|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-263 |
3.63e-116 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 333.28 E-value: 3.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDGRGFFL 80
Cdd:COG1218 4 LLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLVVMDdftvGARSAITVREQPDDR--LA 158
Cdd:COG1218 84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGG----GERQPIRVRDRPPAEplRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 159 LASLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYGK 238
Cdd:COG1218 160 VASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNK 239
|
250 260
....*....|....*....|....*
gi 502307870 239 TGtaadfDFANPNFISWGGRKRVLE 263
Cdd:COG1218 240 KE-----DLLNPGFIASGDHAAILA 259
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
1-253 |
3.18e-97 |
|
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: 284.89 E-value: 3.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVpdIDGRGFFL 80
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLR--LGWDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLVVMDdftvGARSAITVREQPDDRLALA 160
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRP----GAVSLQARPPPLQPLRVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 161 SLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYGKTg 240
Cdd:cd01638 155 SRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNRE- 233
|
250
....*....|...
gi 502307870 241 taadfDFANPNFI 253
Cdd:cd01638 234 -----DFLNPDFI 241
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
1-253 |
3.01e-94 |
|
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: 277.41 E-value: 3.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDGRGFFL 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLVVMDdftVGARSAITVREQPDDRLA-L 159
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDG---QALKAPIHVRPWPSGPLLvV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 160 ASLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYGKT 239
Cdd:TIGR01331 158 ISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237
|
250
....*....|....
gi 502307870 240 GtaadfDFANPNFI 253
Cdd:TIGR01331 238 E-----SFRNPNFV 246
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
1-252 |
4.41e-66 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 205.70 E-value: 4.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFP--VAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDiDGRGF 78
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPldVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 79 FLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLvvmddfTVGARSAITVRE-QPDdrL 157
Cdd:PRK10931 80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKE------ECGVRKQIQVRDaRPP--L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 158 ALASLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYg 237
Cdd:PRK10931 152 VVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDY- 230
|
250
....*....|....*
gi 502307870 238 ktgtAADFDFANPNF 252
Cdd:PRK10931 231 ----TPRESFLNPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-243 |
3.86e-51 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 168.29 E-value: 3.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADAS-------PVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDI 73
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKgksgandLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 74 --DGRgFFLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERG----------HAERLVVMDDFTV 141
Cdd:pfam00459 81 tdDGP-TWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGkgaflngqplPVSRAPPLSEALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 142 GARSAITVREQPDDRLALASLRhnspetgSFLADQAIFkctNIGSS-LKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLR 220
Cdd:pfam00459 160 VTLFGVSSRKDTSEASFLAKLL-------KLVRAPGVR---RVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILR 229
|
250 260
....*....|....*....|...
gi 502307870 221 AAGGSTVTLDGTPLTYGKTGTAA 243
Cdd:pfam00459 230 EAGGVVTDADGGPFDLLAGRVIA 252
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-263 |
3.63e-116 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 333.28 E-value: 3.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDGRGFFL 80
Cdd:COG1218 4 LLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLVVMDdftvGARSAITVREQPDDR--LA 158
Cdd:COG1218 84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGG----GERQPIRVRDRPPAEplRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 159 LASLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYGK 238
Cdd:COG1218 160 VASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNK 239
|
250 260
....*....|....*....|....*
gi 502307870 239 TGtaadfDFANPNFISWGGRKRVLE 263
Cdd:COG1218 240 KE-----DLLNPGFIASGDHAAILA 259
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
1-253 |
3.18e-97 |
|
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: 284.89 E-value: 3.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVpdIDGRGFFL 80
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLR--LGWDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLVVMDdftvGARSAITVREQPDDRLALA 160
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRP----GAVSLQARPPPLQPLRVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 161 SLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYGKTg 240
Cdd:cd01638 155 SRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNRE- 233
|
250
....*....|...
gi 502307870 241 taadfDFANPNFI 253
Cdd:cd01638 234 -----DFLNPDFI 241
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
1-253 |
3.01e-94 |
|
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: 277.41 E-value: 3.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDGRGFFL 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLVVMDdftVGARSAITVREQPDDRLA-L 159
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDG---QALKAPIHVRPWPSGPLLvV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 160 ASLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYGKT 239
Cdd:TIGR01331 158 ISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237
|
250
....*....|....
