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Conserved domains on  [gi|530365927|ref|XP_005273055|]
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3'(2'),5'-bisphosphate nucleotidase 1 isoform X1 [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 ...
11-312 1.26e-143

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: 406.71  E-value: 1.26e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  86 LIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYennekqql 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEK-------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 166 rehrneaKAGPDAVLGRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLI 244
Cdd:cd01640  153 -------TAGAGAWLGRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVL 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530365927 245 EGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 312
Cdd:cd01640  225 EGLADAYVHSTGGIKKWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-312 1.26e-143

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: 406.71  E-value: 1.26e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  86 LIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYennekqql 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEK-------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 166 rehrneaKAGPDAVLGRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLI 244
Cdd:cd01640  153 -------TAGAGAWLGRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVL 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530365927 245 EGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 312
Cdd:cd01640  225 EGLADAYVHSTGGIKKWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
15-283 6.11e-52

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 172.14  E-value: 6.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   15 AYSIAQKAGMIVRRVIAEgDLGIVEKTC--ATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeliedsqw 92
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGKsgANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQ---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   93 eeilkqpcpsqySAIKEEDLVVWVDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyennekqqlrehrnea 172
Cdd:pfam00459  78 ------------TELTDDGPTWIIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  173 kagpdavLGRTIWGVLGLGAF--GFQLKEVPAG----KHIITTTRSHSNKLVTDC------VAAMNPDAVLRVGGAGNKI 240
Cdd:pfam00459 127 -------AGQLYSAAKGKGAFlnGQPLPVSRAPplseALLVTLFGVSSRKDTSEAsflaklLKLVRAPGVRRVGSAALKL 199
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 530365927  241 IQLIEGKASAYVFaSPGCKKWDTCAPEVILHAVGGKLTDIHGN 283
Cdd:pfam00459 200 AMVAAGKADAYIE-FGRLKPWDHAAGVAILREAGGVVTDADGG 241
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-295 1.41e-34

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 126.81  E-value: 1.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  10 RLVASAYSIAQKAGMIVRRvIAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDlpseeVDQELIED 89
Cdd:COG1218    3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEES-----AAIPYEER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  90 SQWEEilkqpcpsqysaikeedlvVW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlreh 168
Cdd:COG1218   76 KSWDR-------------------FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP--------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 169 rneakagpdaVLGRTIWGVLGLGAF----GFQLKEVPAGKH------IITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGN 238
Cdd:COG1218  121 ----------ALGRLYYAAKGQGAFketgGGERQPIRVRDRppaeplRVVASRSHRDEETEALLARLGVAELVSV-GSSL 189
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530365927 239 KIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMN 295
Cdd:COG1218  190 KFCLVAEGEADLYPRLGPTM-EWDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLN 245
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-289 5.69e-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: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDLPseevdQELIEDSQWEEIlk 97
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDAS-----IPLTPRQTWQRF-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   98 qpcpsqysaikeedlvvW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQP-----YYNYENNekqqlrehrNE 171
Cdd:TIGR01331  79 -----------------WlVDPLDGTKEFINR-NGDFTVNIALVEHGVPVLGVVYAPatgvtYFATAGK---------AA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  172 AKAGPDAVLGRTIwgvlglgafgfQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLrVGGAGNKIIQLIEGKASAY 251
Cdd:TIGR01331 132 KREGDGQALKAPI-----------HVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIY 199
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 530365927  252 VFASPgCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHK 289
Cdd:TIGR01331 200 PRLGP-TGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
48-287 2.52e-10

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 59.71  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  48 TKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQeliedsQWEeilkqpcpsQYsaikeedlvvW-VDPLDGTKEYt 126
Cdd:PRK10931  38 TAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ------HWQ---------RY----------WlVDPLDGTKEF- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 127 egLLDN--VTVLIGIAYEGKAIAGVINQPYYN--YENNEKQQLREHRNEAKagpdavlgrtiwgvlglgafgfQLKEVPA 202
Cdd:PRK10931  92 --IKRNgeFTVNIALIEQGKPVLGVVYAPVMNvmYSAAEGKAWKEECGVRK----------------------QIQVRDA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 203 GKHIITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHG 282
Cdd:PRK10931 148 RPPLVVISRSHADAELKEYLQQLGEHQTTSI-GSSLKFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQG 225

                 ....*
gi 530365927 283 NVLQY 287
Cdd:PRK10931 226 KTLDY 230
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-312 1.26e-143

