|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
8-248 |
3.30e-109 |
|
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: 315.02 E-value: 3.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 8 DEIAKKWIREAGARIKQSMHESLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSLEGVVWIID 87
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 88 PIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATWVTENR 167
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 168 ridQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLENHSVLA 247
Cdd:cd01637 161 ---AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIA 237
|
.
gi 504289601 248 G 248
Cdd:cd01637 238 A 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
5-258 |
1.17e-98 |
|
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: 289.05 E-value: 1.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 5 TEIDEIAKKWIREAGARIKQSMHE-SLTIETKSnPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqGDKIHSLEGVV 83
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES-GASEGRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 84 WIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATWV 163
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 164 TENRRiDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFtFLENH 243
Cdd:COG0483 159 RDDRE-YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPL-DLGSG 236
|
250
....*....|....*
gi 504289601 244 SVLAGNPSIHKTIFE 258
Cdd:COG0483 237 SLVAANPALHDELLA 251
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
3-255 |
4.38e-82 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 247.26 E-value: 4.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 3 NWTEIDEIAKKWIREAGARIKQSMHESLTIETKS--NPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqGDKIHSLE 80
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEG-GAKGDQTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 81 ----GVVWIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAIL 156
Cdd:pfam00459 80 ltddGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 157 AINATWVTENRRIDQSVLAPLVKRVR--GTRSYGSAALELANVAAGRIDAYITM-RLAPWDYAAGCVLLNEVGGIYTTIE 233
Cdd:pfam00459 160 VTLFGVSSRKDTSEASFLAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFgRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|..
gi 504289601 234 GEPFTfLENHSVLAGNPSIHKT 255
Cdd:pfam00459 240 GGPFD-LLAGRVIAANPKVLHE 260
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
10-259 |
1.91e-47 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 158.82 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 10 IAKKWIREAGARIKQSMHESLTIET-KSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEgQGDKIHSLEGVVWIIDP 88
Cdd:PRK10757 7 IAVRAARKAGNLIAKNYETPDAVEAsQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEE-SGELEGEDQDVQWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 89 IDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATW-VTENR 167
Cdd:PRK10757 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFkAKQHA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 168 RIDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEpFTFLENHSVLA 247
Cdd:PRK10757 166 TTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGG-HNYMLTGNIVA 244
|
250
....*....|..
gi 504289601 248 GNPSIHKTIFEE 259
Cdd:PRK10757 245 GNPRVVKAMLAN 256
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
16-251 |
9.19e-30 |
|
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: 112.16 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 16 REAGARIKQSMHESLTIETKSNpNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQ--GDKIHSLEGVVWIIDPIDGTM 93
Cdd:TIGR01331 10 RAAGEEILPVYQKELAVAQKAD-NSPVTEADRAAHRFILEGLRALTPDIPVLSEEDAsiPLTPRQTWQRFWLVDPLDGTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 94 NFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNetklapLKETVIEEAILAINatWVTENRR--IDQ 171
Cdd:TIGR01331 89 EFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRE------GDGQALKAPIHVRP--WPSGPLLvvISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 172 SVLAPLVKRVRGTRSY-----GSAALELANVAAGRIDAYItmRLAP---WDYAAGCVLLNEVGGIYTTIEGEPFTFLENH 243
Cdd:TIGR01331 161 SHAEEKTTEYLANLGYdlrtsGGSSLKFCLVAEGSADIYP--RLGPtgeWDTAAGHAVLAAAGGAIFDLDGSPLLYGKRE 238
|
....*...
gi 504289601 244 SVLagNPS 251
Cdd:TIGR01331 239 SFR--NPN 244
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
8-248 |
3.30e-109 |
|
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: 315.02 E-value: 3.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 8 DEIAKKWIREAGARIKQSMHESLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSLEGVVWIID 87
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 88 PIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATWVTENR 167
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 168 ridQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLENHSVLA 247
Cdd:cd01637 161 ---AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIA 237
|
.
