|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-237 |
7.34e-73 |
|
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: 222.57 E-value: 7.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 5 FNFAKHIVLNAASYIKEHLNDQLQIETKSSPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISD-GNVWVID 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDgGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 84 PIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGGGQFDVYCNEQKLLPYQDRPLNQFLMASNAGIFERND 163
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064716 164 W-GIADLAKETLGVRVYGSAAISFSKVLSGQLLTYISYIW-PWDYAAASIMGDKLGYMTLTFEGEEPDFESHQGIM 237
Cdd:cd01637 161 AaVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLnPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGII 236
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-232 |
4.01e-54 |
|
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: 175.03 E-value: 4.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 6 NFAKHIVLNAASYIKEHL-NDQLQIETKSsPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISDGNVWVIDP 84
Cdd:COG0483 5 ELALRAARAAGALILRRFrELDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 85 IDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGqfdVYCNEQKLLPYQDRPLNQFLMA-SNAGIFE 160
Cdd:COG0483 84 IDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTaarGGG---AFLNGRRLRVSARTDLEDALVAtGFPYLRD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568064716 161 RNDWG--IADLAKETLGVRVYGSAAISFSKVLSGQLLTYISY-IWPWDYAAASIM----GdklGYMTlTFEGEEPDFES 232
Cdd:COG0483 161 DREYLaaLAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAgLKPWDIAAGALIvreaG---GVVT-DLDGEPLDLGS 235
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-236 |
5.10e-40 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 139.40 E-value: 5.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 6 NFAKHIVLNAASYIKEHLNDQLQIETKS--SPTDLVTQMDKEVQDNLVTWILEAYPADHILAEE----NGLRHSISDGNV 79
Cdd:pfam00459 7 KVAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTELTDDGPT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 80 WVIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGQFdvyCNEQKLLPYQDRPLNQFLMASNA 156
Cdd:pfam00459 87 WIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSaakGKGAF---LNGQPLPVSRAPPLSEALLVTLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 157 GIFERNDWGIADLAK--ETL----GVRVYGSAAISFSKVLSGQLLTYI--SYIWPWDYAAASIMGDKLGYMTLTFEGEEP 228
Cdd:pfam00459 164 GVSSRKDTSEASFLAklLKLvrapGVRRVGSAALKLAMVAAGKADAYIefGRLKPWDHAAGVAILREAGGVVTDADGGPF 243
|
....*...
gi 568064716 229 DFESHQGI 236
Cdd:pfam00459 244 DLLAGRVI 251
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
16-227 |
2.33e-17 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 80.23 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 16 ASYIKEHLNDQLQIETKSSpTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISDGNVWVIDPIDGTNNFVAQK 95
Cdd:PLN02737 91 AEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCIDPLDGTTNFAHGY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 96 ADFAVVLAYFENGIGQFGVIYDVIGDKL---------YHGGGQFdvyCNEQKLLPYQDRPLNQFLMASNAGiFERND-WG 165
Cdd:PLN02737 170 PSFAVSVGVLFRGTPAAATVVEFVGGPMcwntrtfsaSAGGGAF---CNGQKIHVSQTDKVERSLLVTGFG-YEHDDaWA 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568064716 166 I-ADLAKE----TLGVRVYGSAAISFSKVLSGQLLTYISY-IWPWDYAAASIMGDKLGYMTLTFEGEE 227
Cdd:PLN02737 246 TnIELFKEftdvSRGVRRLGAAAVDMCHVALGIVEAYWEYrLKPWDMAAGVLIVEEAGGTVTRMDGGK 313
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
11-225 |
8.81e-15 |
|
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: 71.71 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 11 IVLNAASYIKEHLNDQLQIETKSSPTDlVTQMDKEVQDNLVTWILEAYPADHILAEEN---GLRHSISDGNVWVIDPIDG 87
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDasiPLTPRQTWQRFWLVDPLDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 88 TNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGQFDVYCNEQKLLPYQDRPL---NQFLMASNAGIFER 161