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: 406.71  E-value: 1.26e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  11 LVASAYSIAQKAGMIVRRVIAEGDLGIV-----EKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  86 LIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYennekqql 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEK-------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 166 rehrneaKAGPDAVLGRTIWGVLGLGAFGFQLKE-VPAGKHIITTTRSHSNKLVTdCVAAMNPDAVLRVGGAGNKIIQLI 244
Cdd:cd01640  153 -------TAGAGAWLGRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVL 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530365927 245 EGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLR-NYDYYASR 312
Cdd:cd01640  225 EGLADAYVHSTGGIKKWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
15-283 6.11e-52

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 172.14  E-value: 6.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   15 AYSIAQKAGMIVRRVIAEgDLGIVEKTC--ATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeliedsqw 92
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGKsgANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQ---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   93 eeilkqpcpsqySAIKEEDLVVWVDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyennekqqlrehrnea 172
Cdd:pfam00459  78 ------------TELTDDGPTWIIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  173 kagpdavLGRTIWGVLGLGAF--GFQLKEVPAG----KHIITTTRSHSNKLVTDC------VAAMNPDAVLRVGGAGNKI 240
Cdd:pfam00459 127 -------AGQLYSAAKGKGAFlnGQPLPVSRAPplseALLVTLFGVSSRKDTSEAsflaklLKLVRAPGVRRVGSAALKL 199
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 530365927  241 IQLIEGKASAYVFaSPGCKKWDTCAPEVILHAVGGKLTDIHGN 283
Cdd:pfam00459 200 AMVAAGKADAYIE-FGRLKPWDHAAGVAILREAGGVVTDADGG 241
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-295 1.41e-34

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 126.81  E-value: 1.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  10 RLVASAYSIAQKAGMIVRRvIAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDlpseeVDQELIED 89
Cdd:COG1218    3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEES-----AAIPYEER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  90 SQWEEilkqpcpsqysaikeedlvVW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlreh 168
Cdd:COG1218   76 KSWDR-------------------FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP--------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 169 rneakagpdaVLGRTIWGVLGLGAF----GFQLKEVPAGKH------IITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGN 238
Cdd:COG1218  121 ----------ALGRLYYAAKGQGAFketgGGERQPIRVRDRppaeplRVVASRSHRDEETEALLARLGVAELVSV-GSSL 189
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530365927 239 KIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMN 295
Cdd:COG1218  190 KFCLVAEGEADLYPRLGPTM-EWDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLN 245
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
11-290 2.72e-29

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: 112.32  E-value: 2.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  11 LVASAYSIAQKAGMIVRRViAEGDLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeliedS 90
Cdd:cd01638    1 LLELLIRIAREAGDAILEV-YRGGFTVERKEDGSPV-TAADLAANAFIVEGLAALRPDIPVLSEESADDPLR-------L 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  91 QWEEilkqpcpsqysaikeedlvVW-VDPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlrehr 169
Cdd:cd01638   72 GWDR-------------------FWlVDPLDGTREFIKGN-GEFAVNIALVEDGRPVLGVVYAP---------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 170 neakagpdaVLGRTIWGVLGLGAF--------GFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGaGNKII 241
Cdd:cd01638  116 ---------ALGELYYALRGGGAYkngrpgavSLQARPPPLQPLRVVASRSHPDEELEALLAALGVAEVVSIGS-SLKFC 185
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530365927 242 QLIEGKASAYVFASPGCKkWDTCAPEVILHAVGGKLTDIHGNVLQYHKD 290
Cdd:cd01638  186 LVAEGEADIYPRLGPTME-WDTAAGDAVLRAAGGAVSDLDGSPLTYNRE 233
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
18-302 1.99e-28

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: 109.71  E-value: 1.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpsEEVDQELIEDSQWeeilk 97
Cdd:cd01637    7 AVREAGALILEAFGEE-LTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG---GGSGNVSDGGRVW----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  98 qpcpsqysaikeedlvvWVDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlrehrneakagpd 177
Cdd:cd01637   78 -----------------VIDPIDGTTNFVAG-LPNFAVSIALYEDGKPVLGVIYDP------------------------ 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 178 aVLGRTIWGVLGLGAFGF-----QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDA--VLRVGGAGNKIIQLIEGKASA 250
Cdd:cd01637  116 -MLDELYYAGRGKGAFLNgkklpLSKDTPLNDALLSTNASMLRSNRAAVLASLVNRAlgIRIYGSAGLDLAYVAAGRLDA 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530365927 251 YVfaSPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHkdvkhmNSAGVLAT 302
Cdd:cd01637  195 YL--SSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTL------NRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
9-302 3.76e-25