gi 504289601 248 G 248
Cdd:cd01637 238 A 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
5-258 |
1.17e-98 |
|
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: 289.05 E-value: 1.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 5 TEIDEIAKKWIREAGARIKQSMHE-SLTIETKSnPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqGDKIHSLEGVV 83
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES-GASEGRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 84 WIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATWV 163
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 164 TENRRiDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFtFLENH 243
Cdd:COG0483 159 RDDRE-YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPL-DLGSG 236
|
250
....*....|....*
gi 504289601 244 SVLAGNPSIHKTIFE 258
Cdd:COG0483 237 SLVAANPALHDELLA 251
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
9-249 |
2.87e-83 |
|
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: 249.38 E-value: 2.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 9 EIAKKWIREAGARIKQSMHE-SLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqGDKIHSLEGVVWIID 87
Cdd:cd01639 3 NIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES-GAAGGLTDEPTWIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 88 PIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILA--INATWVTE 165
Cdd:cd01639 82 PLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVAtgFPYDRGDN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 166 NRRIDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFtFLENHSV 245
Cdd:cd01639 162 FDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPF-DLMSGNI 240
|
....
gi 504289601 246 LAGN 249
Cdd:cd01639 241 LAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
3-255 |
4.38e-82 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 247.26 E-value: 4.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 3 NWTEIDEIAKKWIREAGARIKQSMHESLTIETKS--NPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqGDKIHSLE 80
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEG-GAKGDQTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 81 ----GVVWIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAIL 156
Cdd:pfam00459 80 ltddGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 157 AINATWVTENRRIDQSVLAPLVKRVR--GTRSYGSAALELANVAAGRIDAYITM-RLAPWDYAAGCVLLNEVGGIYTTIE 233
Cdd:pfam00459 160 VTLFGVSSRKDTSEASFLAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFgRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|..
gi 504289601 234 GEPFTfLENHSVLAGNPSIHKT 255
Cdd:pfam00459 240 GGPFD-LLAGRVIAANPKVLHE 260
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
9-252 |
1.86e-53 |
|
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: 173.29 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 9 EIAKKWIREAGARIKQSMHESLTIETKSnPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGdkIHSLEGVVWIIDP 88
Cdd:cd01643 2 SLAEAIAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGG--IFPSSGWYWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 89 IDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATWVTENRR 168
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 169 IDQSVLAPLVKRVRGtrsYGSAALELANVAAGRIDAYI--TMRLapWDYAAGCVLLNEVGGIYTTIEGEPFTFLENHSVL 246
Cdd:cd01643 159 VLRVILRRFPGKIRM---LGSASLNLASVAAGQTLGYVeaTPKI--WDIAAAWVILREAGGSWTILDEEPAFLQTKDYLS 233
|
....*.
gi 504289601 247 AGNPSI 252
Cdd:cd01643 234 AGFPTL 239
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
10-259 |
1.91e-47 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 158.82 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 10 IAKKWIREAGARIKQSMHESLTIET-KSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEgQGDKIHSLEGVVWIIDP 88
Cdd:PRK10757 7 IAVRAARKAGNLIAKNYETPDAVEAsQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEE-SGELEGEDQDVQWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 89 IDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINATW-VTENR 167
Cdd:PRK10757 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFkAKQHA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 168 RIDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEpFTFLENHSVLA 247
Cdd:PRK10757 166 TTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGG-HNYMLTGNIVA 244
|
250
....*....|..
gi 504289601 248 GNPSIHKTIFEE 259
Cdd:PRK10757 245 GNPRVVKAMLAN 256
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
9-263 |
7.57e-44 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 149.45 E-value: 7.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 9 EIAKKWIREAGARIKQSMHESLTIETKsNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqgdkiHSLEGVV----- 83
Cdd:PLN02553 12 EVAVDAAKAAGQIIRKGFYQTKHVEHK-GQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEET-----TAASGGTeltde 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 84 --WIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAinat 161
Cdd:PLN02553 86 ptWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLA---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 162 wvTE--NRRIDQSVLA------PLVKRVRGTRSYGSAALELANVAAGRIDAYITMRL-APWDYAAGCVLLNEVGGIYTTI 232
Cdd:PLN02553 162 --TEvgTKRDKATVDAttnrinALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDP 239
|
250 260 270
....*....|....*....|....*....|.