Cdd:TIGR01331 87 TKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFataGKAAKREGDGQALKAPIHVRPWpsgPLLVVISRSHAEEK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568064716 162 NDWGIADLAKEtlgVRVYGSAAISFSKVLSGQLLTYISyIWP---WDYAAASIMGDKLGYMTLTFEG 225
Cdd:TIGR01331 167 TTEYLANLGYD---LRTSGGSSLKFCLVAEGSADIYPR-LGPtgeWDTAAGHAVLAAAGGAIFDLDG 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-237 |
7.34e-73 |
|
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: 222.57 E-value: 7.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 5 FNFAKHIVLNAASYIKEHLNDQLQIETKSSPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISD-GNVWVID 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDgGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 84 PIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGGGQFDVYCNEQKLLPYQDRPLNQFLMASNAGIFERND 163
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064716 164 W-GIADLAKETLGVRVYGSAAISFSKVLSGQLLTYISYIW-PWDYAAASIMGDKLGYMTLTFEGEEPDFESHQGIM 237
Cdd:cd01637 161 AaVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLnPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGII 236
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-232 |
4.01e-54 |
|
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: 175.03 E-value: 4.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 6 NFAKHIVLNAASYIKEHL-NDQLQIETKSsPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISDGNVWVIDP 84
Cdd:COG0483 5 ELALRAARAAGALILRRFrELDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 85 IDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGqfdVYCNEQKLLPYQDRPLNQFLMA-SNAGIFE 160
Cdd:COG0483 84 IDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTaarGGG---AFLNGRRLRVSARTDLEDALVAtGFPYLRD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568064716 161 RNDWG--IADLAKETLGVRVYGSAAISFSKVLSGQLLTYISY-IWPWDYAAASIM----GdklGYMTlTFEGEEPDFES 232
Cdd:COG0483 161 DREYLaaLAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAgLKPWDIAAGALIvreaG---GVVT-DLDGEPLDLGS 235
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
5-233 |
3.74e-46 |
|
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: 154.23 E-value: 3.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 5 FNFAKHIVLNAASYIKEHL-NDQLQIETKSSPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISDGNVWVID 83
Cdd:cd01639 2 LNIAIEAARKAGEILLEAYeKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 84 PIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGQFdvyCNEQKLLPYQDRPLNQFLMASNAGiFE 160
Cdd:cd01639 82 PLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTavrGQGAF---LNGRRIRVSGRKELKDALVATGFP-YD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 161 RNDWG-------IADLAKETLGVRVYGSAAISFSKVLSGQL-LTYISYIWPWDYAAASIM----GdklGYMTlTFEGEEP 228
Cdd:cd01639 158 RGDNFdrylnnfAKLLAKAVRGVRRLGSAALDLAYVAAGRLdGYWERGLKPWDVAAGALIvreaG---GLVT-DFDGGPF 233
|
....*
gi 568064716 229 DFESH 233
Cdd:cd01639 234 DLMSG 238
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-236 |
5.10e-40 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 139.40 E-value: 5.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 6 NFAKHIVLNAASYIKEHLNDQLQIETKS--SPTDLVTQMDKEVQDNLVTWILEAYPADHILAEE----NGLRHSISDGNV 79
Cdd:pfam00459 7 KVAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTELTDDGPT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 80 WVIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGQFdvyCNEQKLLPYQDRPLNQFLMASNA 156
Cdd:pfam00459 87 WIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSaakGKGAF---LNGQPLPVSRAPPLSEALLVTLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 157 GIFERNDWGIADLAK--ETL----GVRVYGSAAISFSKVLSGQLLTYI--SYIWPWDYAAASIMGDKLGYMTLTFEGEEP 228
Cdd:pfam00459 164 GVSSRKDTSEASFLAklLKLvrapGVRRVGSAALKLAMVAAGKADAYIefGRLKPWDHAAGVAILREAGGVVTDADGGPF 243
|
....*...