gi 502307870 240 GtaadfDFANPNFI 253
Cdd:TIGR01331 238 E-----SFRNPNFV 246
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
1-252 |
4.41e-66 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 205.70 E-value: 4.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFP--VAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDiDGRGF 78
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPldVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 79 FLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLvvmddfTVGARSAITVRE-QPDdrL 157
Cdd:PRK10931 80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKE------ECGVRKQIQVRDaRPP--L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 158 ALASLRHNSPETGSFLADQAIFKCTNIGSSLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTYg 237
Cdd:PRK10931 152 VVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDY- 230
|
250
....*....|....*
gi 502307870 238 ktgtAADFDFANPNF 252
Cdd:PRK10931 231 ----TPRESFLNPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-243 |
3.86e-51 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 168.29 E-value: 3.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADAS-------PVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDI 73
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKgksgandLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 74 --DGRgFFLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERG----------HAERLVVMDDFTV 141
Cdd:pfam00459 81 tdDGP-TWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGkgaflngqplPVSRAPPLSEALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 142 GARSAITVREQPDDRLALASLRhnspetgSFLADQAIFkctNIGSS-LKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLR 220
Cdd:pfam00459 160 VTLFGVSSRKDTSEASFLAKLL-------KLVRAPGVR---RVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILR 229
|
250 260
....*....|....*....|...
gi 502307870 221 AAGGSTVTLDGTPLTYGKTGTAA 243
Cdd:pfam00459 230 EAGGVVTDADGGPFDLLAGRVIA 252
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
1-250 |
2.69e-46 |
|
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: 155.39 E-value: 2.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREG-FPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESvaaGKVPDIDGRGFF 79
Cdd:COG0483 3 LLELALRAARAAGALILRRFRELdLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 80 LVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHA-----ERLVVMDDFTV-GARSAITVREQP 153
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGaflngRRLRVSARTDLeDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 154 DDRLALASLRHNSPETGSFladqaifkcTNIGS-SLKFCLLAEGKADVYPRFtRTMEWDTAAGDAVLRAAGGSTVTLDGT 232
Cdd:COG0483 160 DDREYLAALAALLPRVRRV---------RRLGSaALDLAYVAAGRLDAFVEA-GLKPWDIAAGALIVREAGGVVTDLDGE 229
|
250
....*....|....*...
gi 502307870 233 PLTYGKTGTAAdfdfANP 250
Cdd:COG0483 230 PLDLGSGSLVA----ANP 243
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
2-236 |
3.07e-44 |
|
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: 149.39 E-value: 3.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 2 LRTFEKAALEAGRAIITVLREGFPVA-MKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDidGRGFFL 80
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVEtKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSD--GGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAErlvvmddFTVGARSAITVREQPDDRLAL- 159
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGA-------FLNGKKLPLSKDTPLNDALLSt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 160 --ASLRHNSPETGSFLAdQAIFKCTNIGS-SLKFCLLAEGKADVYPRFtRTMEWDTAAGDAVLRAAGGSTVTLDGTPLTY 236
Cdd:cd01637 152 naSMLRSNRAAVLASLV-NRALGIRIYGSaGLDLAYVAAGRLDAYLSS-GLNPWDYAAGALIVEEAGGIVTDLDGEPLDT 229
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
6-241 |
1.63e-41 |
|
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: 143.61 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 6 EKAALEAGRAIITVLREGfPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAgkvpdiDGRgFFLVDPLD 85
Cdd:cd01517 10 RAAASLTLPVFRNLGAGD-VVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA------LGR-FWVLDPID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 86 GTREFVDGRQeFTVNIAYIENGAPIAGIVYAPAL-------GLAFSGERGHAERLVVMDDftVGARSAITVREQPDDRLA 158
Cdd:cd01517 82 GTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLplddgggGDLFSAVRGQGAWLRPLDG--SSLQPLSVRQLTNAARAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 159 -LASLRHNSPETGSFLADQAIFKCT---NIGSSLKFCLLAEGKADVYPRF-----TRTMEWDTAAGDAVLRAAGGSTVTL 229
Cdd:cd01517 159 fCESVESAHSSHRLQAAIKALGGTPqpvRLDSQAKYAAVARGAADFYLRLplsmsYREKIWDHAAGVLIVEEAGGKVTDA 238
|
250
....*....|..
