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Conserved domains on  [gi|2024390618|ref|XP_040552981|]
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3'(2'),5'-bisphosphate nucleotidase 1 isoform X1 [Gallus gallus]

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 ...
11-296 9.45e-141

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: 399.00  E-value: 9.45e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  11 VASAYSVAEKAATIVRKVMAGGDLGIV-----EKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNEEL 85
Cdd:cd01640     2 LRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  86 IEDGYCEEILKKSCPAQYTGIKEEELVIWVDPLDGTKEYTEGLLDHVTVLIGIAYGGKAIAGVINQPYYNYEAGADAVLG 165
Cdd:cd01640    82 RDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 166 RTIWGVLGIGAFGFQLTE-VPAGKHIIVTTRSHGSTLVNdCISALNPDSVIRVGGAGNKIIQLIEGKASAYVFASPGCKK 244
Cdd:cd01640   162 RTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024390618 245 WDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMNSAGVLATLR-NYDYYASR 296
Cdd:cd01640   241 WDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-296 9.45e-141

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: 399.00  E-value: 9.45e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  11 VASAYSVAEKAATIVRKVMAGGDLGIV-----EKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNEEL 85
Cdd:cd01640     2 LRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  86 IEDGYCEEILKKSCPAQYTGIKEEELVIWVDPLDGTKEYTEGLLDHVTVLIGIAYGGKAIAGVINQPYYNYEAGADAVLG 165
Cdd:cd01640    82 RDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 166 RTIWGVLGIGAFGFQLTE-VPAGKHIIVTTRSHGSTLVNdCISALNPDSVIRVGGAGNKIIQLIEGKASAYVFASPGCKK 244
Cdd:cd01640   162 RTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024390618 245 WDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMNSAGVLATLR-NYDYYASR 296
Cdd:cd01640   241 WDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
10-289 5.49e-52

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 171.76  E-value: 5.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  10 VVASAYSVAEKAATIVRKVmAGGDLGIVEKS--GANDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNEelie 87
Cdd:pfam00459   5 VLKVAVELAAKAGEILREA-FSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTE---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  88 dgyceeilkkscpaqytgIKEEELVIWVDPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPYynyeagadavLGRT 167
Cdd:pfam00459  80 ------------------LTDDGPTWIIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF----------AGQL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 168 IWGVLGIGAF----GFQLTEVPAGKHIIVTTRSHGST--LVNDCI------SALNPDSVIRVGGAGNKIIQLIEGKASAY 235
Cdd:pfam00459 131 YSAAKGKGAFlngqPLPVSRAPPLSEALLVTLFGVSSrkDTSEASflakllKLVRAPGVRRVGSAALKLAMVAAGKADAY 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024390618 236 VFaSPGCKKWDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMNSAGVLATLRN 289
Cdd:pfam00459 211 IE-FGRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAGRVIAANPKVLHELLA 263
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
9-279 1.60e-37

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 134.13  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618   9 RVVASAYSVAEKAATIVRKVMAGgDLGIVEKSGANDLqTKADRLVQMSICASLTRKFPKATIIGEEelppeevneelied 88
Cdd:COG1218     3 ALLEAAIEIAREAGEAILEIYRA-DFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEE-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  89 gyceeilkkSCPAQYTGIKEEELVIWVDPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTI 168
Cdd:COG1218    67 ---------SAAIPYEERKSWDRFWLVDPLDGTKEFIKRN-GEFTVNIALIEDGRPVLGVVYAP----------ALGRLY 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 169 WGVLGIGAF----GFQLTEVPAGKH------IIVTTRSHGSTLVNDCISALNPDSVIRVGgAGNKIIQLIEGKASAYVFA 238
Cdd:COG1218   127 YAAKGQGAFketgGGERQPIRVRDRppaeplRVVASRSHRDEETEALLARLGVAELVSVG-SSLKFCLVAEGEADLYPRL 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2024390618 239 SPGCKkWDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMN 279
Cdd:COG1218   206 GPTME-WDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLN 245
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
17-273 6.05e-21