gi 504289601 233 EGEPFTfLENHSVLAGNPSIhKTIFEEYLHA 263
Cdd:PLN02553 240 SGGPFD-IMSRRVAASNGHL-KDAFVEALRQ 268
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
5-247 |
1.12e-39 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 138.37 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 5 TEIDEIAKKWIREAGARIKQSMHESLTIETKSnPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEG--QGDKIHSLEGV 82
Cdd:COG1218 2 EALLEAAIEIAREAGEAILEIYRADFEVEEKA-DDSPVTEADLAAHAIILAGLAALTPDIPVLSEESaaIPYEERKSWDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 83 VWIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNE-----TKLAPLKETVIEEAILA 157
Cdd:COG1218 81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerQPIRVRDRPPAEPLRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 158 INATwvTENRRIDQsVLAPLvkRVRGTRSYGSaALELANVAAGRIDAYItmRLAP---WDYAAGCVLLNEVGGIYTTIEG 234
Cdd:COG1218 161 ASRS--HRDEETEA-LLARL--GVAELVSVGS-SLKFCLVAEGEADLYP--RLGPtmeWDTAAGQAILEAAGGRVTDLDG 232
|
250
....*....|....*...
gi 504289601 235 EPFTF-----LENHSVLA 247
Cdd:COG1218 233 KPLRYnkkedLLNPGFIA 250
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
16-239 |
1.51e-38 |
|
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: 135.05 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 16 REAGARIKQSMHESLTIETKSnPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSLEGVVWIIDPIDGTMNF 95
Cdd:cd01638 10 REAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDRFWLVDPLDGTREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 96 VHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAP-LKETVIEEAILAINATWVTENRRIDQSVL 174
Cdd:cd01638 89 IKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVsLQARPPPLQPLRVVASRSHPDEELEALLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504289601 175 APLVKRVrgtRSYGSaALELANVAAGRIDAYItmRLAP---WDYAAGCVLLNEVGGIYTTIEGEPFTF 239
Cdd:cd01638 169 ALGVAEV---VSIGS-SLKFCLVAEGEADIYP--RLGPtmeWDTAAGDAVLRAAGGAVSDLDGSPLTY 230
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
40-258 |
1.70e-38 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 138.01 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 40 DLVTNIDKETEKFFIDRIQETFPGHRILGEEGQ--GDkihSLEGVVWIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIG 117
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGviGD---SSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 118 LIYDVV------HDELYHAFSGRGAYMNETKLAPLKETVIEEAILAINA------TWVTenrriDQSVLAPLVKRVRGTR 185
Cdd:PLN02737 188 TVVEFVggpmcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFgyehddAWAT-----NIELFKEFTDVSRGVR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504289601 186 SYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLEnHSVLAGNPSIHKTIFE 258
Cdd:PLN02737 263 RLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFD-RSVLVSNGVLHPKLLD 334
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
16-254 |
1.27e-36 |
|
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: 130.07 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 16 REAGARIKQSMHESLTIETKSNpNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSleGVVWIIDPIDGTMNF 95
Cdd:cd01641 10 DAAGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDA--GYVWVLDPIDGTKSF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 96 VHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLK---ETVIEEAILAI-NATWVTENrriDQ 171
Cdd:cd01641 87 IRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRvraCADLAEAVLSTtDPHFFTPG---DR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 172 SVLAPLVKRVRGTRsYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLENHSVLAGNPS 251
Cdd:cd01641 164 AAFERLARAVRLTR-YGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVVAAGDAE 242
|
...
