQTELTDDGPTWIIDPIDGTKNFVHGiPQFAVSIGLAVNGEPVLGVIYQPFAGQ--------LYSAAKGKGAFL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 194 slegDSHPPQKVQVSNI-ENPEEATFVESSHKPIPIHSSIANKLGIK-APPLRIH--SQVKYAALARGDAEIYLRFTlkg 269
Cdd:pfam00459 142 ----NGQPLPVSRAPPLsEALLVTLFGVSSRKDTSEASFLAKLLKLVrAPGVRRVgsAALKLAMVAAGKADAYIEFG--- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032280832 270 yREFIWNHAAGAIITTEAGGVVCDADGNPLDfsrgnhLEHKTGIVVSTKNLMPRLLKAIRESIE 333
Cdd:pfam00459 215 -RLKPWDHAAGVAILREAGGVVTDADGGPFD------LLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
7-330 |
1.76e-39 |
|
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: 139.98 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 7 LAAAKKAVSLAARLSQEVQKSLlQSDVRSKSDKSPVTAADYGSQAVISHVLeRELHPEpLYLVAEEnaedlhkngaeefl 86
Cdd:COG0483 4 LELALRAARAAGALILRRFREL-DLEVETKGDGDLVTEADRAAEAAIRERL-RAAFPD-HGILGEE-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 87 esitklvnnalasddsyansslsmddvrkaidHGRSQGGSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKVVLGVM 165
Cdd:COG0483 67 --------------------------------SGASEGRDSGYVWVIDPIDGTTNFVHGlPLFAVSIALVRDGEPVAGVV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 166 ACPklenhkssSSGCLFFATVGEGAYvqsLEGdshppQKVQVSNIENPEEATFVESSHKPIPIHSSIAN--KLGIKAPPL 243
Cdd:COG0483 115 YDP--------ALGELFTAARGGGAF---LNG-----RRLRVSARTDLEDALVATGFPYLRDDREYLAAlaALLPRVRRV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 244 RIH--SQVKYAALARGDAEIYLRFTLKgyrefIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNhlehktgIVVSTKNLM 321
Cdd:COG0483 179 RRLgsAALDLAYVAAGRLDAFVEAGLK-----PWDIAAGALIVREAGGVVTDLDGEPLDLGSGS-------LVAANPALH 246
|
....*....
gi 1032280832 322 PRLLKAIRE 330
Cdd:COG0483 247 DELLALLRE 255
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
16-307 |
3.78e-36 |
|
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: 130.81 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 16 LAARLSQEVQKSLLQ-----SDVRSKSDKSPVTAADYGSQAVISHVLeRELHPE-PLylVAEENAEDLHKNGAEEFlesi 89
Cdd:cd01638 4 LLIRIAREAGDAILEvyrggFTVERKEDGSPVTAADLAANAFIVEGL-AALRPDiPV--LSEESADDPLRLGWDRF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 90 tklvnnalasddsyansslsmddvrkaidhgrsqggssgrhWILDPVDGTRGFVKGE-EYAVALALLVEGKVVLGVMACP 168
Cdd:cd01638 77 -----------------------------------------WLVDPLDGTREFIKGNgEFAVNIALVEDGRPVLGVVYAP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 169 KLenhkssssGCLFFATVGEGAYVQSLEGdsHPPQKVQVSNienPEEATFVESSHKPIPIHSSIANKLGIkAPPLRIHSQ 248
Cdd:cd01638 116 AL--------GELYYALRGGGAYKNGRPG--AVSLQARPPP---LQPLRVVASRSHPDEELEALLAALGV-AEVVSIGSS 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1032280832 249 VKYAALARGDAEIYLRFTLKgyreFIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHL 307
Cdd:cd01638 182 LKFCLVAEGEADIYPRLGPT----MEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDFL 236
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
10-305 |
8.38e-30 |
|