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: 89.43  E-value: 6.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  17 VAEKAATIVRKVMAGGdLGIVEKSGANDLqTKADRLVQMSICASLTRKFPKATIIGEEELPPeevneeliedgyceeilk 96
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDASI------------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  97 kscpaqytGIKEEELviW-----VDPLDGTKEYTEGLLDhVTVLIGIAYGGKAIAGVINQP-----YYNYEAGADAVLGR 166
Cdd:TIGR01331  68 --------PLTPRQT--WqrfwlVDPLDGTKEFINRNGD-FTVNIALVEHGVPVLGVVYAPatgvtYFATAGKAAKREGD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 167 TIWGVLGIgafgfQLTEVPAGKHIIVTTRSHGSTLVNDCISALNPDSVIrVGGAGNKIIQLIEGKASAYVFASPgCKKWD 246
Cdd:TIGR01331 137 GQALKAPI-----HVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIYPRLGP-TGEWD 209
                         250       260
                  ....*....|....*....|....*..
gi 2024390618 247 TCAPEAILHAVGGKITDIHGNSFQYNK 273
Cdd:TIGR01331 210 TAAGHAVLAAAGGAIFDLDGSPLLYGK 236
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
114-271 9.84e-09

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 55.08  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 114 W-VDPLDGTKEYTE--GlldHVTVLIGIAYGGKAIAGVINQPYYN--YeAGADAVLGRTIWGVLgigafgFQLTEVPAGK 188
Cdd:PRK10931   80 WlVDPLDGTKEFIKrnG---EFTVNIALIEQGKPVLGVVYAPVMNvmY-SAAEGKAWKEECGVR------KQIQVRDARP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 189 HIIVTTRSHGSTLVNDCISALNPDSVIRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEAILHAVGGKITDIHGNS 268
Cdd:PRK10931  150 PLVVISRSHADAELKEYLQQLGEHQTTSI-GSSLKFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQGKT 227

                  ...
gi 2024390618 269 FQY 271
Cdd:PRK10931  228 LDY 230
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-296 9.45e-141

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: 399.00  E-value: 9.45e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  11 VASAYSVAEKAATIVRKVMAGGDLGIV-----EKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNEEL 85
Cdd:cd01640     2 LRSLLAVAEKAGGIARDVVKKGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  86 IEDGYCEEILKKSCPAQYTGIKEEELVIWVDPLDGTKEYTEGLLDHVTVLIGIAYGGKAIAGVINQPYYNYEAGADAVLG 165
Cdd:cd01640    82 RDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 166 RTIWGVLGIGAFGFQLTE-VPAGKHIIVTTRSHGSTLVNdCISALNPDSVIRVGGAGNKIIQLIEGKASAYVFASPGCKK 244
Cdd:cd01640   162 RTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024390618 245 WDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMNSAGVLATLR-NYDYYASR 296
Cdd:cd01640   241 WDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLLATIRsNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
10-289 5.49e-52

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 171.76  E-value: 5.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  10 VVASAYSVAEKAATIVRKVmAGGDLGIVEKS--GANDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNEelie 87
Cdd:pfam00459   5 VLKVAVELAAKAGEILREA-FSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTE---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  88 dgyceeilkkscpaqytgIKEEELVIWVDPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPYynyeagadavLGRT 167
Cdd:pfam00459  80 ------------------LTDDGPTWIIDPIDGTKNFVHGI-PQFAVSIGLAVNGEPVLGVIYQPF----------AGQL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 168 IWGVLGIGAF----GFQLTEVPAGKHIIVTTRSHGST--LVNDCI------SALNPDSVIRVGGAGNKIIQLIEGKASAY 235
Cdd:pfam00459 131 YSAAKGKGAFlngqPLPVSRAPPLSEALLVTLFGVSSrkDTSEASflakllKLVRAPGVRRVGSAALKLAMVAAGKADAY 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024390618 236 VFaSPGCKKWDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMNSAGVLATLRN 289
Cdd:pfam00459 211 IE-FGRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAGRVIAANPKVLHELLA 263
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
9-279 1.60e-37

