|
Name |
Accession |
Description |
Interval |
E-value |
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
11-266 |
9.87e-84 |
|
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: 251.30 E-value: 9.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 11 ARYRFACSLAESGGKLAYEFYQQRDsLQTLHKGSdlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTAD-EGKSVL 89
Cdd:COG0483 2 PLLELALRAARAAGALILRRFRELD-LEVETKGD--GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEgRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 90 WVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHR 169
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 170 VSTEDFLPFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEGIARGNVV 249
Cdd:COG0483 159 RDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSL 238
|
250
....*....|....*..
gi 2020427645 250 LLASEKIYPQLKQWVKQ 266
Cdd:COG0483 239 VAANPALHDELLALLRE 255
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-237 |
1.35e-65 |
|
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: 204.69 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 13 YRFACSLAESGGKLAYEFYQQRDsLQTLHKGSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESG-TADEGKSVLWV 91
Cdd:cd01639 2 LNIAIEAARKAGEILLEAYEKLG-LNVEEKGSP-VDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGaAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 92 VDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSH--- 168
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYdrg 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 169 -RVSTEDFLpFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDY 237
Cdd:cd01639 160 dNFDRYLNN-FAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDF 228
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
13-233 |
7.48e-46 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 154.81 E-value: 7.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 13 YRFACSLAESGGKLAYEFYqqRDSLQTLHKGSDLQ-DVVSRADCEVESFVKSRIAEAFPNDGFLGEESGtADEGKSVL-- 89
Cdd:pfam00459 6 LKVAVELAAKAGEILREAF--SNKLTIEEKGKSGAnDLVTAADKAAEELILEALAALFPSHKIIGEEGG-AKGDQTELtd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 90 ----WVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQI--SPHPATTVAGGVMG 163
Cdd:pfam00459 83 dgptWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLpvSRAPPLSEALLVTL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020427645 164 VGTSHRVSTEDfLPFLDQLLQH--GGMFVRNGSGALMSAWAAAGRLIGYYE-PHMNPWDGLPGIVLMREAGGI 233
Cdd:pfam00459 163 FGVSSRKDTSE-ASFLAKLLKLvrAPGVRRVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGV 234
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
16-249 |
6.39e-45 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 152.27 E-value: 6.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 16 ACSLAESGGKLAYEFYQQRDSLQTLHKGSDlqDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGT-ADEGKSVLWVVDP 94
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEASQKGSN--DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGElEGEDQDVQWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 95 IDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHRVS--T 172
Cdd:PRK10757 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKqhA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020427645 173 EDFLPFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEG-IARGNVV 249
Cdd:PRK10757 166 TTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNyMLTGNIV 243
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
14-249 |
1.55e-31 |
|
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: 117.02 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 14 RFACSLAESGGKLAYEFYQQrdSLQTLHKGSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADEGKSVL-WVV 92
Cdd:TIGR02067 3 AFAEDLADAAGETILPFFRA--SLLVVDKKSD-KTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERvWVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 93 DPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHRVST 172
Cdd:TIGR02067 80 DPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020427645 173 EDFLPfLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEGIARGNVV 249
Cdd:TIGR02067 160 PGNRP-AFERLRRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGGAV 235
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
11-266 |
9.87e-84 |
|
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: 251.30 E-value: 9.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 11 ARYRFACSLAESGGKLAYEFYQQRDsLQTLHKGSdlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTAD-EGKSVL 89
Cdd:COG0483 2 PLLELALRAARAAGALILRRFRELD-LEVETKGD--GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEgRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 90 WVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHR 169
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 170 VSTEDFLPFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEGIARGNVV 249
Cdd:COG0483 159 RDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSL 238
|
250
....*....|....*..
