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Conserved domains on  [gi|530365931|ref|XP_005273057|]
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3'(2'),5'-bisphosphate nucleotidase 1 isoform X2 [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 ...
11-297 8.65e-147

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: 414.03  E-value: 8.65e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  86 LIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVL 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 166 GRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCK 244
Cdd:cd01640  161 GRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530365931 245 KWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 297
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 ...
11-297 8.65e-147

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: 414.03  E-value: 8.65e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  86 LIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVL 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 166 GRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCK 244
Cdd:cd01640  161 GRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530365931 245 KWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 297
Cdd:cd01640  240 KWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
15-268 1.01e-53

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 176.38  E-value: 1.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   15 AYSIAQKAGMIVRRVIAEgDLGIVEKTC--ATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeliedsqw 92
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGKsgANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQ---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   93 eeilkqpcpsqySAIKEEDLVVWVDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyeagpdavLGRTIWGV 172
Cdd:pfam00459  78 ------------TELTDDGPTWIIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF----------AGQLYSAA 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  173 LGLGAF--GFQLKEVPAG----KHIITTTRSHSNKLVTDC------VAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFaS 240
Cdd:pfam00459 135 KGKGAFlnGQPLPVSRAPplseALLVTLFGVSSRKDTSEAsflaklLKLVRAPGVRRVGSAALKLAMVAAGKADAYIE-F 213
                         250       260
                  ....*....|....*....|....*...
gi 530365931  241 PGCKKWDTCAPEVILHAVGGKLTDIHGN 268
Cdd:pfam00459 214 GRLKPWDHAAGVAILREAGGVVTDADGG 241
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-280 9.93e-37

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 131.82  E-value: 9.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  10 RLVASAYSIAQKAGMIVRRvIAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDlpseeVDQELIED 89
Cdd:COG1218    3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEES-----AAIPYEER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  90 SQWEEilkqpcpsqysaikeedlvVW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRT 168
Cdd:COG1218   76 KSWDR-------------------FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP----------ALGRL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 169 IWGVLGLGAF----GFQLKEVPAGKH------IITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVF 238
Cdd:COG1218  126 YYAAKGQGAFketgGGERQPIRVRDRppaeplRVVASRSHRDEETEALLARLGVAELVSV-GSSLKFCLVAEGEADLYPR 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 530365931 239 ASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMN 280
Cdd:COG1218  205 LGPTM-EWDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLN 245
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-274 3.64e-22

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: 92.90  E-value: 3.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDLPseevdQELIEDSQWEEIlk 97
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDAS-----IPLTPRQTWQRF-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   98 qpcpsqysaikeedlvvW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLG 176
Cdd:TIGR01331  79 -----------------WlVDPLDGTKEFINR-NGDFTVNIALVEHGVPVLGVVYAP----------ATGVTYFATAGKA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  177 AF----------GFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLrVGGAGNKIIQLIEGKASAYVFASPgCKKW 246
Cdd:TIGR01331 131 AKregdgqalkaPIHVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIYPRLGP-TGEW 208
                         250       260
                  ....*....|....*....|....*...
gi 530365931  247 DTCAPEVILHAVGGKLTDIHGNVLQYHK 274
Cdd:TIGR01331 209 DTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
48-272 6.34e-11

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 61.25  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  48 TKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQeliedsQWEeilkqpcpsQYsaikeedlvvW-VDPLDGTKEYt 126
Cdd:PRK10931  38 TAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ------HWQ---------RY----------WlVDPLDGTKEF- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 127 egLLDN--VTVLIGIAYEGKAIAGVINQPYYN--YEAGpdavlGRTIW----GVLglgafgFQLKEVPAGKHIITTTRSH 198
Cdd:PRK10931  92 --IKRNgeFTVNIALIEQGKPVLGVVYAPVMNvmYSAA-----EGKAWkeecGVR------KQIQVRDARPPLVVISRSH 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530365931 199 SNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQY 272
Cdd:PRK10931 159 ADAELKEYLQQLGEHQTTSI-GSSLKFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQGKTLDY 230
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-297 8.65e-147