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: 113.95 E-value: 8.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 10 AKKAVSLAARLSQEVQKSLLqSDVRSKSDKSPVTAADYGSQAVISHVLERELHPEPLylVAEEnaedlhkngaeeflesi 89
Cdd:cd01637 4 ALKAVREAGALILEAFGEEL-TVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGI--LGEE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 90 tklvnnalasddsyansslsmddvrkaiDHGRSQGGSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKVVLGVMACP 168
Cdd:cd01637 64 ----------------------------GGGSGNVSDGGRVWVIDPIDGTTNFVAGlPNFAVSIALYEDGKPVLGVIYDP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 169 KLENhkssssgcLFFATVGEGAYVQslegdshpPQKVQVSNIENPEEAT-FVESSHKPIPIHSSIAnklGIKAPPLRIHS 247
Cdd:cd01637 116 MLDE--------LYYAGRGKGAFLN--------GKKLPLSKDTPLNDALlSTNASMLRSNRAAVLA---SLVNRALGIRI 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032280832 248 ----QVKYAALARGDAEIYLRFTLKgyrefIWNHAAGAIITTEAGGVVCDADGNPLDFSRGN 305
Cdd:cd01637 177 ygsaGLDLAYVAAGRLDAYLSSGLN-----PWDYAAGALIVEEAGGIVTDLDGEPLDTLNRS 233
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
17-329 |
1.19e-22 |
|
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: 95.01 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 17 AARLSQEVQKSLLQS--DVRSKSDKSPVTAADYGSQAVISHVLERELhPEplylvaeenaedlHKNGAEEFLESitklvn 94
Cdd:cd01641 8 LADAAGQITLPYFRTrlQVETKADFSPVTEADRAAEAAMRELIAAAF-PD-------------HGILGEEFGNE------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 95 nalasddsyansslsmddvrkaidhgrsqGGSSGRHWILDPVDGTRGFVKGEE-YAVALALLVEGKVVLGVMACPKLenh 173
Cdd:cd01641 68 -----------------------------GGDAGYVWVLDPIDGTKSFIRGLPvWGTLIALLHDGRPVLGVIDQPAL--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 174 kssssGCLFFATVGEGAYVQSLEGdshppQKVQVSNIENPEEATFVESSHKPIPIHSsianklgiKAPPLRIHSQVK--- 250
Cdd:cd01641 116 -----GERWIGARGGGTFLNGAGG-----RPLRVRACADLAEAVLSTTDPHFFTPGD--------RAAFERLARAVRltr 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 251 -------YAALARGDAEIYLRFTLKgyrefIWNHAAGAIITTEAGGVVCDADGNPLDfsrGNHlehktGIVVSTKNlmPR 323
Cdd:cd01641 178 yggdcyaYALVASGRVDLVVEAGLK-----PYDVAALIPIIEGAGGVITDWDGGPLT---GGS-----GRVVAAGD--AE 242
|
....*.
gi 1032280832 324 LLKAIR 329
Cdd:cd01641 243 LHEALL 248
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
32-302 |
1.40e-16 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 78.20 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 32 DVRSKSDKSPVTAADYGSQAVISHVLEReLHPEpLYLVAEENAEDLhkngaeeflesitklvnnalasddsyansslsmd 111
Cdd:PRK10931 27 DVASKADDSPVTAADIAAHTVIKDGLRT-LTPD-IPVLSEEDPPAW---------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 112 DVRKaidHGRsqggssgRHWILDPVDGTRGFVKGE-EYAVALALLVEGKVVLGVMACPKLENHKSSSSGCLFFATVGEGA 190
Cdd:PRK10931 71 EVRQ---HWQ-------RYWLVDPLDGTKEFIKRNgEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 191 YVQSLegDSHPPQKVqVSNIENPEEatfVESSHKPIPIHSSIAnklgikapplrIHSQVKYAALARGDAEIYLRFTLKGy 270
Cdd:PRK10931 141 QIQVR--DARPPLVV-ISRSHADAE---LKEYLQQLGEHQTTS-----------IGSSLKFCLVAEGQAQLYPRFGPTN- 202
|
250 260 270
....*....|....*....|....*....|..