gi 2020427645 250 LLASEKIYPQLKQWVKQ 266
Cdd:COG0483 239 VAANPALHDELLALLRE 255
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-237 |
1.35e-65 |
|
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: 204.69 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 13 YRFACSLAESGGKLAYEFYQQRDsLQTLHKGSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESG-TADEGKSVLWV 91
Cdd:cd01639 2 LNIAIEAARKAGEILLEAYEKLG-LNVEEKGSP-VDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGaAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 92 VDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSH--- 168
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYdrg 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 169 -RVSTEDFLpFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDY 237
Cdd:cd01639 160 dNFDRYLNN-FAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDF 228
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
15-253 |
5.61e-65 |
|
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: 202.95 E-value: 5.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 15 FACSLAESGGKLAYEFYqqRDSLQTLHKGSdlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADEGKSVLWVVDP 94
Cdd:cd01643 3 LAEAIAQEAGDRALADF--GNSLSAETKAD--GSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWYWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 95 IDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHRVSTEd 174
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASAR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 175 flPFLDQLLQH-GGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGI-------TNDYLAAEGIARG 246
Cdd:cd01643 158 --AVLRVILRRfPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSwtildeePAFLQTKDYLSAG 235
|
....*..
gi 2020427645 247 NVVLLAS 253
Cdd:cd01643 236 FPTLIAA 242
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
13-237 |
8.31e-59 |
|
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: 187.14 E-value: 8.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 13 YRFACSLAESGGKLAYEFYQQRDSLQTlHKGSDlqDVVSRADCEVESFVKSRIAEAFPNDGFLGEESG--TADEGKSVLW 90
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVET-KKGDG--DLVTEADLAAEELIVDVLKALFPDDGILGEEGGgsGNVSDGGRVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 91 VVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHrv 170
Cdd:cd01637 78 VIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASM-- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020427645 171 STEDFLPFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDY 237
Cdd:cd01637 156 LRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDL 222
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
13-233 |
7.48e-46 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 154.81 E-value: 7.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 13 YRFACSLAESGGKLAYEFYqqRDSLQTLHKGSDLQ-DVVSRADCEVESFVKSRIAEAFPNDGFLGEESGtADEGKSVL-- 89
Cdd:pfam00459 6 LKVAVELAAKAGEILREAF--SNKLTIEEKGKSGAnDLVTAADKAAEELILEALAALFPSHKIIGEEGG-AKGDQTELtd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 90 ----WVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQI--SPHPATTVAGGVMG 163
Cdd:pfam00459 83 dgptWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLpvSRAPPLSEALLVTL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020427645 164 VGTSHRVSTEDfLPFLDQLLQH--GGMFVRNGSGALMSAWAAAGRLIGYYE-PHMNPWDGLPGIVLMREAGGI 233
Cdd:pfam00459 163 FGVSSRKDTSE-ASFLAKLLKLvrAPGVRRVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGV 234
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
16-249 |
6.39e-45 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 152.27 E-value: 6.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 16 ACSLAESGGKLAYEFYQQRDSLQTLHKGSDlqDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGT-ADEGKSVLWVVDP 94
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEASQKGSN--DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGElEGEDQDVQWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 95 IDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHRVS--T 172
Cdd:PRK10757 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKqhA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020427645 173 EDFLPFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEG-IARGNVV 249
Cdd:PRK10757 166 TTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNyMLTGNIV 243
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
15-236 |
2.32e-36 |
|
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: 127.51 E-value: 2.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 15 FACSLAESGGKLAYEFYQQRDSLQTLHKGSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADE----GKSVLW 90
Cdd:cd01636 3 ELCRVAKEAGLAILKAFGRELSGKVKITKSD-NDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEvmgrRDEYTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 91 VVDPIDGTSCFLNGLHTWCFSLAIVidgepVIGVVYDPNHhelfhackgqgawlndqqisphpattvaggvmgvgtshrv 170
Cdd:cd01636 82 VIDPIDGTKNFINGLPFVAVVIAVY-----VILILAEPSH---------------------------------------- 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020427645 171 STEDFLPFLDQLLQHgGMFVRNGSGALMSAWAAAGRLIGYYEPHM--NPWDGLPGIVLMREAGGITND 236
Cdd:cd01636 117 KRVDEKKAELQLLAV-YRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTD 183
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-236 |
3.14e-36 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 129.81 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 5 ENDSLLARYRFACSLAESGGK-LAYEFYQQRDslqTLHKGsdLQDVVSRADCEVESFVKSRIAEAFPNDGFLGEES---- 79
Cdd:PLN02553 3 QNDDLEQFLEVAVDAAKAAGQiIRKGFYQTKH---VEHKG--QVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaas 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 80 GTADEGKSVLWVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAG 159
Cdd:PLN02553 78 GGTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 160 GVMG--VGTSHRVSTEDFLPFLDQLLQHGGMFVR-NGSGALMSAWAAAGRLIGYYEPHM-NPWDGLPGIVLMREAGGITN 235
Cdd:PLN02553 158 ALLAteVGTKRDKATVDATTNRINALLYKVRSLRmSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVF 237
|
.