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: 414.03  E-value: 8.65e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  86 LIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVL 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 166 GRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCK 244
Cdd:cd01640  161 GRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530365931 245 KWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 297
Cdd:cd01640  240 KWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
15-268 1.01e-53

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 176.38  E-value: 1.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   15 AYSIAQKAGMIVRRVIAEgDLGIVEKTC--ATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeliedsqw 92
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGKsgANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQ---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   93 eeilkqpcpsqySAIKEEDLVVWVDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyeagpdavLGRTIWGV 172
Cdd:pfam00459  78 ------------TELTDDGPTWIIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF----------AGQLYSAA 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  173 LGLGAF--GFQLKEVPAG----KHIITTTRSHSNKLVTDC------VAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFaS 240
Cdd:pfam00459 135 KGKGAFlnGQPLPVSRAPplseALLVTLFGVSSRKDTSEAsflaklLKLVRAPGVRRVGSAALKLAMVAAGKADAYIE-F 213
                         250       260
                  ....*....|....*....|....*...
gi 530365931  241 PGCKKWDTCAPEVILHAVGGKLTDIHGN 268
Cdd:pfam00459 214 GRLKPWDHAAGVAILREAGGVVTDADGG 241
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-280 9.93e-37

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 131.82  E-value: 9.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  10 RLVASAYSIAQKAGMIVRRvIAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDlpseeVDQELIED 89
Cdd:COG1218    3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEES-----AAIPYEER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  90 SQWEEilkqpcpsqysaikeedlvVW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRT 168
Cdd:COG1218   76 KSWDR-------------------FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP----------ALGRL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 169 IWGVLGLGAF----GFQLKEVPAGKH------IITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVF 238
Cdd:COG1218  126 YYAAKGQGAFketgGGERQPIRVRDRppaeplRVVASRSHRDEETEALLARLGVAELVSV-GSSLKFCLVAEGEADLYPR 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 530365931 239 ASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMN 280
Cdd:COG1218  205 LGPTM-EWDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLN 245
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
11-275 2.89e-31

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: 116.94  E-value: 2.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  11 LVASAYSIAQKAGMIVRRViAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeliedS 90
Cdd:cd01638    1 LLELLIRIAREAGDAILEV-YRGGFTVERKEDGSPV-TAADLAANAFIVEGLAALRPDIPVLSEESADDPLR-------L 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  91 QWEEilkqpcpsqysaikeedlvVW-VDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTI 169
Cdd:cd01638   72 GWDR-------------------FWlVDPLDGTREFIKGN-GEFAVNIALVEDGRPVLGVVYAP----------ALGELY 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 170 WGVLGLGAF--------GFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGaGNKIIQLIEGKASAYVFASP 241
Cdd:cd01638  122 YALRGGGAYkngrpgavSLQARPPPLQPLRVVASRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGP 200
                        250       260       270
                 ....*....|....*....|....*....|....
gi 530365931 242 GCKkWDTCAPEVILHAVGGKLTDIHGNVLQYHKD 275
Cdd:cd01638  201 TME-WDTAAGDAVLRAAGGAVSDLDGSPLTYNRE 233
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
18-287 3.26e-30

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: 114.33  E-value: 3.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpsEEVDQELIEDSQWeeilk 97
Cdd:cd01637    7 AVREAGALILEAFGEE-LTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG---GGSGNVSDGGRVW----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  98 qpcpsqysaikeedlvvWVDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLGA 177
Cdd:cd01637   78 -----------------VIDPIDGTTNFVAG-LPNFAVSIALYEDGKPVLGVIYDP----------MLDELYYAGRGKGA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 178 FGF-----QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDA--VLRVGGAGNKIIQLIEGKASAYVfaSPGCKKWDTCA 250
Cdd:cd01637  130 FLNgkklpLSKDTPLNDALLSTNASMLRSNRAAVLASLVNRAlgIRIYGSAGLDLAYVAAGRLDAYL--SSGLNPWDYAA 207
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 530365931 251 PEVILHAVGGKLTDIHGNVLQYHkdvkhmNSAGVLAT 287
Cdd:cd01637  208 GALIVEEAGGIVTDLDGEPLDTL------NRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
9-287 5.90e-27