gi 568064716 229 DFESHQGI 236
Cdd:pfam00459 244 DLLAGRVI 251
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-234 |
1.46e-32 |
|
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: 118.98 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 5 FNFAKHIVLNAASYIKEHLNDQLQIETKSsPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSiSDGNVWVIDP 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFP-SSGWYWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 85 IDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGGGQFDVYCNEQKLLPYQDRPLnqflmaSNAGIFERNDW 164
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQL------PDCNVGFNRSS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568064716 165 GIADLAKETL-------GVRVYGSAAISFSKVLSGQLLTYIS-YIWPWDYAAASIMGDKLGYMTLTFEGEEPDFESHQ 234
Cdd:cd01643 153 RASARAVLRVilrrfpgKIRMLGSASLNLASVAAGQTLGYVEaTPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKD 230
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
6-208 |
3.94e-19 |
|
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: 83.46 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 6 NFAKHIVLNAASYIKEHLNDQLQIETK--SSPtdlVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISdGNVWVID 83
Cdd:cd01641 3 AFALELADAAGQITLPYFRTRLQVETKadFSP---VTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDA-GYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 84 PIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGGGQFDVYCNEQKLLPYQDRP---LNQ-FLMASNAGIF 159
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVRAcadLAEaVLSTTDPHFF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568064716 160 ERNDWGIADLAKETLGVRVYGSAAISFSKVLSGQL-LTYISYIWPWDYAA 208
Cdd:cd01641 159 TPGDRAAFERLARAVRLTRYGGDCYAYALVASGRVdLVVEAGLKPYDVAA 208
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
8-209 |
6.43e-19 |
|
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: 82.66 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 8 AKHIVLNAASYIKEHLNDQLQIETKSsPTDLVTQMDKEVQDNLVTWILEAYPADHILAEEN-GLRHSISDGNVWVIDPID 86
Cdd:cd01638 5 LIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESaDDPLRLGWDRFWLVDPLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 87 GTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGGGQFDVYCNEQKL---LPYQDRPLNQFLM-ASNAgifeRN 162
Cdd:cd01638 84 GTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGavsLQARPPPLQPLRVvASRS----HP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568064716 163 DWGIADLAKEtLGVRVYGSAAIS--FSKVLSGQLLTYISYIWP--WDYAAA 209
Cdd:cd01638 160 DEELEALLAA-LGVAEVVSIGSSlkFCLVAEGEADIYPRLGPTmeWDTAAG 209
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
8-127 |
6.76e-19 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 83.29 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 8 AKHIVLNAASYIKEHLNDQLQIETKS--SPtdlVTQMDKEVQDnlvtWILEA----YPADHILAEEN---GLRHSISDGN 78
Cdd:COG1218 8 AIEIAREAGEAILEIYRADFEVEEKAddSP---VTEADLAAHA----IILAGlaalTPDIPVLSEESaaiPYEERKSWDR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568064716 79 VWVIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGG 127
Cdd:COG1218 81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAA 129
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
16-227 |
2.33e-17 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 80.23 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 16 ASYIKEHLNDQLQIETKSSpTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISDGNVWVIDPIDGTNNFVAQK 95
Cdd:PLN02737 91 AEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCIDPLDGTTNFAHGY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 96 ADFAVVLAYFENGIGQFGVIYDVIGDKL---------YHGGGQFdvyCNEQKLLPYQDRPLNQFLMASNAGiFERND-WG 165
Cdd:PLN02737 170 PSFAVSVGVLFRGTPAAATVVEFVGGPMcwntrtfsaSAGGGAF---CNGQKIHVSQTDKVERSLLVTGFG-YEHDDaWA 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568064716 166 I-ADLAKE----TLGVRVYGSAAISFSKVLSGQLLTYISY-IWPWDYAAASIMGDKLGYMTLTFEGEE 227
Cdd:PLN02737 246 TnIELFKEftdvSRGVRRLGAAAVDMCHVALGIVEAYWEYrLKPWDMAAGVLIVEEAGGTVTRMDGGK 313
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
31-230 |
5.06e-17 |
|
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: 78.12 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 31 TKSSPTDLVTQMDKEVQdNLVTWIL-EAYPADHILAEENglrhSISDGNVWVIDPIDGTNNFVAQKAdFAVVLAYFENGI 109
Cdd:cd01517 30 WKKSDKSPVTVADYGAQ-ALITAALaRLFPSDPIVGEED----SAALGRFWVLDPIDGTKGFLRGDQ-FAVALALIEDGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 110 GQFGVIYD-------VIGDKLY---HGGGQFDVYCNEQKLLPYQDRPL-NQFLMASNAGIfernDWGIADLAKETLGVRV 178
Cdd:cd01517 104 VVLGVIGCpnlplddGGGGDLFsavRGQGAWLRPLDGSSLQPLSVRQLtNAARASFCESV----ESAHSSHRLQAAIKAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064716 179 YGSAA-------ISFSKVLSGQLLTYI-------SYIWPWDYAAASIMGDKLGYMTLTFEGEEPDF 230
