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Conserved domains on  [gi|1034554666|ref|XP_016855532|]
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3'(2'),5'-bisphosphate nucleotidase 1 isoform X4 [Homo sapiens]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108167)

inositol monophosphatase family protein similar to human inositol polyphosphate 1-phosphatase (INPP1) which hydrolyzes the 1 position phosphate from inositol 1,4-bisphosphate (Ins(1,4)P2) or inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), and to human 3'(2'),5'-bisphosphate nucleotidase 1 (BPNT1) which converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP and has 1000-fold lower activity towards (Ins(1,4)P2) and (Ins(1,3,4)P3)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-261 4.40e-128

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: 365.11  E-value: 4.40e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEE---------- 75
Cdd:cd01640     1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEdnefenqede 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  76 --------------------------LVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVL 129
Cdd:cd01640    81 srdvdldeeileescpspskdlpeedLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 130 GRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCK 208
Cdd:cd01640   161 GRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIK 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034554666 209 KWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 261
Cdd:cd01640   240 KWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-261 4.40e-128

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: 365.11  E-value: 4.40e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEE---------- 75
Cdd:cd01640     1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEdnefenqede 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  76 --------------------------LVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVL 129
Cdd:cd01640    81 srdvdldeeileescpspskdlpeedLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 130 GRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCK 208
Cdd:cd01640   161 GRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIK 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034554666 209 KWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 261
Cdd:cd01640   240 KWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
15-232 2.86e-53

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 174.07  E-value: 2.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  15 AYSIAQKAGMIVRRVIAEgDLGIVEKTC--ATDLQTKADRLAQMSICSSLARKFPKLTIIGEE--------------LVV 78
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGKsgANDLVTAADKAAEELILEALAALFPSHKIIGEEggakgdqteltddgPTW 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  79 WVDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyeagpdavLGRTIWGVLGLGAF--GFQLKEVPAG---- 152
Cdd:pfam00459  88 IIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF----------AGQLYSAAKGKGAFlnGQPLPVSRAPplse 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 153 KHIITTTRSHSNKLVTDC------VAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFaSPGCKKWDTCAPEVILHAVGGKL 226
Cdd:pfam00459 157 ALLVTLFGVSSRKDTSEAsflaklLKLVRAPGVRRVGSAALKLAMVAAGKADAYIE-FGRLKPWDHAAGVAILREAGGVV 235

                  ....*.
gi 1034554666 227 TDIHGN 232
Cdd:pfam00459 236 TDADGG 241
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-244 4.88e-36

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 129.12  E-value: 4.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  10 RLVASAYSIAQKAGMIVRRvIAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEELV------------ 77
Cdd:COG1218     3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEESAaipyeerkswdr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  78 VW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF----GFQLKEVPAG 152
Cdd:COG1218    81 FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP----------ALGRLYYAAKGQGAFketgGGERQPIRVR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 153 KH------IITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKL 226
Cdd:COG1218   150 DRppaeplRVVASRSHRDEETEALLARLGVAELVSV-GSSLKFCLVAEGEADLYPRLGPTM-EWDTAAGQAILEAAGGRV 227
                         250
                  ....*....|....*...
gi 1034554666 227 TDIHGNVLQYHKDVKHMN 244
Cdd:COG1218   228 TDLDGKPLRYNKKEDLLN 245
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-238 5.43e-23

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: 94.44  E-value: 5.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEELV--------VW-----VDPLD 84
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDAsipltprqTWqrfwlVDPLD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  85 GTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF----------GFQLKEVPAGKH 154
Cdd:TIGR01331  86 GTKEFINR-NGDFTVNIALVEHGVPVLGVVYAP----------ATGVTYFATAGKAAKregdgqalkaPIHVRPWPSGPL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 155 IITTTRSHSNKLVTDCVAAMNPDAVLrVGGAGNKIIQLIEGKASAYVFASPgCKKWDTCAPEVILHAVGGKLTDIHGNVL 234
Cdd:TIGR01331 155 LVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIYPRLGP-TGEWDTAAGHAVLAAAGGAIFDLDGSPL 232

                  ....
gi 1034554666 235 QYHK 238
Cdd:TIGR01331 233 LYGK 236
PLN02911 PLN02911
inositol-phosphate phosphatase
1-117 2.73e-12