gi 1032280832 271 refIWNHAAGAIITTEAGGVVCDADGNPLDFS 302
Cdd:PRK10931 203 ---IWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
11-331 |
2.01e-14 |
|
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: 71.95 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 11 KKAVSLAARLSQEV-----QKSLLQSDvrSKSDKSPVTAADYGSQAVISHVLERELhpePLYLVAEEnaedlhkngaeEF 85
Cdd:TIGR02067 2 LAFAEDLADAAGETilpffRASLLVVD--KKSDKTPVTEADRAAEEAMRELIAAFF---PDHGILGE-----------EF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 86 lesitklvnnalasddsyansslsmddvrkaidhGRSQGGSSGRHWILDPVDGTRGFVKGEEYAVALALLVE-GKVVLGV 164
Cdd:TIGR02067 66 ----------------------------------GHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEgGMPVLGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 165 MACPKLENhkssssgcLFFATVGEGAYVQslegdshpPQKVQVSNIENPEEATFVESShkpiPIHssiANKLGIKAPPLR 244
Cdd:TIGR02067 112 IFQPATGE--------RWWAAGGGAAFLG--------GRRLRVSSCANLSDAVLFTTS----PDL---LDDPGNRPAFER 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 245 IHSQVK----------YAALARGDAEIYLRFTLKgyrefIWNHAAGAIITTEAGGVVCDADGNPLDFSrgnhlehktGIV 314
Cdd:TIGR02067 169 LRRAARltryggdcyaYLMVAGGAVDIVVEPGLS-----PWDIAALIPVIEEAGGCFTDWDGKPAPDG---------GGA 234
|
330
....*....|....*..
gi 1032280832 315 VSTKNlmPRLLKAIRES 331
Cdd:TIGR02067 235 VAAGN--AMLHDEALEI 249
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
124-309 |
9.39e-13 |
|
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: 66.97 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 124 GGSSGRHWILDPVDGTRGFVKGEEY-AVALALLVEGKVVLGVMACPKLenhkssssGCLFFATVGEGAYVQslegdshpP 202
Cdd:cd01643 67 FPSSGWYWVIDPIDGTTNFARGIPIwAISIALLYRGEPVFGVIALPAL--------NQTFVAFKGGGAFLN--------G 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 203 QKVQVSNIENPEEATFVESshkpIPIHSSIANKLGIKAPPLRIH------SQVKYAALARGDAEIYLRFTLKgyrefIWN 276
Cdd:cd01643 131 KPLALHPPLQLPDCNVGFN----RSSRASARAVLRVILRRFPGKirmlgsASLNLASVAAGQTLGYVEATPK-----IWD 201
|
170 180 190
....*....|....*....|....*....|...
gi 1032280832 277 HAAGAIITTEAGGVVCDADGNPLDFSRGNHLEH 309
Cdd:cd01643 202 IAAAWVILREAGGSWTILDEEPAFLQTKDYLSA 234
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
120-329 |
1.17e-11 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 64.16 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 120 GRSQGGSSGRHWILDPVDGTRGFVKGEE-YAVALALLVEGKVVLGVMacpklenhKSSSSGCLFFATVGEGAYvqsLEGd 198
Cdd:PRK12676 73 GEIVGNGPEYTVVLDPLDGTYNAINGIPfYAISIAVFKGGKPVYGYV--------YNLATGDFYEAIPGKGAY---LNG- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 199 shppQKVQVSNIENPEEATFVESSHKPIPIHSSianKLGIKAPPLRI--HSQVKYAALARG--DAEIYLRFTLKgyrefI 274
Cdd:PRK12676 141 ----KPIKVSKTSELNESAVSIYGYRRGKERTV---KLGRKVRRVRIlgAIALELCYVASGrlDAFVDVRNYLR-----V 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032280832 275 WNHAAGAIITTEAGGVVCDADGNPLDFSRgNHLEHKTGIVVSTKNLMPRLLKAIR 329
Cdd:PRK12676 209 TDIAAGKLICEEAGGIVTDEDGNELKLPL-NVTERTNLIAANGEELHKKILELLE 262
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
120-336 |
3.46e-10 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 59.82 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 120 GRSQGGSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGKVVLGVMACPkLENHkssssgcLFFATVGEGAYVQS--LE 196