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: 106.08  E-value: 5.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   9 MRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTcATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQELie 88
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRELDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGY-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  89 dsqweeilkqpcpsqysaikeedlvVWV-DPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGR 167
Cdd:COG0483   78 -------------------------VWViDPIDGTTNFVHG-LPLFAVSIALVRDGEPVAGVVYDP----------ALGE 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 168 TIWGVLGLGAF--GFQLK---EVPAGKHIITTTRSH--SNKLVTDCVAAMNPDA--VLRVGGAGNKIIQLIEGKASAYVf 238
Cdd:COG0483  122 LFTAARGGGAFlnGRRLRvsaRTDLEDALVATGFPYlrDDREYLAALAALLPRVrrVRRLGSAALDLAYVAAGRLDAFV- 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530365931 239 aSPGCKKWDTCAPEVILHAVGGKLTDIHGNVLqyhkdvkHMNSAGVLAT 287
Cdd:COG0483  201 -EAGLKPWDIAAGALIVREAGGVVTDLDGEPL-------DLGSGSLVAA 241
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-274 3.64e-22

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: 92.90  E-value: 3.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDLPseevdQELIEDSQWEEIlk 97
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDAS-----IPLTPRQTWQRF-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   98 qpcpsqysaikeedlvvW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVLGLG 176
Cdd:TIGR01331  79 -----------------WlVDPLDGTKEFINR-NGDFTVNIALVEHGVPVLGVVYAP----------ATGVTYFATAGKA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  177 AF----------GFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLrVGGAGNKIIQLIEGKASAYVFASPgCKKW 246
Cdd:TIGR01331 131 AKregdgqalkaPIHVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIYPRLGP-TGEW 208
                         250       260
                  ....*....|....*....|....*...
gi 530365931  247 DTCAPEVILHAVGGKLTDIHGNVLQYHK 274
Cdd:TIGR01331 209 DTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
15-268 5.57e-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: 92.21  E-value: 5.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  15 AYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpseevdqeliedsqwee 94
Cdd:cd01639    5 AIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES------------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  95 ilkqpcpsqYSAIKEEDLVVW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIWGVL 173
Cdd:cd01639   67 ---------GAAGGLTDEPTWiIDPLDGTTNFVHG-FPHFAVSIALAVKGEPVVGVVYDP----------IRNELFTAVR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 174 GLGAF--GFQLK--------------EVPAGKH-IITTTRSHSNKLVTDCVAamnpdAVLRVGGAGNKIIQLIEGKASAY 236
Cdd:cd01639  127 GQGAFlnGRRIRvsgrkelkdalvatGFPYDRGdNFDRYLNNFAKLLAKAVR-----GVRRLGSAALDLAYVAAGRLDGY 201
                        250       260       270
                 ....*....|....*....|....*....|..
gi 530365931 237 VFAspGCKKWDTCAPEVILHAVGGKLTDIHGN 268
Cdd:cd01639  202 WER--GLKPWDVAAGALIVREAGGLVTDFDGG 231
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
9-287 9.16e-20

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: 86.98  E-value: 9.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   9 MRLVASAysIAQKAGMIVRRVIAE-GDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLpseevdqeli 87
Cdd:cd01517    1 ELEVAIL--AVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  88 edsqweeilkqpcpsqysaiKEEDLVVWVDPLDGTKEYTEGLLdnVTVLIGIAYEGKAIAGVINQPYYNYEAGPdavLGR 167
Cdd:cd01517   69 --------------------AALGRFWVLDPIDGTKGFLRGDQ--FAVALALIEDGEVVLGVIGCPNLPLDDGG---GGD 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 168 TIWGVLGLGAFGFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGN-------------KIIQLIEGKAS 234
Cdd:cd01517  124 LFSAVRGQGAWLRPLDGSSLQPLSVRQLTNAARASFCESVESAHSSHRLQAAIKALggtpqpvrldsqaKYAAVARGAAD 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530365931 235 AYV-FASPGCKK---WDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLAT 287
Cdd:cd01517  204 FYLrLPLSMSYRekiWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIAA 260
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
18-264 1.36e-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: 78.97  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  18 IAQKAGMIVRRVIAEGDLGIVEKTCAT-DLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeLIEDSQWeeil 96
Cdd:cd01636    7 VAKEAGLAILKAFGRELSGKVKITKSDnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEV---MGRRDEY---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  97 kqpcpsqysaikeedlVVWVDPLDGTKEYTEGlLDNVTVLIGIayegkaiaGVINQPYYNYEAGPDavlgrtiwgvlglg 176
Cdd:cd01636   80 ----------------TWVIDPIDGTKNFING-LPFVAVVIAV--------YVILILAEPSHKRVD-------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 177 afgfqlkevpagkhiitttrshSNKLVTDCVAamnPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILH 256
Cdd:cd01636  121 ----------------------EKKAELQLLA---VYRIRIVGSAVAKMCLVALGLADIYYEPGGKRRAWDVAASAAIVR 175