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: 101.46  E-value: 3.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   9 MRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTcATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQELie 88
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRELDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGY-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  89 dsqweeilkqpcpsqysaikeedlvVWV-DPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlre 167
Cdd:COG0483   78 -------------------------VWViDPIDGTTNFVHG-LPLFAVSIALVRDGEPVAGVVYDP-------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 168 hrneakagpdaVLGRTIWGVLGLGAF--GFQLK---EVPAGKHIITTTRSH--SNKLVTDCVAAMNPDA--VLRVGGAGN 238
Cdd:COG0483  118 -----------ALGELFTAARGGGAFlnGRRLRvsaRTDLEDALVATGFPYlrDDREYLAALAALLPRVrrVRRLGSAAL 186
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530365927 239 KIIQLIEGKASAYVfaSPGCKKWDTCAPEVILHAVGGKLTDIHGNVLqyhkdvkHMNSAGVLAT 302
Cdd:COG0483  187 DLAYVAAGRLDAFV--EAGLKPWDIAAGALIVREAGGVVTDLDGEPL-------DLGSGSLVAA 241
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-289 5.69e-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: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   18 IAQKAGMIVRRVIAEGdLGIVEKTCATDLqTKADRLAQMSICSSLARKFPKLTIIGEEDLPseevdQELIEDSQWEEIlk 97
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDAS-----IPLTPRQTWQRF-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   98 qpcpsqysaikeedlvvW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQP-----YYNYENNekqqlrehrNE 171
Cdd:TIGR01331  79 -----------------WlVDPLDGTKEFINR-NGDFTVNIALVEHGVPVLGVVYAPatgvtYFATAGK---------AA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  172 AKAGPDAVLGRTIwgvlglgafgfQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLrVGGAGNKIIQLIEGKASAY 251
Cdd:TIGR01331 132 KREGDGQALKAPI-----------HVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIY 199
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 530365927  252 VFASPgCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHK 289
Cdd:TIGR01331 200 PRLGP-TGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
15-283 2.78e-20

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: 87.98  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  15 AYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpseevdqeliedsqwee 94
Cdd:cd01639    5 AIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES------------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  95 ilkqpcpsqYSAIKEEDLVVW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlreHRNEak 173
Cdd:cd01639   67 ---------GAAGGLTDEPTWiIDPLDGTTNFVHG-FPHFAVSIALAVKGEPVVGVVYDP--------------IRNE-- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 174 agpdavlgrTIWGVLGLGAF--GFQLK--------------EVPAGKH-IITTTRSHSNKLVTDCVAamnpdAVLRVGGA 236
Cdd:cd01639  121 ---------LFTAVRGQGAFlnGRRIRvsgrkelkdalvatGFPYDRGdNFDRYLNNFAKLLAKAVR-----GVRRLGSA 186
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530365927 237 GNKIIQLIEGKASAYVFAspGCKKWDTCAPEVILHAVGGKLTDIHGN 283
Cdd:cd01639  187 ALDLAYVAAGRLDGYWER--GLKPWDVAAGALIVREAGGLVTDFDGG 231
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
9-302 3.35e-18

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: 82.75  E-value: 3.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   9 MRLVASAysIAQKAGMIVRRVIAE-GDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLpseevdqeli 87
Cdd:cd01517    1 ELEVAIL--AVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  88 edsqweeilkqpcpsqysaiKEEDLVVWVDPLDGTKEYTEGLLdnVTVLIGIAYEGKAIAGVINQPYYNYENNEKqqlre 167
Cdd:cd01517   69 --------------------AALGRFWVLDPIDGTKGFLRGDQ--FAVALALIEDGEVVLGVIGCPNLPLDDGGG----- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 168 hrneakagpdavlGRTIWGVLGLGAFGFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGN--------- 238
Cdd:cd01517  122 -------------GDLFSAVRGQGAWLRPLDGSSLQPLSVRQLTNAARASFCESVESAHSSHRLQAAIKALggtpqpvrl 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530365927 239 ----KIIQLIEGKASAYV-FASPGCKK---WDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLAT 302
Cdd:cd01517  189 dsqaKYAAVARGAADFYLrLPLSMSYRekiWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIAA 260
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
18-279 2.49e-16