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 65.51  E-value: 2.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666   1 MASSNTVLMRLVASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIG 73
Cdd:PLN02911   26 SALSDAVLDRFVDVAHKLADAAGEVTRKyfrtkfeIIDKEDLSPV---------TIADRAAEEAMRSIILENFPSHAIFG 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034554666  74 EE--LV--------VWV-DPLDGTKEYTEG--LLDnvtVLIGIAYEGKAIAGVINQP 117
Cdd:PLN02911   97 EEhgLRcgegssdyVWVlDPIDGTKSFITGkpLFG---TLIALLYKGKPVLGIIDQP 150
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-261 4.40e-128

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: 365.11  E-value: 4.40e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEE---------- 75
Cdd:cd01640     1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEdnefenqede 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  76 --------------------------LVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVL 129
Cdd:cd01640    81 srdvdldeeileescpspskdlpeedLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 130 GRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCK 208
Cdd:cd01640   161 GRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIK 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034554666 209 KWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 261
Cdd:cd01640   240 KWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
15-232 2.86e-53

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 174.07  E-value: 2.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  15 AYSIAQKAGMIVRRVIAEgDLGIVEKTC--ATDLQTKADRLAQMSICSSLARKFPKLTIIGEE--------------LVV 78
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGKsgANDLVTAADKAAEELILEALAALFPSHKIIGEEggakgdqteltddgPTW 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  79 WVDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyeagpdavLGRTIWGVLGLGAF--GFQLKEVPAG---- 152
Cdd:pfam00459  88 IIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF----------AGQLYSAAKGKGAFlnGQPLPVSRAPplse 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 153 KHIITTTRSHSNKLVTDC------VAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFaSPGCKKWDTCAPEVILHAVGGKL 226
Cdd:pfam00459 157 ALLVTLFGVSSRKDTSEAsflaklLKLVRAPGVRRVGSAALKLAMVAAGKADAYIE-FGRLKPWDHAAGVAILREAGGVV 235

                  ....*.
gi 1034554666 227 TDIHGN 232
Cdd:pfam00459 236 TDADGG 241
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-244 4.88e-36

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 129.12  E-value: 4.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  10 RLVASAYSIAQKAGMIVRRvIAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEELV------------ 77
Cdd:COG1218     3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEESAaipyeerkswdr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  78 VW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF----GFQLKEVPAG 152
Cdd:COG1218    81 FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP----------ALGRLYYAAKGQGAFketgGGERQPIRVR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 153 KH------IITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKL 226
Cdd:COG1218   150 DRppaeplRVVASRSHRDEETEALLARLGVAELVSV-GSSLKFCLVAEGEADLYPRLGPTM-EWDTAAGQAILEAAGGRV 227
                         250
                  ....*....|....*...
gi 1034554666 227 TDIHGNVLQYHKDVKHMN 244
Cdd:COG1218   228 TDLDGKPLRYNKKEDLLN 245
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
11-239 1.10e-33

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: 122.33  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  11 LVASAYSIAQKAGMIVRRViAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEELV----------VW- 79
Cdd:cd01638     1 LLELLIRIAREAGDAILEV-YRGGFTVERKEDGSPV-TAADLAANAFIVEGLAALRPDIPVLSEESAddplrlgwdrFWl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  80 VDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF--------GFQLKEVPA 151
Cdd:cd01638    79 VDPLDGTREFIKGN-GEFAVNIALVEDGRPVLGVVYAP----------ALGELYYALRGGGAYkngrpgavSLQARPPPL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 152 GKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGaGNKIIQLIEGKASAYVFASPGCKkWDTCAPEVILHAVGGKLTDIHG 231
Cdd:cd01638   148 QPLRVVASRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTME-WDTAAGDAVLRAAGGAVSDLDG 225

                  ....*...
gi 1034554666 232 NVLQYHKD 239
Cdd:cd01638   226 SPLTYNRE 233
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
18-251 6.48e-31