gi 2020427645 236 D 236
Cdd:PLN02553 238 D 238
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
19-236 |
5.70e-34 |
|
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: 123.10 E-value: 5.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 19 LAESGGKLAYEFYQqrdSLQTLHKGSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEEsgTADEGKSV----LWVVDP 94
Cdd:cd01638 8 IAREAGDAILEVYR---GGFTVERKED-GSPVTAADLAANAFIVEGLAALRPDIPVLSEE--SADDPLRLgwdrFWLVDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 95 IDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVA-GGVMGVGTSHRVSTE 173
Cdd:cd01638 82 LDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPpLQPLRVVASRSHPDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020427645 174 DFLPFLDQLLQHGgmFVRNGSGALMsAWAAAGRLIGYyePHMNP---WDGLPGIVLMREAGGITND 236
Cdd:cd01638 162 ELEALLAALGVAE--VVSIGSSLKF-CLVAEGEADIY--PRLGPtmeWDTAAGDAVLRAAGGAVSD 222
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
15-253 |
2.60e-33 |
|
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: 121.59 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 15 FACSLAESGGKLAYEFYQQRdsLQTLHKGSDlqDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADEGKSVLWVVDP 94
Cdd:cd01641 4 FALELADAAGQITLPYFRTR--LQVETKADF--SPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYVWVLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 95 IDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQqiSPHPATTVAGGVMGVGTSHRVSTED 174
Cdd:cd01641 80 IDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGA--GGRPLRVRACADLAEAVLSTTDPHF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 175 FLP-----FLDQLLQHGgmFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEGIARGNVV 249
Cdd:cd01641 158 FTPgdraaFERLARAVR--LTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRV 235
|
....
gi 2020427645 250 LLAS 253
Cdd:cd01641 236 VAAG 239
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
16-236 |
5.88e-32 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 118.34 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 16 ACSLAESGGKLAYEFYQQrdSLQTLHKgSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTAD----EGKSVLWV 91
Cdd:COG1218 8 AIEIAREAGEAILEIYRA--DFEVEEK-AD-DSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPyeerKSWDRFWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 92 VDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLND-----QQISPHPATTVAGGVMGVGT 166
Cdd:COG1218 84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerQPIRVRDRPPAEPLRVVASR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020427645 167 SHRvsTEDFLPFLDQLLQHGgmFVRNGSGaLMSAWAAAGRlIGYYePHMNP---WDGLPGIVLMREAGGITND 236
Cdd:COG1218 164 SHR--DEETEALLARLGVAE--LVSVGSS-LKFCLVAEGE-ADLY-PRLGPtmeWDTAAGQAILEAAGGRVTD 229
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
14-249 |
1.55e-31 |
|
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: 117.02 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 14 RFACSLAESGGKLAYEFYQQrdSLQTLHKGSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADEGKSVL-WVV 92
Cdd:TIGR02067 3 AFAEDLADAAGETILPFFRA--SLLVVDKKSD-KTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERvWVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 93 DPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVMGVGTSHRVST 172
Cdd:TIGR02067 80 DPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020427645 173 EDFLPfLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGGITNDYLAAEGIARGNVV 249
Cdd:TIGR02067 160 PGNRP-AFERLRRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGGAV 235
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
47-260 |
1.60e-29 |
|
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: 112.41 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 47 QDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADegkSVLWVVDPIDGTSCFLNGLhtwCF--SLAIVIDGEPVIGV 124
Cdd:cd01517 35 KSPVTVADYGAQALITAALARLFPSDPIVGEEDSAAL---GRFWVLDPIDGTKGFLRGD---QFavALALIEDGEVVLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 125 VYDPNH-------HELFHACKGQGAWLNDQQIS---PHPATTVAGGVMGVGTSHRVSTEDFLPFLDQLLQHGGMfvrNGS 194
Cdd:cd01517 109 IGCPNLplddgggGDLFSAVRGQGAWLRPLDGSslqPLSVRQLTNAARASFCESVESAHSSHRLQAAIKALGGT---PQP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 195 GALMS----AWAAAGRL-IGYYEPH-----MNPWDGLPGIVLMREAGGITNDylaAEG----------IARGNVVLLASE 254
Cdd:cd01517 186 VRLDSqakyAAVARGAAdFYLRLPLsmsyrEKIWDHAAGVLIVEEAGGKVTD---ADGkpldfgkgrkLLNNGGLIAAPG 262
|
....*.