gi 502307870 230 DGTPLTYGKTGT 241
Cdd:cd01517 239 DGKPLDFGKGRK 250
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
2-243 |
4.83e-32 |
|
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: 118.13 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 2 LRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEEsvAAGKVPDIDGRgfFLV 81
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEE--FGNEGGDAGYV--WVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 82 DPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERlvvmddFTVGARSAITVREQPDdrLALAS 161
Cdd:cd01641 78 DPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTF------LNGAGGRPLRVRACAD--LAEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 162 LRHNSPETGSFlADQAIF--------KCTNIGSSLKFCLLAEGKADVyprftrTME-----WDTAAGDAVLRAAGGSTVT 228
Cdd:cd01641 150 LSTTDPHFFTP-GDRAAFerlaravrLTRYGGDCYAYALVASGRVDL------VVEaglkpYDVAALIPIIEGAGGVITD 222
|
250
....*....|....*
gi 502307870 229 LDGTPLTYGKTGTAA 243
Cdd:cd01641 223 WDGGPLTGGSGRVVA 237
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
1-243 |
3.64e-27 |
|
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: 105.31 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRaiitVLREGFP-----VAMKADAS-PVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDiD 74
Cdd:cd01639 1 LLNIAIEAARKAGE----ILLEAYEklglnVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTD-E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 75 GRgfFLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHaerlvvmddftvGAR---SAITVRE 151
Cdd:cd01639 76 PT--WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQ------------GAFlngRRIRVSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 152 QPDDRLAL------ASLRHNSPETGSFLADQAIFKCTNI---GS-SLKFCLLAEGKADVYprFTRTM-EWDTAAGDAVLR 220
Cdd:cd01639 142 RKELKDALvatgfpYDRGDNFDRYLNNFAKLLAKAVRGVrrlGSaALDLAYVAAGRLDGY--WERGLkPWDVAAGALIVR 219
|
250 260
....*....|....*....|...
gi 502307870 221 AAGGSTVTLDGTPLTYGKTGTAA 243
Cdd:cd01639 220 EAGGLVTDFDGGPFDLMSGNILA 242
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
29-248 |
2.21e-24 |
|
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate inositol monophosphate or similar substrates.
Pssm-ID: 238821 [Multi-domain] Cd Length: 242 Bit Score: 97.79 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 29 KADASPVTVADEEAERIILAHLARDYPEIPVVAEESvaAGKVPDIDGrgFFLVDPLDGTREFVDGRQEFTVNIAYIENGA 108
Cdd:cd01643 28 KADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG--GGIFPSSGW--YWVIDPIDGTTNFARGIPIWAISIALLYRGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 109 PIAGIVYAPALGLAFSGERGHAerlvvmdDFTVGARSAITVREQPDDRLALASLRHNSPETGSFLADQAIFKCT--NIGS 186
Cdd:cd01643 104 PVFGVIALPALNQTFVAFKGGG-------AFLNGKPLALHPPLQLPDCNVGFNRSSRASARAVLRVILRRFPGKirMLGS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502307870 187 -SLKFCLLAEGKADVYPRFTRTMeWDTAAGDAVLRAAGGSTVTLDGTP--LTYGKTGTAADFDFA 248
Cdd:cd01643 177 aSLNLASVAAGQTLGYVEATPKI-WDIAAAWVILREAGGSWTILDEEPafLQTKDYLSAGFPTLI 240
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
2-236 |
7.08e-23 |
|
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: 94.70 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 2 LRTFEKAALEAGRAI-----ITVLREGfpVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDgR 76
Cdd:cd01640 6 LAVAEKAGGIARDVVkkgrlLILLVEG--KTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDES-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 77 GFFL------------------------VDPLDGTREFVDGRQEF-TVNIAYIENGAPIAGIVYAP-----ALGLAFSGE 126