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: 115.10  E-value: 6.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEE-----------LVVWVDPLDGT 86
Cdd:cd01637     7 AVREAGALILEAFGEE-LTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEgggsgnvsdggRVWVIDPIDGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  87 KEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAFGF-----QLKEVPAGKHIITTTRS 161
Cdd:cd01637    86 TNFVAG-LPNFAVSIALYEDGKPVLGVIYDP----------MLDELYYAGRGKGAFLNgkklpLSKDTPLNDALLSTNAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 162 HSNKLVTDCVAAMNPDA--VLRVGGAGNKIIQLIEGKASAYVfaSPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHkd 239
Cdd:cd01637   155 MLRSNRAAVLASLVNRAlgIRIYGSAGLDLAYVAAGRLDAYL--SSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTL-- 230
                         250
                  ....*....|..
gi 1034554666 240 vkhmNSAGVLAT 251
Cdd:cd01637   231 ----NRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
9-251 6.23e-29

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: 110.32  E-value: 6.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666   9 MRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTcATDLQTKADRLAQMSICSSLARKFPKLTIIGEEL---------VVW 79
Cdd:COG0483     1 HPLLELALRAARAAGALILRRFRELDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESgasegrdsgYVW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  80 V-DPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF--GFQLK---EVPAGK 153
Cdd:COG0483    80 ViDPIDGTTNFVHG-LPLFAVSIALVRDGEPVAGVVYDP----------ALGELFTAARGGGAFlnGRRLRvsaRTDLED 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 154 HIITTTRSH--SNKLVTDCVAAMNPDA--VLRVGGAGNKIIQLIEGKASAYVfaSPGCKKWDTCAPEVILHAVGGKLTDI 229
Cdd:COG0483   149 ALVATGFPYlrDDREYLAALAALLPRVrrVRRLGSAALDLAYVAAGRLDAFV--EAGLKPWDIAAGALIVREAGGVVTDL 226
                         250       260
                  ....*....|....*....|..
gi 1034554666 230 HGNVLqyhkdvkHMNSAGVLAT 251
Cdd:COG0483   227 DGEPL-------DLGSGSLVAA 241
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-238 5.43e-23

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: 94.44  E-value: 5.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEELV--------VW-----VDPLD 84
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDAsipltprqTWqrfwlVDPLD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  85 GTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF----------GFQLKEVPAGKH 154
Cdd:TIGR01331  86 GTKEFINR-NGDFTVNIALVEHGVPVLGVVYAP----------ATGVTYFATAGKAAKregdgqalkaPIHVRPWPSGPL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 155 IITTTRSHSNKLVTDCVAAMNPDAVLrVGGAGNKIIQLIEGKASAYVFASPgCKKWDTCAPEVILHAVGGKLTDIHGNVL 234
Cdd:TIGR01331 155 LVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIYPRLGP-TGEWDTAAGHAVLAAAGGAIFDLDGSPL 232

                  ....
gi 1034554666 235 QYHK 238
Cdd:TIGR01331 233 LYGK 236
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
15-232 2.03e-22

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: 92.60  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  15 AYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEL---------VVW-VDPLD 84
Cdd:cd01639     5 AIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESgaaggltdePTWiIDPLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  85 GTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF--GFQLK--------------E 148
Cdd:cd01639    85 GTTNFVHG-FPHFAVSIALAVKGEPVVGVVYDP----------IRNELFTAVRGQGAFlnGRRIRvsgrkelkdalvatG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 149 VPAGKH-IITTTRSHSNKLVTDCVAamnpdAVLRVGGAGNKIIQLIEGKASAYVFAspGCKKWDTCAPEVILHAVGGKLT 227
Cdd:cd01639   154 FPYDRGdNFDRYLNNFAKLLAKAVR-----GVRRLGSAALDLAYVAAGRLDGYWER--GLKPWDVAAGALIVREAGGLVT 226

                  ....*
gi 1034554666 228 DIHGN 232
Cdd:cd01639   227 DFDGG 231
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
9-251 3.90e-22