gi 504289601 252 IHK 254
Cdd:cd01641 243 LHE 245
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-258 |
1.75e-35 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 127.33 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 45 IDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSLEGVVwIIDPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVH 124
Cdd:PRK12676 46 IDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTV-VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLAT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 125 DELYHAFSGRGAYMNETKLAPLKETVIEEAILAINAtwvtenRRIDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDA 204
Cdd:PRK12676 125 GDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSIYG------YRRGKERTVKLGRKVRRVRILGAIALELCYVASGRLDA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504289601 205 YITMR--LAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLENHS-----VLAGNPSIHKTIFE 258
Cdd:PRK12676 199 FVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNELKLPLNVTertnlIAANGEELHKKILE 259
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
7-258 |
9.99e-33 |
|
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: 120.49 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 7 IDEIAKKWIREAGARIKQSMHE--SLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQgdkihSLEGVVW 84
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNlgAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS-----AALGRFW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 85 IIDPIDGTMNFVhQQRNFAISIGIFENGEGKIGLIYDVVHDE-------LYHAFSGRGAYMNE---TKLAPLKETVIEEA 154
Cdd:cd01517 76 VLDPIDGTKGFL-RGDQFAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLRPldgSSLQPLSVRQLTNA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 155 ILAINATWVtENRRIDQSVLAPLVKR--VRGTRSYGSAAlELANVAAGRIDAYI------TMRLAPWDYAAGCVLLNEVG 226
Cdd:cd01517 155 ARASFCESV-ESAHSSHRLQAAIKALggTPQPVRLDSQA-KYAAVARGAADFYLrlplsmSYREKIWDHAAGVLIVEEAG 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 504289601 227 GIYTTIEGEPFTF------LENHSVLAGNPSIHKTIFE 258
Cdd:cd01517 233 GKVTDADGKPLDFgkgrklLNNGGLIAAPGEIHEQVLE 270
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
16-251 |
9.19e-30 |
|
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: 112.16 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 16 REAGARIKQSMHESLTIETKSNpNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQ--GDKIHSLEGVVWIIDPIDGTM 93
Cdd:TIGR01331 10 RAAGEEILPVYQKELAVAQKAD-NSPVTEADRAAHRFILEGLRALTPDIPVLSEEDAsiPLTPRQTWQRFWLVDPLDGTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 94 NFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNetklapLKETVIEEAILAINatWVTENRR--IDQ 171
Cdd:TIGR01331 89 EFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRE------GDGQALKAPIHVRP--WPSGPLLvvISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 172 SVLAPLVKRVRGTRSY-----GSAALELANVAAGRIDAYItmRLAP---WDYAAGCVLLNEVGGIYTTIEGEPFTFLENH 243
Cdd:TIGR01331 161 SHAEEKTTEYLANLGYdlrtsGGSSLKFCLVAEGSADIYP--RLGPtgeWDTAAGHAVLAAAGGAIFDLDGSPLLYGKRE 238
|
....*...
gi 504289601 244 SVLagNPS 251
Cdd:TIGR01331 239 SFR--NPN 244
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
45-258 |
1.55e-28 |
|
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: 109.00 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 45 IDKETEKFFIDRIQETFPGhRILGEE----GQGDKihslEGVVWIIDPIDGTMNFVHQQRNFAISIGIFENGEGK--IGL 118
Cdd:cd01515 41 IDKVAEDAAIEILKKLGSV-NIVSEEigviDNGDE----PEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDpyYGY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 119 IYDVVHDELYHAFSGRGAYMNETKL-----APLKETVIeeaILAINATWVTENRRIDqsvlaplvKRVRGTRSYGSAALE 193
Cdd:cd01515 116 VYNLATGDLYYAIKGKGAYLNGKRIkvsdfSSLKSISV---SYYIYGKNHDRTFKIC--------RKVRRVRIFGSVALE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504289601 194 LANVAAGRIDAYITMR--LAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLENH----SVLAGNPSIHKTIFE 258
Cdd:cd01515 185 LCYVASGALDAFVDVRenLRLVDIAAGYLIAEEAGGIVTDENGKELKLKLNVtervNIIAANSELHKKLLE 255
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
18-258 |
5.91e-27 |
|
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: 104.69 E-value: 5.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 18 AGARIKQSMHESLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEgQGDKIHSLEGVVWIIDPIDGTMNFVH 97
Cdd:TIGR02067 12 AGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE-FGHNEEGDAERVWVLDPIDGTKSFIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 98 QQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILAIN--ATWVT-ENRRIDQSvL 174
Cdd:TIGR02067 91 GVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTspDLLDDpGNRPAFER-L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 175 APLVKRVRGTRSYGSAALelanVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFTFLENhSVLAGNPSIHK 254
Cdd:TIGR02067 170 RRAARLTRYGGDCYAYLM----VAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGG-AVAAGNAMLHD 244
|
....