gi 2020427645 255 KIYPQL 260
Cdd:cd01517 263 EIHEQV 268
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
17-237 |
6.77e-21 |
|
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: 88.66 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 17 CSLAESGGKLAYEFYQQrdSLQTLHKgSDlQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTA-----DEGKSvLWV 91
Cdd:TIGR01331 6 IKIARAAGEEILPVYQK--ELAVAQK-AD-NSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIpltprQTWQR-FWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 92 VDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWL--NDQ----QISPHPATTVAggvMGVG 165
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegDGQalkaPIHVRPWPSGP---LLVV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020427645 166 TSHRVSTEDFLPFLDQLlqhGGMFVRNGSGALMSAWAAAGRLIGYyePHMNP---WDGLPGIVLMREAGGITNDY 237
Cdd:TIGR01331 158 ISRSHAEEKTTEYLANL---GYDLRTSGGSSLKFCLVAEGSADIY--PRLGPtgeWDTAAGHAVLAAAGGAIFDL 227
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
65-236 |
5.50e-18 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 81.11 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 65 IAEAFPNDGF----LGEESGTA-DEGKSVLWVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKG 139
Cdd:PRK12676 54 ILEVLKPLGRcvniISEELGEIvGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 140 QGAWLNDQQISPHPATTVAGGVMGVGTSHRvSTEDflpfLDQLLQHggmfVRN----GSGALMSAWAAAGRLIGYYE--P 213
Cdd:PRK12676 134 KGAYLNGKPIKVSKTSELNESAVSIYGYRR-GKER----TVKLGRK----VRRvrilGAIALELCYVASGRLDAFVDvrN 204
|
170 180
....*....|....*....|...
gi 2020427645 214 HMNPWDGLPGIVLMREAGGITND 236
Cdd:PRK12676 205 YLRVTDIAAGKLICEEAGGIVTD 227
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-178 |
2.71e-17 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 79.76 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 6 NDSLLARY-RFACSLAESGGKLAYEFYQQRdsLQTLHKgSDLQDVvSRADCEVESFVKSRIAEAFPNDGFLGEESG--TA 82
Cdd:PLN02911 29 SDAVLDRFvDVAHKLADAAGEVTRKYFRTK--FEIIDK-EDLSPV-TIADRAAEEAMRSIILENFPSHAIFGEEHGlrCG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 83 DEGKSVLWVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGVVYDPNHHELFHACKGQGAWLNDQQISPHPATTVAGGVM 162
Cdd:PLN02911 105 EGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYL 184
|
170
....*....|....*.
gi 2020427645 163 GVGTSHRVSTEDFLPF 178
Cdd:PLN02911 185 YTTSPHMFSGDAEDAF 200
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
46-232 |
3.26e-17 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 80.23 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 46 LQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESG-TADEGKSVLWVVDPIDGTSCFLNGLHTWCFSLAIVIDGEPVIGV 124
Cdd:PLN02737 109 LTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGvIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAAT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 125 VYD----PN--HHELFHACKGQGAWLNDQQISPHPATTVAGG--VMGVGTSHR----VSTEDFLPFLDqlLQHGgmfVRN 192
Cdd:PLN02737 189 VVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSllVTGFGYEHDdawaTNIELFKEFTD--VSRG---VRR 263
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2020427645 193 -GSGALMSAWAAAGRLIGYYEPHMNPWDGLPGIVLMREAGG 232
Cdd:PLN02737 264 lGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGG 304
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
75-236 |
8.13e-15 |
|
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: 72.02 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 75 LGEESGTADEGKSVLW--VVDPIDGTSCFLNGLHTWCFSLAIV-IDGE-PVIGVVYDPNHHELFHACKGQGAWLNDQQIS 150
Cdd:cd01515 62 VSEEIGVIDNGDEPEYtvVLDPLDGTYNAINGIPFYSVSVAVFkIDKSdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 151 ---PHPATTVAGGVMGVGTSHRVSTEDFLPFLDqllqhggmfVRN-GSGALMSAWAAAGRLIGYYE--PHMNPWDGLPGI 224
Cdd:cd01515 142 vsdFSSLKSISVSYYIYGKNHDRTFKICRKVRR---------VRIfGSVALELCYVASGALDAFVDvrENLRLVDIAAGY 212
|
170
....*....|..