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: 92.76  E-value: 3.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666   9 MRLVASAysIAQKAGMIVRRVIAE-GDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEELV-----VWV-D 81
Cdd:cd01517     1 ELEVAIL--AVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSaalgrFWVlD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  82 PLDGTKEYTEGLLdnVTVLIGIAYEGKAIAGVINQPYYNYEAGPdavLGRTIWGVLGLGAFGFQLKEVPAGKHIITTTRS 161
Cdd:cd01517    79 PIDGTKGFLRGDQ--FAVALALIEDGEVVLGVIGCPNLPLDDGG---GGDLFSAVRGQGAWLRPLDGSSLQPLSVRQLTN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 162 HSNKLVTDCVAAMNPDAVLRVGGAGN-------------KIIQLIEGKASAYV-FASPGCKK---WDTCAPEVILHAVGG 224
Cdd:cd01517   154 AARASFCESVESAHSSHRLQAAIKALggtpqpvrldsqaKYAAVARGAADFYLrLPLSMSYRekiWDHAAGVLIVEEAGG 233
                         250       260
                  ....*....|....*....|....*..
gi 1034554666 225 KLTDIHGNVLQYHKDVKHMNSAGVLAT 251
Cdd:cd01517   234 KVTDADGKPLDFGKGRKLLNNGGLIAA 260
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
18-228 5.30e-17

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: 76.66  E-value: 5.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  18 IAQKAGMIVRRVIAEGDLGIVEKTCAT-DLQTKADRLAQMSICSSLARKFPKLTIIGEE-------------LVVWVDPL 83
Cdd:cd01636     7 VAKEAGLAILKAFGRELSGKVKITKSDnDPVTTADVAAETLIRNMLKSSFPDVKIVGEEsgvaeevmgrrdeYTWVIDPI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  84 DGTKEYTEGlLDNVTVLIGIayegkaiaGVINQPYYNYEAGPDavlgrtiwgvlglgafgfqlkevpagkhiitttrshS 163
Cdd:cd01636    87 DGTKNFING-LPFVAVVIAV--------YVILILAEPSHKRVD------------------------------------E 121
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034554666 164 NKLVTDCVAamnPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTD 228
Cdd:cd01636   122 KKAELQLLA---VYRIRIVGSAVAKMCLVALGLADIYYEPGGKRRAWDVAASAAIVREAGGIMTD 183
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
12-235 1.03e-16

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: 77.29  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  12 VASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIGEEL-------- 76
Cdd:cd01641     2 LAFALELADAAGQITLPyfrtrlqVETKADFSPV---------TEADRAAEAAMRELIAAAFPDHGILGEEFgneggdag 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  77 VVWV-DPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyeagpdavLGRTIWGVLGLGAFgfqlKEVPAGKHI 155
Cdd:cd01641    73 YVWVlDPIDGTKSFIRGL-PVWGTLIALLHDGRPVLGVIDQPA----------LGERWIGARGGGTF----LNGAGGRPL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 156 ITttrSHSNKLVTDCVAAMNPDAVLRVGGAG----NKIIQLIEGKASAYVFAS-----------PGCKKWDTCAPEVILH 220
Cdd:cd01641   138 RV---RACADLAEAVLSTTDPHFFTPGDRAAferlARAVRLTRYGGDCYAYALvasgrvdlvveAGLKPYDVAALIPIIE 214
                         250
                  ....*....|....*
gi 1034554666 221 AVGGKLTDIHGNVLQ 235
Cdd:cd01641   215 GAGGVITDWDGGPLT 229
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
13-224 1.44e-12

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: 65.43  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  13 ASAYSIAQKAGmivRRVIAE-GDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEL--------VVWV-DP 82
Cdd:cd01643     2 SLAEAIAQEAG---DRALADfGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGggifpssgWYWViDP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  83 LDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF--GFQLK-EVPAGKHIITTT 159
Cdd:cd01643    79 IDGTTNFARG-IPIWAISIALLYRGEPVFGVIALP----------ALNQTFVAFKGGGAFlnGKPLAlHPPLQLPDCNVG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034554666 160 RSHSNKLVtdcvaamnPDAVLRVG--GAGNKIIQLieGKAS---AYVFA-------SPGCKKWDTCAPEVILHAVGG 224
Cdd:cd01643   148 FNRSSRAS--------ARAVLRVIlrRFPGKIRML--GSASlnlASVAAgqtlgyvEATPKIWDIAAAWVILREAGG 214
PLN02911 PLN02911
inositol-phosphate phosphatase
1-117 2.73e-12