Cdd:cd01517 180 GGTPQpvrldsqAKYAAVARGAADFYLrlplsmsYREKIWDHAAGVLIVEEAGGKVTDADGKPLDF 245
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-225 |
9.59e-17 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 77.54 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 1 MEKKFNFAKHIVLNAASYIKEHLN--DQLQIETKSSpTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGlRHSISDGN 78
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYEtpDAVEASQKGS-NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESG-ELEGEDQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 79 V-WVIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHG----GGQFDVY----CNEQKL--------LP 141
Cdd:PRK10757 79 VqWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTAtrgqGAQLNGYrlrgSTARDLdgtilatgFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 142 YQDRPLNQFLMASNAGIFERndwgIADLaketlgvRVYGSAAISFSKVLSGQLLTYISY-IWPWDYAAASIMGDKLGYMT 220
Cdd:PRK10757 159 FKAKQHATTYINIVGKLFTE----CADF-------RRTGSAALDLAYVAAGRVDGFFEIgLKPWDFAAGELLVREAGGIV 227
|
....*
gi 568064716 221 LTFEG 225
Cdd:PRK10757 228 SDFTG 232
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
11-225 |
8.81e-15 |
|
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: 71.71 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 11 IVLNAASYIKEHLNDQLQIETKSSPTDlVTQMDKEVQDNLVTWILEAYPADHILAEEN---GLRHSISDGNVWVIDPIDG 87
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDasiPLTPRQTWQRFWLVDPLDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 88 TNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYH---GGGQFDVYCNEQKLLPYQDRPL---NQFLMASNAGIFER 161
Cdd:TIGR01331 87 TKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFataGKAAKREGDGQALKAPIHVRPWpsgPLLVVISRSHAEEK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568064716 162 NDWGIADLAKEtlgVRVYGSAAISFSKVLSGQLLTYISyIWP---WDYAAASIMGDKLGYMTLTFEG 225
Cdd:TIGR01331 167 TTEYLANLGYD---LRTSGGSSLKFCLVAEGSADIYPR-LGPtgeWDTAAGHAVLAAAGGAIFDLDG 229
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
27-130 |
1.59e-13 |
|
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: 68.10 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 27 LQIETKSSPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSISDGNVWVIDPIDGTNNFVAQKADFAVVLAYFE 106
Cdd:TIGR02067 24 LLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVE 103
|
90 100
....*....|....*....|....*.
gi 568064716 107 NGIGQFGVIYDVIGDKLY--HGGGQF 130
Cdd:TIGR02067 104 GGMPVLGVIFQPATGERWwaAGGGAA 129
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
14-212 |
1.61e-13 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 68.56 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 14 NAASYIKEHLNDQLQIETKSSpTDLVTQMDKEVQDNLVTWILEAYPADHILAEE----NGLRhSISDGNVWVIDPIDGTN 89
Cdd:PLN02553 20 AAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEEttaaSGGT-ELTDEPTWIVDPLDGTT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 90 NFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLY---HGGGQFdvyCNEQKLLPYQDRPLNQFLMASNAG--------- 157
Cdd:PLN02553 98 NFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFtavKGKGAF---LNGKPIKASSQSELGKALLATEVGtkrdkatvd 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568064716 158 -IFERndwgIADLAKETLGVRVYGSAAISFSKVLSGQL-LTY-ISYIWPWDYAAASIM 212
Cdd:PLN02553 175 aTTNR----INALLYKVRSLRMSGSCALNLCGVACGRLdIFYeIGFGGPWDVAAGAVI 228
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
6-223 |
3.69e-13 |
|
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: 65.88 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 6 NFAKHIVLNAAS----YIKEHLNDQLQIetKSSPTDLVTQMDKEVQDNLVTWILEAYPADHILAEENGLRHSIS---DGN 78
Cdd:cd01636 2 EELCRVAKEAGLailkAFGRELSGKVKI--TKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMgrrDEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 79 VWVIDPIDGTNNFVAQKADFAVVLAyfengigqFGVIYdvIGDKLYHgggqfdvycneqkllpyQDRPLNQFLMASNAGi 158
Cdd:cd01636 80 TWVIDPIDGTKNFINGLPFVAVVIA--------VYVIL--ILAEPSH-----------------KRVDEKKAELQLLAV- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568064716 159 ferndwgiadlaketLGVRVYGSAAISFSKVLSGQLLTYIS---YIWPWDYAAASIMGDKLGYMTLTF 223
Cdd:cd01636 132 ---------------YRIRIVGSAVAKMCLVALGLADIYYEpggKRRAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
1-115 |
1.61e-12 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 65.90 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 1 MEKKFNFAKHIVLNAASYIKEHLNDQLQIETK--SSPtdlVTQMDKEVQDNLVTWILEAYPADHILAEENGLR--HSISD 76
Cdd:PLN02911 33 LDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKedLSP---VTIADRAAEEAMRSIILENFPSHAIFGEEHGLRcgEGSSD 109
|
90 100 110
....*....|....*....|....*....|....*....