Cdd:PRK10757 70 GELEGEDQDVQWVIDPLDGTTNFIKRlPHFAVSIAVRIKGRTEVAVVYDP-MRNE-------LFTATRGQGAQLNGyrLR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 197 GDShppqkvqVSNIENPEEAT---FVESSHKPIPIhsSIANKLGIKAPPLRI--HSQVKYAALARGDAEIYLRFTLKGyr 271
Cdd:PRK10757 142 GST-------ARDLDGTILATgfpFKAKQHATTYI--NIVGKLFTECADFRRtgSAALDLAYVAAGRVDGFFEIGLKP-- 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032280832 272 efiWNHAAGAIITTEAGGVVCDADGNPLDFSRGNhlehktgIVVSTknlmPRLLKAIRESIEEEM 336
Cdd:PRK10757 211 ---WDFAAGELLVREAGGIVSDFTGGHNYMLTGN-------IVAGN----PRVVKAMLANMRDEL 261
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
123-328 |
1.07e-09 |
|
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: 58.16 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 123 QGGSSGRHWILDPVDGTRGFVKG-EEYAVALALLVEGK--VVLGVMacpklenhKSSSSGCLFFATVGEGAYvqsLEGds 199
Cdd:cd01515 71 NGDEPEYTVVLDPLDGTYNAINGiPFYSVSVAVFKIDKsdPYYGYV--------YNLATGDLYYAIKGKGAY---LNG-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 200 hppQKVQVSniENPEEATFVESSHKPIPIHsSIANKLGIKAPPLRIHSQVK----YAALARGDAEIYLRFTLKgyrefIW 275
Cdd:cd01515 138 ---KRIKVS--DFSSLKSISVSYYIYGKNH-DRTFKICRKVRRVRIFGSVAlelcYVASGALDAFVDVRENLR-----LV 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032280832 276 NHAAGAIITTEAGGVVCDADGNPLDFSrgNHLEHKTGIVVSTKNLMPRLLKAI 328
Cdd:cd01515 207 DIAAGYLIAEEAGGIVTDENGKELKLK--LNVTERVNIIAANSELHKKLLELL 257
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
131-300 |
1.54e-09 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 57.78 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 131 WILDPVDGTRGFVKGEEYA-VALALLVEGKVVLGVMACPKLENhkssssgcLFFATVGEGAYvqsLEGDshpPQKV-QVS 208
Cdd:PLN02553 88 WIVDPLDGTTNFVHGFPFVcVSIGLTIGKVPVVGVVYNPILDE--------LFTAVKGKGAF---LNGK---PIKAsSQS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 209 NIENPEEATFVESSH--KPIPIHSSIANKLGIKAPPLRIHSQ--VKYAALARGDAEIYLRFTLKGyrefIWNHAAGAIIT 284
Cdd:PLN02553 154 ELGKALLATEVGTKRdkATVDATTNRINALLYKVRSLRMSGScaLNLCGVACGRLDIFYEIGFGG----PWDVAAGAVIV 229
|
170
....*....|....*.
gi 1032280832 285 TEAGGVVCDADGNPLD 300
Cdd:PLN02553 230 KEAGGLVFDPSGGPFD 245
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
7-316 |
9.53e-09 |
|
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: 55.79 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 7 LAAAKKAVSLAARLSQEVQksLLQSDVRSKSDKS---PVTAADYGSQAVISHVLERelHPEPLYLVAEENAEDLHKNG-A 82
Cdd:cd01640 6 LAVAEKAGGIARDVVKKGR--LLILLVEGKTKEGandFKTLADRLSQRVIKHSLQK--QFPKLKIIGEEDNEFENQEDeS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 83 EEFLESITKLVNNALASDDsyansSLSMDDVRKaidhgrsqggssgrhWIlDPVDGTRGFVKGE-EYAVALA-LLVEGKV 160
Cdd:cd01640 82 RDVDLDEEILEESCPSPSK-----DLPEEDLGV---------------WV-DPLDATQEYTEGLlEYVTVLIgVAVKGKP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 161 VLGVMACP---KLENHkSSSSGCLFFATVGEGAYVQSLEGDSHPPQKVqvsnienpeeatfVESSHK-PIPIHSSIANKL 236
Cdd:cd01640 141 IAGVIHQPfyeKTAGA-GAWLGRTIWGLSGLGAHSSDFKEREDAGKII-------------VSTSHShSVKEVQLITAGN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 237 GIKapplrihsqVKYAA--------LARGDAEIYLRFTLKGYRefiWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHLE 308
Cdd:cd01640 207 KDE---------VLRAGgagykvlqVLEGLADAYVHSTGGIKK---WDICAPEAILRALGGDMTDLHGEPLSYSKAVKPV 274
|
....*...