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 65.51  E-value: 2.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666   1 MASSNTVLMRLVASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIG 73
Cdd:PLN02911   26 SALSDAVLDRFVDVAHKLADAAGEVTRKyfrtkfeIIDKEDLSPV---------TIADRAAEEAMRSIILENFPSHAIFG 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034554666  74 EE--LV--------VWV-DPLDGTKEYTEG--LLDnvtVLIGIAYEGKAIAGVINQP 117
Cdd:PLN02911   97 EEhgLRcgegssdyVWVlDPIDGTKSFITGkpLFG---TLIALLYKGKPVLGIIDQP 150
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
48-236 1.43e-09

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 57.01  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  48 TKADRLAQMSICSSLARKFPKLTIIGEE-LVVW-----------VDPLDGTKEYtegLLDN--VTVLIGIAYEGKAIAGV 113
Cdd:PRK10931   38 TAADIAAHTVIKDGLRTLTPDIPVLSEEdPPAWevrqhwqrywlVDPLDGTKEF---IKRNgeFTVNIALIEQGKPVLGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 114 INQPYYN--YEAGpdavlGRTIW----GVLglgafgFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGN 187
Cdd:PRK10931  115 VYAPVMNvmYSAA-----EGKAWkeecGVR------KQIQVRDARPPLVVISRSHADAELKEYLQQLGEHQTTSI-GSSL 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034554666 188 KIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQY 236
Cdd:PRK10931  183 KFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQGKTLDY 230
PRK10757 PRK10757
inositol-1-monophosphatase;
19-250 1.15e-08

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 54.43  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  19 AQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEL---------VVWV-DPLDGTKE 88
Cdd:PRK10757   12 ARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESgelegedqdVQWViDPLDGTTN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  89 YTEgLLDNVTVLIGIAYEGKAIAGVINQPYYN--YEA--GPDAVL---------GRTIWGVLGLGAFGFQLKEvpagkHI 155
Cdd:PRK10757   92 FIK-RLPHFAVSIAVRIKGRTEVAVVYDPMRNelFTAtrGQGAQLngyrlrgstARDLDGTILATGFPFKAKQ-----HA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 156 ITTTRSHSnKLVTDCVaamnpdAVLRVGGAGNKIIQLIEGKASAYVfaSPGCKKWDTCAPEVILHAVGGKLTDIHGNvlq 235
Cdd:PRK10757  166 TTYINIVG-KLFTECA------DFRRTGSAALDLAYVAAGRVDGFF--EIGLKPWDFAAGELLVREAGGIVSDFTGG--- 233
                         250
                  ....*....|....*
gi 1034554666 236 yHkdvKHMNSAGVLA 250
Cdd:PRK10757  234 -H---NYMLTGNIVA 244
PLN02737 PLN02737
inositol monophosphatase family protein
43-231 6.94e-08

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 52.88  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666  43 ATDLQTKADRLAQMSICSSLARKFPKLTIIGEELVV---------W-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAG 112
Cdd:PLN02737  109 LTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVigdsssdylWcIDPLDGTTNFAHG-YPSFAVSVGVLFRGTPAAA 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666 113 VINQpyynYEAGPDAVLGRTIWGVLGLGAF--GFQLkevpagkHIITTTRSHSNKLVT------DCVAAMNPD------- 177
Cdd:PLN02737  188 TVVE----FVGGPMCWNTRTFSASAGGGAFcnGQKI-------HVSQTDKVERSLLVTgfgyehDDAWATNIElfkeftd 256
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034554666 178 ---AVLRVGGAGNKIIQLIEGKASAYvfASPGCKKWDTCAPEVILHAVGGKLTDIHG 231
Cdd:PLN02737  257 vsrGVRRLGAAAVDMCHVALGIVEAY--WEYRLKPWDMAAGVLIVEEAGGTVTRMDG 311
PLN02553 PLN02553
inositol-phosphate phosphatase
8-142 1.97e-06

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 47.76  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034554666   8 LMRLVASAYSIAQKAGMIVRRVIAEGDlgIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEELV---------- 77
Cdd:PLN02553    7 LEQFLEVAVDAAKAAGQIIRKGFYQTK--HVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTaasggteltd 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034554666  78 --VW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGAF 142
Cdd:PLN02553   85 epTWiVDPLDGTTNFVHG-FPFVCVSIGLTIGKVPVVGVVYNP----------ILDELFTAVKGKGAF 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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