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: 75.51  E-value: 2.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  18 IAQKAGMIVRRVIAEGDLGIVEKTCAT-DLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVdqeLIEDSQWeeil 96
Cdd:cd01636    7 VAKEAGLAILKAFGRELSGKVKITKSDnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEV---MGRRDEY---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  97 kqpcpsqysaikeedlVVWVDPLDGTKEYTEGlLDNVTVLIGIA----YEGKAIAGVINQPYynyennEKQQLREHRnea 172
Cdd:cd01636   80 ----------------TWVIDPIDGTKNFING-LPFVAVVIAVYviliLAEPSHKRVDEKKA------ELQLLAVYR--- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 173 kagpdavlgrtiwgvlglgafgfqlkevpagkhiitttrshsnklvtdcvaamnpdaVLRVGGAGNKIIQLIEGKASAYV 252
Cdd:cd01636  134 ---------------------------------------------------------IRIVGSAVAKMCLVALGLADIYY 156
                        250       260
                 ....*....|....*....|....*..
gi 530365927 253 FASPGCKKWDTCAPEVILHAVGGKLTD 279
Cdd:cd01636  157 EPGGKRRAWDVAASAAIVREAGGIMTD 183
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
12-286 2.97e-12

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: 65.35  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  12 VASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIGEEdlpseevdq 84
Cdd:cd01641    2 LAFALELADAAGQITLPyfrtrlqVETKADFSPV---------TEADRAAEAAMRELIAAAFPDHGILGEE--------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  85 eliedsqweeilkqpcpsqYSAIKEEDLVVWV-DPLDGTKEYTEGLlDNVTVLIGIAYEGKAIAGVINQPYynyennekq 163
Cdd:cd01641   64 -------------------FGNEGGDAGYVWVlDPIDGTKSFIRGL-PVWGTLIALLHDGRPVLGVIDQPA--------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 164 qlrehrneakagpdavLGRTIWGVLGLGAFgfqlKEVPAGKHIITttrSHSNKLVTDCVAAMNPDAVLRVGGAG----NK 239
Cdd:cd01641  115 ----------------LGERWIGARGGGTF----LNGAGGRPLRV---RACADLAEAVLSTTDPHFFTPGDRAAferlAR 171
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365927 240 IIQLIEGKASAYVFAS-----------PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQ 286
Cdd:cd01641  172 AVRLTRYGGDCYAYALvasgrvdlvveAGLKPYDVAALIPIIEGAGGVITDWDGGPLT 229
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
48-287 2.52e-10

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 59.71  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  48 TKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQeliedsQWEeilkqpcpsQYsaikeedlvvW-VDPLDGTKEYt 126
Cdd:PRK10931  38 TAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ------HWQ---------RY----------WlVDPLDGTKEF- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 127 egLLDN--VTVLIGIAYEGKAIAGVINQPYYN--YENNEKQQLREHRNEAKagpdavlgrtiwgvlglgafgfQLKEVPA 202
Cdd:PRK10931  92 --IKRNgeFTVNIALIEQGKPVLGVVYAPVMNvmYSAAEGKAWKEECGVRK----------------------QIQVRDA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 203 GKHIITTTRSHSNKLVTDCVAAMNPDAVLRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGGKLTDIHG 282
Cdd:PRK10931 148 RPPLVVISRSHADAELKEYLQQLGEHQTTSI-GSSLKFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQG 225

                 ....*
gi 530365927 283 NVLQY 287
Cdd:PRK10931 226 KTLDY 230
PLN02911 PLN02911
inositol-phosphate phosphatase
1-153 4.56e-10

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 59.73  E-value: 4.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   1 MASSNTVLMRLVASAYSIAQKAGMIVRR-------VIAEGDLGIVektcatdlqTKADRLAQMSICSSLARKFPKLTIIG 73
Cdd:PLN02911  26 SALSDAVLDRFVDVAHKLADAAGEVTRKyfrtkfeIIDKEDLSPV---------TIADRAAEEAMRSIILENFPSHAIFG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  74 EEDlpseevdqeliedsQWEeilkqpCPSQYSAIkeedlvVWV-DPLDGTKEYTEG--LLDnvtVLIGIAYEGKAIAGVI 150
Cdd:PLN02911  97 EEH--------------GLR------CGEGSSDY------VWVlDPIDGTKSFITGkpLFG---TLIALLYKGKPVLGII 147

                 ...
gi 530365927 151 NQP 153
Cdd:PLN02911 148 DQP 150
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
13-275 1.81e-09