                 ....*...
gi 530365931 257 AVGGKLTD 264
Cdd:cd01636  176 EAGGIMTD 183
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
12-271 6.41e-14

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: 69.98  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  12 VASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIGEEdlpseevdq 84
Cdd:cd01641    2 LAFALELADAAGQITLPyfrtrlqVETKADFSPV---------TEADRAAEAAMRELIAAAFPDHGILGEE--------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  85 eliedsqweeilkqpcpsqYSAIKEEDLVVWV-DPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyeagpda 163
Cdd:cd01641   64 -------------------FGNEGGDAGYVWVlDPIDGTKSFIRGL-PVWGTLIALLHDGRPVLGVIDQPA--------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 164 vLGRTIWGVLGLGAFgfqlKEVPAGKHIITttrSHSNKLVTDCVAAMNPDAVLRVGGAG----NKIIQLIEGKASAYVFA 239
Cdd:cd01641  115 -LGERWIGARGGGTF----LNGAGGRPLRV---RACADLAEAVLSTTDPHFFTPGDRAAferlARAVRLTRYGGDCYAYA 186
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 530365931 240 S-----------PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQ 271
Cdd:cd01641  187 LvasgrvdlvveAGLKPYDVAALIPIIEGAGGVITDWDGGPLT 229
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
13-260 4.90e-11

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: 61.58  E-value: 4.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  13 ASAYSIAQKAGmivRRVIAE-GDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpseevdQELIEDSQ 91
Cdd:cd01643    2 SLAEAIAQEAG---DRALADfGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG-------GGIFPSSG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  92 WeeilkqpcpsqysaikeedlvVWV-DPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLGRTIW 170
Cdd:cd01643   72 W---------------------YWViDPIDGTTNFARG-IPIWAISIALLYRGEPVFGVIALP----------ALNQTFV 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 171 GVLGLGAF--GFQLK-EVPAGKHIITTTRSHSNKLVtdcvaamnPDAVLRVG--GAGNKIIQLieGKAS---AYVFA--- 239
Cdd:cd01643  120 AFKGGGAFlnGKPLAlHPPLQLPDCNVGFNRSSRAS--------ARAVLRVIlrRFPGKIRML--GSASlnlASVAAgqt 189
                        250       260
                 ....*....|....*....|....*
gi 530365931 240 ----SPGCKKWDTCAPEVILHAVGG 260
Cdd:cd01643  190 lgyvEATPKIWDIAAAWVILREAGG 214
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
48-272 6.34e-11

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 61.25  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  48 TKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQeliedsQWEeilkqpcpsQYsaikeedlvvW-VDPLDGTKEYt 126
Cdd:PRK10931  38 TAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ------HWQ---------RY----------WlVDPLDGTKEF- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 127 egLLDN--VTVLIGIAYEGKAIAGVINQPYYN--YEAGpdavlGRTIW----GVLglgafgFQLKEVPAGKHIITTTRSH 198
Cdd:PRK10931  92 --IKRNgeFTVNIALIEQGKPVLGVVYAPVMNvmYSAA-----EGKAWkeecGVR------KQIQVRDARPPLVVISRSH 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530365931 199 SNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQY 272
Cdd:PRK10931 159 ADAELKEYLQQLGEHQTTSI-GSSLKFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQGKTLDY 230
PLN02911 PLN02911
inositol-phosphate phosphatase
1-153 4.95e-10