gi 504289601 255 TIFE 258
Cdd:TIGR02067 245 EALE 248
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
8-231 |
5.54e-26 |
|
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: 100.54 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 8 DEIAKKWIREAGARIKQ--SMHESLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSLE--GVV 83
Cdd:cd01636 1 LEELCRVAKEAGLAILKafGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRrdEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 84 WIIDPIDGTMNFVHQQRNFAISIGIFengegKIGLIYdvvhdELYHafsgrgaymnetklaplketvieeailainatwv 163
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY-----VILILA-----EPSH---------------------------------- 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 164 tenRRIDQSVLAPLVKRVRGTRSYGSAALELANVAAGRIDAYITMRLA--PWDYAAGCVLLNEVGGIYTT 231
Cdd:cd01636 117 ---KRVDEKKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTD 183
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
83-256 |
3.87e-17 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 80.54 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 83 VWIIDPIDGTMNFVHQQRNFAISIGIFE-NGEGK----------------IGLIYDVVHDELYHAFSGRGAYM----NET 141
Cdd:PRK14076 83 IFVLDPIDGTYNALKDIPIYSASIAIAKiDGFDKkikefigknltindleVGVVKNIATGDTYYAEKGEGAYLlkkgEKK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 142 KLAPLKETVIEEAILAINATWVTENrridqsvLAPLVK--RVRGTRSYGSAALELANVAAGRIDAYI----TMRLApwDY 215
Cdd:PRK14076 163 KIEISNISNLKDASIGLFAYGLSLD-------TLKFIKdrKVRRIRLFGSIALEMCYVASGALDAFInvneTTRLC--DI 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504289601 216 AAGCVLLNEVGGIYTTIEGEP----FTFLENHSVLAGNPSIHKTI 256
Cdd:PRK14076 234 AAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKKL 278
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
9-254 |
4.86e-17 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 78.99 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 9 EIAKKWIREAGARIKQSMHESLTIETKSnpnDL--VTNIDKETEKFFIDRIQETFPGHRILGEEGQGDKIHSLEGVVWII 86
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTKFEIIDKE---DLspVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDYVWVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 87 DPIDGTMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRGAYMNETKLAPLKETVIEEAILainatWVTEN 166
Cdd:PLN02911 115 DPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYL-----YTTSP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 167 RRIDQSVLAPLvKRVRG---TRSYGSAALELANVAAGRIDAYITMRLAPWDYAAGCVLLNEVGGIYTTIEGEPFTFlENH 243
Cdd:PLN02911 190 HMFSGDAEDAF-ARVRDkvkVPLYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKLRW-EPS 267
|
250 260
....*....|....*....|
gi 504289601 244 S---------VLAGNPSIHK 254
Cdd:PLN02911 268 PgslatsfnvVAAGDARLHK 287
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
5-239 |
1.33e-10 |
|
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: 60.65 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 5 TEIDeIAKKWIREAGA---RIKQSMHESLTIETKS-NPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEGQGD------ 74
Cdd:TIGR01330 4 RELD-VATQAVRLASLltkKVQSELISHKDSTVITkDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSGlseadf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 75 -------------------------KIHSLE----------------GVVWIIDPIDGTMNFVHQQRnFAISIGIFENGE 113
Cdd:TIGR01330 83 tlgrvnelvnetlvyaknykkddqfPLKSLEdvlqiidfgnyeggrkGRHWVLDPIDGTKGFLRGDQ-YAVCLALIENGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 114 ---GKIG---LIYDVV-------HDE---LYHAFSGRGAYMNETKLAPLKETVIEEailainatwvtenRRIDQSVLAPL 177
Cdd:TIGR01330 162 vvlGVIGcpnLPLSSYgaqnlkgSESkgcIFRAVRGSGAFMYSLSSDAESPTKVHV-------------SSVKDTKDAIF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 178 VKRVRGTRSYGSAALELAN-----------------VAAGRIDAYITMRLAP--------WDYAAGCVLLNEVGGIYTTI 232
Cdd:TIGR01330 229 CEGVEKGHSSHDEQTAIANklgisksplrldsqakyAALARGDADVYLRLPIklsyqekiWDHAAGNVIVEEAGGIVTDA 308
|
....*..