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: 57.34  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  13 ASAYSIAQKAGmivRRVIAE-GDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpseevdQELIEDSQ 91
Cdd:cd01643    2 SLAEAIAQEAG---DRALADfGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG-------GGIFPSSG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  92 WeeilkqpcpsqysaikeedlvVWV-DPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQPyynyennekqqlrehrn 170
Cdd:cd01643   72 W---------------------YWViDPIDGTTNFARG-IPIWAISIALLYRGEPVFGVIALP----------------- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 171 eakagpdaVLGRTIWGVLGLGAF--GFQLK-EVPAGKHIITTTRSHSNKLVtdcvaamnPDAVLRVG--GAGNKIIQLie 245
Cdd:cd01643  113 --------ALNQTFVAFKGGGAFlnGKPLAlHPPLQLPDCNVGFNRSSRAS--------ARAVLRVIlrRFPGKIRML-- 174
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 530365927 246 GKAS---AYVFA-------SPGCKKWDTCAPEVILHAVGG 275
Cdd:cd01643  175 GSASlnlASVAAgqtlgyvEATPKIWDIAAAWVILREAGG 214
PRK10757 PRK10757
inositol-1-monophosphatase;
19-301 2.32e-07

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 51.35  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  19 AQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEE--DLPSEEvdqeliEDSQWEeil 96
Cdd:PRK10757  12 ARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEEsgELEGED------QDVQWV--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  97 kqpcpsqysaikeedlvvwVDPLDGTKEYTEgLLDNVTVLIGIAYEGKAIAGVINQPYYN--YENNEKQ--QLREHRNEA 172
Cdd:PRK10757  83 -------------------IDPLDGTTNFIK-RLPHFAVSIAVRIKGRTEVAVVYDPMRNelFTATRGQgaQLNGYRLRG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 173 KAGPDavLGRTIWgvlglgAFGFQLKEvpagKHIITTTRSHSNKLVTDCVaamnpdAVLRVGGAGNKIIQLIEGKASAYV 252
Cdd:PRK10757 143 STARD--LDGTIL------ATGFPFKA----KQHATTYINIVGKLFTECA------DFRRTGSAALDLAYVAAGRVDGFF 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530365927 253 faSPGCKKWDTCAPEVILHAVGGKLTDIHGNvlqyHkdvKHMNSAGVLA 301
Cdd:PRK10757 205 --EIGLKPWDFAAGELLVREAGGIVSDFTGG----H---NYMLTGNIVA 244
PLN02737 PLN02737
inositol monophosphatase family protein
43-282 6.19e-05

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 44.41  E-value: 6.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927  43 ATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpseevdqELIEDSQweeilkqpcpSQYsaikeedlvVW-VDPLDG 121
Cdd:PLN02737 109 LTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG--------GVIGDSS----------SDY---------LWcIDPLDG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 122 TKEYTEGlLDNVTVLIGIAYEGKAIAGVInqpyynyennekqqlrehrNEAKAGPDAVLGRTIWGVLGLGAF--GFQLke 199
Cdd:PLN02737 162 TTNFAHG-YPSFAVSVGVLFRGTPAAATV-------------------VEFVGGPMCWNTRTFSASAGGGAFcnGQKI-- 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927 200 vpagkHIITTTRSHSNKLVT------DCVAAMNPD----------AVLRVGGAGNKIIQLIEGKASAYvfASPGCKKWDT 263
Cdd:PLN02737 220 -----HVSQTDKVERSLLVTgfgyehDDAWATNIElfkeftdvsrGVRRLGAAAVDMCHVALGIVEAY--WEYRLKPWDM 292
                        250
                 ....*....|....*....
gi 530365927 264 CAPEVILHAVGGKLTDIHG 282
Cdd:PLN02737 293 AAGVLIVEEAGGTVTRMDG 311
PLN02553 PLN02553
inositol-phosphate phosphatase
8-153 2.72e-04

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 41.98  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365927   8 LMRLVASAYSIAQKAGMIVRRVIAEGDlgIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDlpSEEVDQELI 87
Cdd:PLN02553   7 LEQFLEVAVDAAKAAGQIIRKGFYQTK--HVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEET--TAASGGTEL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530365927  88 EDSqweeilkqPCpsqysaikeedlvvW-VDPLDGTKEYTEGlLDNVTVLIGIAYEGKAIAGVINQP 153
Cdd:PLN02553  83 TDE--------PT--------------WiVDPLDGTTNFVHG-FPFVCVSIGLTIGKVPVVGVVYNP 126
 
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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