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 59.35  E-value: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   1 MASSNTVLMRLVASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIG 73
Cdd:PLN02911  26 SALSDAVLDRFVDVAHKLADAAGEVTRKyfrtkfeIIDKEDLSPV---------TIADRAAEEAMRSIILENFPSHAIFG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  74 EEDlpseevdqeliedsQWEeilkqpCPSQYSAIkeedlvVWV-DPLDGTKEYTEG--LLDnvtVLIGIAYEGKAIAGVI 150
Cdd:PLN02911  97 EEH--------------GLR------CGEGSSDY------VWVlDPIDGTKSFITGkpLFG---TLIALLYKGKPVLGII 147

                 ...
gi 530365931 151 NQP 153
Cdd:PLN02911 148 DQP 150
PRK10757 PRK10757
inositol-1-monophosphatase;
19-286 6.53e-07

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 49.81  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  19 AQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEE--DLPSEEvdqeliEDSQWEeil 96
Cdd:PRK10757  12 ARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEEsgELEGED------QDVQWV--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  97 kqpcpsqysaikeedlvvwVDPLDGTKEYTEgLLDNVTVLIGIAYEGKAIAGVINQPYYN--YEA--GPDAVL------- 165
Cdd:PRK10757  83 -------------------IDPLDGTTNFIK-RLPHFAVSIAVRIKGRTEVAVVYDPMRNelFTAtrGQGAQLngyrlrg 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 166 --GRTIWGVLGLGAFGFQLKEvpagkHIITTTRSHSnKLVTDCVaamnpdAVLRVGGAGNKIIQLIEGKASAYVfaSPGC 243
Cdd:PRK10757 143 stARDLDGTILATGFPFKAKQ-----HATTYINIVG-KLFTECA------DFRRTGSAALDLAYVAAGRVDGFF--EIGL 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 530365931 244 KKWDTCAPEVILHAVGGKLTDIHGNvlqyHkdvKHMNSAGVLA 286
Cdd:PRK10757 209 KPWDFAAGELLVREAGGIVSDFTGG----H---NYMLTGNIVA 244
PLN02737 PLN02737
inositol monophosphatase family protein
43-267 1.08e-06

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 49.41  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  43 ATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpseevdqELIEDSQweeilkqpcpSQYsaikeedlvVW-VDPLDG 121
Cdd:PLN02737 109 LTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG--------GVIGDSS----------SDY---------LWcIDPLDG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 122 TKEYTEGlLDNVTVLIGIAYEGKAIAGVINQpyynYEAGPDAVLGRTIWGVLGLGAF--GFQLkevpagkHIITTTRSHS 199
Cdd:PLN02737 162 TTNFAHG-YPSFAVSVGVLFRGTPAAATVVE----FVGGPMCWNTRTFSASAGGGAFcnGQKI-------HVSQTDKVER 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931 200 NKLVT------DCVAAMNPD----------AVLRVGGAGNKIIQLIEGKASAYvfASPGCKKWDTCAPEVILHAVGGKLT 263
Cdd:PLN02737 230 SLLVTgfgyehDDAWATNIElfkeftdvsrGVRRLGAAAVDMCHVALGIVEAY--WEYRLKPWDMAAGVLIVEEAGGTVT 307

                 ....
gi 530365931 264 DIHG 267
Cdd:PLN02737 308 RMDG 311
PLN02553 PLN02553
inositol-phosphate phosphatase
8-178 4.20e-05

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 44.30  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931   8 LMRLVASAYSIAQKAGMIVRRVIAEGDlgIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpSEEVDQELI 87
Cdd:PLN02553   7 LEQFLEVAVDAAKAAGQIIRKGFYQTK--HVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEET--TAASGGTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365931  88 EDSqweeilkqPCpsqysaikeedlvvW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyeagpdaVLG 166
Cdd:PLN02553  83 TDE--------PT--------------WiVDPLDGTTNFVHG-FPFVCVSIGLTIGKVPVVGVVYNP----------ILD 129
                        170
                 ....*....|..
gi 530365931 167 RTIWGVLGLGAF 178
Cdd:PLN02553 130 ELFTAVKGKGAF 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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