Cdd:cd01640 83 DVDLdeeileescpspskdlpeedlgvwVDPLDATQEYTEGLLEYvTVLIGVAVKGKPIAGVIHQPfyektAGAGAWLGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 127 rgHAERLVvmddfTVGARSAITVrEQPDDRLALASLRHNSpeTGSFLADQAIFKCTNI----GSSLKFCLLAEGKADVYP 202
Cdd:cd01640 163 --TIWGLS-----GLGAHSSDFK-EREDAGKIIVSTSHSH--SVKEVQLITAGNKDEVlragGAGYKVLQVLEGLADAYV 232
|
250 260 270
....*....|....*....|....*....|....*
gi 502307870 203 RFTR-TMEWDTAAGDAVLRAAGGSTVTLDGTPLTY 236
Cdd:cd01640 233 HSTGgIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
7-229 |
3.36e-22 |
|
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: 90.53 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 7 KAALEAGRAIITVLRE---GFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDGRGFFLVDP 83
Cdd:cd01636 6 RVAKEAGLAILKAFGRelsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 84 LDGTREFVDGRQEFTVNIAYIEngapiagivyapALGLAFSGERGHAERLVvmddftvgarsaitvreqPDDRLALASLR 163
Cdd:cd01636 86 IDGTKNFINGLPFVAVVIAVYV------------ILILAEPSHKRVDEKKA------------------ELQLLAVYRIR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502307870 164 HNSpetgsfladqaifkctniGSSLKFCLLAEGKADVYPRFTRTME-WDTAAGDAVLRAAGGSTVTL 229
Cdd:cd01636 136 IVG------------------SAVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
2-224 |
3.11e-17 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 78.96 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 2 LRTFEKAALEAGRAIITVLREGF----PVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESVAAGKVPDIDGRG 77
Cdd:PLN02553 7 LEQFLEVAVDAAKAAGQIIRKGFyqtkHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 78 FFLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLvvmddftVGARsaITVREQPDDRL 157
Cdd:PLN02553 87 TWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFL-------NGKP--IKASSQSELGK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502307870 158 AL-----------ASLRHNSPETGSFLADQAIFKCTniGS-SLKFCLLAEGKADVYPRFTRTMEWDTAAGDAVLRAAGG 224
Cdd:PLN02553 158 ALlatevgtkrdkATVDATTNRINALLYKVRSLRMS--GScALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGG 234
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-120 |
1.10e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 72.06 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 6 EKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESvaAGKVPDIDGRGFFLVDPLD 85
Cdd:PLN02911 41 HKLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEH--GLRCGEGSSDYVWVLDPID 118
|
90 100 110
....*....|....*....|....*....|....*
gi 502307870 86 GTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALG 120
Cdd:PLN02911 119 GTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLK 153
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
26-234 |
1.40e-14 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 71.48 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 26 VAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEEsvaAGKVPDIDGRGFFLVDPLDGTREFVDGRQEFTVNIAYIE 105
Cdd:PRK12676 34 VGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEE---LGEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 106 NGAPIAGIVYAPALGLAFSGERGHAERLvvmddftVGARSAITVREQPDDRLALASLRHNSPETGSFLADQA----IFKC 181
Cdd:PRK12676 111 GGKPVYGYVYNLATGDFYEAIPGKGAYL-------NGKPIKVSKTSELNESAVSIYGYRRGKERTVKLGRKVrrvrILGA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502307870 182 tnigSSLKFCLLAEGKADV------YPRFTrtmewDTAAGDAVLRAAGGSTVTLDGTPL 234
Cdd:PRK12676 184 ----IALELCYVASGRLDAfvdvrnYLRVT-----DIAAGKLICEEAGGIVTDEDGNEL 233