gi 568064716 77 gNVWVIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVI 115
Cdd:PLN02911 110 -YVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGII 147
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
63-194 |
7.48e-10 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 57.61 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 63 ILAEENGLrhSISDGNVW--VIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHG-GGQFdVYCNEQKL 139
Cdd:PRK12676 67 IISEELGE--IVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAiPGKG-AYLNGKPI 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568064716 140 LPYQDRPLNQFLMASNAGIFERNDwgIADLAKETLGVRVYGSAAISFSKVLSGQL 194
Cdd:PRK12676 144 KVSKTSELNESAVSIYGYRRGKER--TVKLGRKVRRVRILGAIALELCYVASGRL 196
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
62-217 |
1.10e-06 |
|
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: 48.21 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 62 HILAEENGLRHSISDGNVWVIDPIDGTNNFVAQKADFAVVLAYFENGIGQ-----FGVIYDVIGDKLYHGGGQFdVYCNE 136
Cdd:cd01642 59 QIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVkaatlDNFVSGEGGLKVYSPPTRF-SYISV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 137 QKLLPYQDRPLnqflmASNAGIFE---RNDWGIADLAKETLGVRVYGSAAISFSKVLSGQLLTYI---SYIWPWDYAAAS 210
Cdd:cd01642 138 PKLGPPLVPEV-----PSKIGIYEgssRNPEKFLLLSRNGLKFRSLGSAALELAYTCEGSFVLFLdlrGKLRNFDVAAAL 212
|
....*..
gi 568064716 211 IMGDKLG 217
Cdd:cd01642 213 GACKRLG 219
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
35-230 |
2.03e-06 |
|
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: 47.76 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 35 PTDLVtqmDKeVQDNLVTWILEAYPADHILAEENG-LRHSISDGNVWVIDPIDGTNNFVAQKADFAVVLAYFENGIGQ-- 111
Cdd:cd01515 37 PTKLI---DK-VAEDAAIEILKKLGSVNIVSEEIGvIDNGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDpy 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 112 FGVIYDVIGDKLYHGGGQFDVYCNEQKLLPYQDRPLNQFLmaSNAGIFERNDWGIADLAKETLGVRVYGSAAISFSKVLS 191
Cdd:cd01515 113 YGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSIS--VSYYIYGKNHDRTFKICRKVRRVRIFGSVALELCYVAS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568064716 192 GQLLTYIS---YIWPWDYAAASIMGDKLGYMTLTFEGEEPDF 230
Cdd:cd01515 191 GALDAFVDvreNLRLVDIAAGYLIAEEAGGIVTDENGKELKL 232
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
1-115 |
2.24e-06 |
|
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: 47.94 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 1 MEKKFNFAKHIVLNAASYIKE-----HLNDQLQIETKS--SPtdlVTQMDKEVQdNLVTWIL-EAYPADHILAEENG--- 69
Cdd:TIGR01330 2 LERELDVATQAVRLASLLTKKvqselISHKDSTVITKDdkSP---VTVGDYGAQ-AIVINVLkSNFPDDPIVGEEDSsgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064716 70 -------------------------------------LRHSISDGN--------VWVIDPIDGTNNFVaQKADFAVVLAY 104
Cdd:TIGR01330 78 seadftlgrvnelvnetlvyaknykkddqfplksledVLQIIDFGNyeggrkgrHWVLDPIDGTKGFL-RGDQYAVCLAL 156
|
170
....*....|.
gi 568064716 105 FENGIGQFGVI 115
Cdd:TIGR01330 157 IENGKVVLGVI 167
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
80-128 |
6.69e-05 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 43.14 E-value: 6.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568064716 80 WVIDPIDGTNNFVAQKADFAVVLAYFENGIGQFGVIYDVIGDKLYHGGG 128
Cdd:PRK10931 80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAE 128
|
|
| |