gi 2020427645 225 VLMREAGGITND 236
Cdd:cd01515 213 LIAEEAGGIVTD 224
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
17-143 |
1.05e-11 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 63.17 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 17 CSLAESGGKLAYEFYQQRDSLQTLHKGSDlqDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADEGK---SVLWVVD 93
Cdd:PRK10931 6 CQLARNAGDAIMQVYDGTKPLDVASKADD--SPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRqhwQRYWLVD 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2020427645 94 PIDGTSCFL--NGLHTwcFSLAIVIDGEPVIGVVYDPNHHELFHACKGQgAW 143
Cdd:PRK10931 84 PLDGTKEFIkrNGEFT--VNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AW 132
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
18-145 |
1.76e-07 |
|
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: 51.17 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 18 SLAESGGKLAYEFYQQRDSLQTLHKGSD---LQDVVSRADCEVESFVKSRIAEAFPNDGFLGEESGTADEGKSVLWV--- 91
Cdd:cd01640 7 AVAEKAGGIARDVVKKGRLLILLVEGKTkegANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDvdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 92 ------------------------VDPIDGTSCFLNGLHTWCFSLA-IVIDGEPVIGVVYDPnhhelFHACK-GQGAWLN 145
Cdd:cd01640 87 deeileescpspskdlpeedlgvwVDPLDATQEYTEGLLEYVTVLIgVAVKGKPIAGVIHQP-----FYEKTaGAGAWLG 161
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
50-236 |
2.67e-07 |
|
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: 51.02 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 50 VSRADCEVESFVKSRIAEAFPNDGFLGEE-SGTADEGKSVL--------------------------------------- 89
Cdd:TIGR01330 44 VTVGDYGAQAIVINVLKSNFPDDPIVGEEdSSGLSEADFTLgrvnelvnetlvyaknykkddqfplksledvlqiidfgn 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 90 ---------WVVDPIDGTSCFLNGlHTWCFSLAIVIDGEPVIGVVYDPN------------HHE----LFHACKGQGAWL 144
Cdd:TIGR01330 124 yeggrkgrhWVLDPIDGTKGFLRG-DQYAVCLALIENGKVVLGVIGCPNlplssygaqnlkGSEskgcIFRAVRGSGAFM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 145 NDQQISPHPATTV----------AGGVMGVGTSHrvSTEDFLPFLDQLLQHGGMFVRNGSGALMSAWAAAGRLIGYYEPH 214
Cdd:TIGR01330 203 YSLSSDAESPTKVhvssvkdtkdAIFCEGVEKGH--SSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPI 280
|
250 260
....*....|....*....|....*..
gi 2020427645 215 MNP-----WDGLPGIVLMREAGGITND 236
Cdd:TIGR01330 281 KLSyqekiWDHAAGNVIVEEAGGIVTD 307
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
65-237 |
1.56e-06 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 48.96 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 65 IAEAFPNDGFLGEESGTADEGKSVL---WVVDPIDGTSCFLNGLHTWCFSLAIV-IDGEPV----------------IGV 124
Cdd:PRK14076 56 SLEKFCSGILISEEIGFKKIGKNKPeyiFVLDPIDGTYNALKDIPIYSASIAIAkIDGFDKkikefigknltindleVGV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020427645 125 VYDPNHHELFHACKGQGAWL--NDQQISPHPATTVAGGVMGVGTSHRVSTEDFLPFLDqllqhgGMFVRN----GSGALM 198
Cdd:PRK14076 136 VKNIATGDTYYAEKGEGAYLlkKGEKKKIEISNISNLKDASIGLFAYGLSLDTLKFIK------DRKVRRirlfGSIALE 209
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2020427645 199 SAWAAAGRLIGYYEPHMNP--WDGLPGIVLMREAGG-ITNDY 237
Cdd:PRK14076 210 MCYVASGALDAFINVNETTrlCDIAAGYVICKEAGGiITNKN 251
|
|
| |