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
26-234 |
5.27e-12 |
|
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: 63.94 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 26 VAMKADASPVTVADEEAERIILAHLARDYPEIpVVAEES--VAAGKVPDIdgrgFFLVDPLDGTREFVDGRQEFTVNIA- 102
Cdd:cd01515 29 VKIGADGTPTKLIDKVAEDAAIEILKKLGSVN-IVSEEIgvIDNGDEPEY----TVVLDPLDGTYNAINGIPFYSVSVAv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 103 -YIENGAPIAGIVYAPALGLAFSGERGHAERLvvmddftvgARSAITVREQPDDRLALASLrhNSPETGSFLADQAIFKC 181
Cdd:cd01515 104 fKIDKSDPYYGYVYNLATGDLYYAIKGKGAYL---------NGKRIKVSDFSSLKSISVSY--YIYGKNHDRTFKICRKV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502307870 182 TNI---GS-SLKFCLLAEGKADVYPRFTRTME-WDTAAGDAVLRAAGGSTVTLDGTPL 234
Cdd:cd01515 173 RRVrifGSvALELCYVASGALDAFVDVRENLRlVDIAAGYLIAEEAGGIVTDENGKEL 230
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-224 |
2.24e-10 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 59.44 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLR--EGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEES-VAAGKVPDIDgrg 77
Cdd:PRK10757 4 MLNIAVRAARKAGNLIAKNYEtpDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESgELEGEDQDVQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 78 fFLVDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVYAPALGLAFSGERGHAERLvvmddftVGAR-SAITVREQPDDR 156
Cdd:PRK10757 81 -WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQL-------NGYRlRGSTARDLDGTI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502307870 157 LALA---SLRHNSPE----TGSFLADQAIFKCTNiGSSLKFCLLAEGKADVYprFTRTME-WDTAAGDAVLRAAGG 224
Cdd:PRK10757 153 LATGfpfKAKQHATTyiniVGKLFTECADFRRTG-SAALDLAYVAAGRVDGF--FEIGLKpWDFAAGELLVREAGG 225
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
1-215 |
1.43e-09 |
|
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: 57.07 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGF-PVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEESvaaGKVPDIDGRGFF 79
Cdd:cd01642 1 MLEVLEKITKEIILLLNEKNRQGLvKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 80 LVDPLDGTREFVDGRQEFTVNIAYIENGAPiagiVYAPALglaFSGERGHAERLVVMDDFT-----VGARSAITVREQPD 154
Cdd:cd01642 78 VLDPLDGSTNYLSGIPFYSVSVALADPRSK----VKAATL---DNFVSGEGGLKVYSPPTRfsyisVPKLGPPLVPEVPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502307870 155 DRLALASlRHNSPETGSFLAdQAIFKCTNIGSS-LKFCLLAEGKADVY-PRFTRTMEWDTAAG 215
Cdd:cd01642 151 KIGIYEG-SSRNPEKFLLLS-RNGLKFRSLGSAaLELAYTCEGSFVLFlDLRGKLRNFDVAAA 211
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
1-235 |
5.77e-08 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 52.88 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 1 MLRTFEKAALEAGRAIITVLREGFPVAMKADASPVTVADEEAERIILAHLARDYPEIPVVAEEsvaAGKVPDIDGRGFFL 80
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEE---GGVIGDSSSDYLWC 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 81 VDPLDGTREFVDGRQEFTVNIAYIENGAPIAGIVY---------------APALGLAF-SGERGHAERlvvmddfTVGAR 144
Cdd:PLN02737 156 IDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVefvggpmcwntrtfsASAGGGAFcNGQKIHVSQ-------TDKVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502307870 145 SAITVREqpddrlalASLRHNSPetgsFLADQAIFK-CTNI--------GSSLKFCLLAEGKADVYPRFtRTMEWDTAAG 215
Cdd:PLN02737 229 RSLLVTG--------FGYEHDDA----WATNIELFKeFTDVsrgvrrlgAAAVDMCHVALGIVEAYWEY-RLKPWDMAAG 295
|
250 260
....*....|....*....|
gi 502307870 216 DAVLRAAGGSTVTLDGTPLT 235
Cdd:PLN02737 296 VLIVEEAGGTVTRMDGGKFS 315
|
|
| |