gi 1032280832 309 HKTGIVVS 316
Cdd:cd01640 275 NKGGLLAT 282
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
63-328 |
2.22e-08 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 55.19 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 63 PEPLYLVAEENAedlhKNGAEEFLESITKLVN------NALASDDSYANSSLSMDDVRKAI-DH-------GRSQGGSSG 128
Cdd:PLN02737 76 AEELLAVAELAA----KTGAEVVMEAVNKPRNisykglTDLVTDTDKASEAAILEVVRKNFpDHlilgeegGVIGDSSSD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 129 RHWILDPVDGTRGFVKG-EEYAVALALLVEGKVVLGVM----ACPKLENHKSsssgclFFATVGEGAYVQSlegdshppQ 203
Cdd:PLN02737 152 YLWCIDPLDGTTNFAHGyPSFAVSVGVLFRGTPAAATVvefvGGPMCWNTRT------FSASAGGGAFCNG--------Q 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 204 KVQVSNIENPEEATFVES---SH-----------KPIPIHSSIANKLGIKApplrihsqVKYAALARGDAEIYLRFTLKG 269
Cdd:PLN02737 218 KIHVSQTDKVERSLLVTGfgyEHddawatnielfKEFTDVSRGVRRLGAAA--------VDMCHVALGIVEAYWEYRLKP 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 270 yrefiWNHAAGAIITTEAGGVVCDADGNPLD-FSRgnhlehktGIVVSTKNLMPRLLKAI 328
Cdd:PLN02737 290 -----WDMAAGVLIVEEAGGTVTRMDGGKFSvFDR--------SVLVSNGVLHPKLLDRI 336
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
9-294 |
2.50e-07 |
|
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: 50.08 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 9 AAKKAvSLAARlsQEVQKSLLQSDVRSKSDKSPVTAADYGSQAVISHVLeRELHPEpLYLVAEENAEDLHKngaeefles 88
Cdd:cd01636 7 VAKEA-GLAIL--KAFGRELSGKVKITKSDNDPVTTADVAAETLIRNML-KSSFPD-VKIVGEESGVAEEV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 89 itklvnnalasddsyansslsmddvrkaidhgrsQGGSSGRHWILDPVDGTRGFVKGeeyavalalLVEGKVVLGVMACp 168
Cdd:cd01636 73 ----------------------------------MGRRDEYTWVIDPIDGTKNFING---------LPFVAVVIAVYVI- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 169 kLENHKSSSSGclffatvgegayvqslegdsHPPQKVQVSNIEnpeeatfvessHKPIPIHSSianklgikapplrihSQ 248
Cdd:cd01636 109 -LILAEPSHKR--------------------VDEKKAELQLLA-----------VYRIRIVGS---------------AV 141
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1032280832 249 VKYAALARGDAEIYLRFTLKgyrEFIWNHAAGAIITTEAGGVVCDA 294
Cdd:cd01636 142 AKMCLVALGLADIYYEPGGK---RRAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
32-170 |
2.22e-06 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 48.56 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 32 DVRSKSDKSPVTAADYGSQAVISHVLERELHPEPLYlvAEENAEDLHKNGAEeflesitklvnnalasddsYAnsslsmd 111
Cdd:PLN02911 60 EIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIF--GEEHGLRCGEGSSD-------------------YV------- 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032280832 112 dvrkaidhgrsqggssgrhWILDPVDGTRGFVKGEE-YAVALALLVEGKVVLGVMACPKL 170
Cdd:PLN02911 112 -------------------WVLDPIDGTKSFITGKPlFGTLIALLYKGKPVLGIIDQPVL 152
|
|
| |