gi 504289601 233 EGEPFTF 239
Cdd:TIGR01330 309 MGKPLDF 315
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
27-239 |
1.73e-10 |
|
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: 60.03 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 27 HESLTIETKSNPNDLVTNIDKETEKFFIDRIQETFPGHRILGEEG--QGDKIHSLEG----------------------- 81
Cdd:cd01640 27 ILLVEGKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDneFENQEDESRDvdldeeileescpspskdlpeed 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 82 -VVWIiDPIDGTMNFVHQQRNFA-ISIGIFENGEGKIGLIYDVVHDELYHA--FSGRGAYMNETKLAPLKETVIEEAILA 157
Cdd:cd01640 107 lGVWV-DPLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQPFYEKTAGAgaWLGRTIWGLSGLGAHSSDFKEREDAGK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 158 INATWvTENRRIDQSVLAPLVKRVRGTRSYGSA--ALELANVAAgriDAYI--TMRLAPWDYAAGCVLLNEVGGIYTTIE 233
Cdd:cd01640 186 IIVST-SHSHSVKEVQLITAGNKDEVLRAGGAGykVLQVLEGLA---DAYVhsTGGIKKWDICAPEAILRALGGDMTDLH 261
|
....*.
gi 504289601 234 GEPFTF 239
Cdd:cd01640 262 GEPLSY 267
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
39-261 |
6.79e-10 |
|
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: 57.84 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 39 NDLVTNIDKETEKFFIDRIQETFPGHRILGEEGqGDKIHSLEGVVWIIDPIDGTMNFVHQQRNFAISIGIFE-NGEGKIG 117
Cdd:cd01642 33 GDVTRVADLKAEEIILKLLREEGVFGQIISEES-GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADpRSKVKAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 118 LIYDVVHDELYHAF---SGRGAYMNETKLAPlkeTVIEEAILAINATwvtENRRIDQSVLAPLVKRVRGTRSYGSAALEL 194
Cdd:cd01642 112 TLDNFVSGEGGLKVyspPTRFSYISVPKLGP---PLVPEVPSKIGIY---EGSSRNPEKFLLLSRNGLKFRSLGSAALEL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504289601 195 ANVAAGRIDAYITMR--LAPWDYAAGCVLLNEVGgiyttIEGEPftflenhSVLAGNPSIHKTIFEEYL 261
Cdd:cd01642 186 AYTCEGSFVLFLDLRgkLRNFDVAAALGACKRLG-----LHGDP-------SNLLLSRIKDKSIDEIIL 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
16-257 |
1.80e-07 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 50.85 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 16 REAGARIKQSMHESLTIETKSNPNDL-VTNIDKETEKFFIDRIQETFPGHRILGEE---GQGDKIHSLEgvVWIIDPIDG 91
Cdd:PRK10931 10 RNAGDAIMQVYDGTKPLDVASKADDSpVTAADIAAHTVIKDGLRTLTPDIPVLSEEdppAWEVRQHWQR--YWLVDPLDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 92 TMNFVHQQRNFAISIGIFENGEGKIGLIYDVVHDELYHAFSGRgAYMNETklAPLKETVIEEAILAInatwVTENRRIDQ 171
Cdd:PRK10931 88 TKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKEEC--GVRKQIQVRDARPPL----VVISRSHAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504289601 172 SVLAPLVKRV--RGTRSYGSaALELANVAAGRidAYITMRLAP---WDYAAGCVLLNEVGGIYTTIEGEPFTFLENHSVL 246
Cdd:PRK10931 161 AELKEYLQQLgeHQTTSIGS-SLKFCLVAEGQ--AQLYPRFGPtniWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFL 237
|
250
....*....|.
gi 504289601 247 agNPSIHKTIF 257
Cdd:PRK10931 238 --NPGFRVSIY 246
|
|
| |