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 134.13  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618   9 RVVASAYSVAEKAATIVRKVMAGgDLGIVEKSGANDLqTKADRLVQMSICASLTRKFPKATIIGEEelppeevneelied 88
Cdd:COG1218     3 ALLEAAIEIAREAGEAILEIYRA-DFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEE-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  89 gyceeilkkSCPAQYTGIKEEELVIWVDPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTI 168
Cdd:COG1218    67 ---------SAAIPYEERKSWDRFWLVDPLDGTKEFIKRN-GEFTVNIALIEDGRPVLGVVYAP----------ALGRLY 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 169 WGVLGIGAF----GFQLTEVPAGKH------IIVTTRSHGSTLVNDCISALNPDSVIRVGgAGNKIIQLIEGKASAYVFA 238
Cdd:COG1218   127 YAAKGQGAFketgGGERQPIRVRDRppaeplRVVASRSHRDEETEALLARLGVAELVSVG-SSLKFCLVAEGEADLYPRL 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2024390618 239 SPGCKkWDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMN 279
Cdd:COG1218   206 GPTME-WDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLN 245
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
17-286 5.20e-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: 116.26  E-value: 5.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  17 VAEKAATIVRKVMaGGDLGIVEKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEelppeevneeliedgYCEEILK 96
Cdd:cd01637     7 AVREAGALILEAF-GEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEE---------------GGGSGNV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  97 KScpaqytgikeEELVIWVDPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTIWGVLGIGA 176
Cdd:cd01637    71 SD----------GGRVWVIDPIDGTTNFVAGL-PNFAVSIALYEDGKPVLGVIYDP----------MLDELYYAGRGKGA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 177 FGF-----QLTEVPAGKHIIVTTRSHGSTLVNDCISALNPDSVI--RVGGAGNKIIQLIEGKASAYVfaSPGCKKWDTCA 249
Cdd:cd01637   130 FLNgkklpLSKDTPLNDALLSTNASMLRSNRAAVLASLVNRALGirIYGSAGLDLAYVAAGRLDAYL--SSGLNPWDYAA 207
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2024390618 250 PEAILHAVGGKITDIHGNsfqynkEVKHMNSAGVLAT 286
Cdd:cd01637   208 GALIVEEAGGIVTDLDGE------PLDTLNRSGIIAA 238
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
18-274 1.06e-30

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: 115.40  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  18 AEKAATIVRKVmAGGDLGIVEKSGaNDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNeeliedgyceeilkk 97
Cdd:cd01638     9 AREAGDAILEV-YRGGFTVERKED-GSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRL--------------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  98 scPAQYtgikeeelvIW-VDPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTIWGVLGIGA 176
Cdd:cd01638    72 --GWDR---------FWlVDPLDGTREFIKGN-GEFAVNIALVEDGRPVLGVVYAP----------ALGELYYALRGGGA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 177 F--------GFQLTEVPAGKHIIVTTRSHGSTLVNDCISALNPDSVIRVGGaGNKIIQLIEGKASAYVFASPGCKkWDTC 248
Cdd:cd01638   130 YkngrpgavSLQARPPPLQPLRVVASRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTME-WDTA 207
                         250       260
                  ....*....|....*....|....*.
gi 2024390618 249 APEAILHAVGGKITDIHGNSFQYNKE 274
Cdd:cd01638   208 AGDAVLRAAGGAVSDLDGSPLTYNRE 233
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
17-286 1.69e-28

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: 109.93  E-value: 1.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  17 VAEKAATIVRKVMAGGDLGIVEKsGANDLQTKADRLVQMSICASLTRKFPKATIIGEeelppEEVNEELIEDGYCeeilk 96
Cdd:COG0483    10 AARAAGALILRRFRELDLEVETK-GDGDLVTEADRAAEAAIRERLRAAFPDHGILGE-----ESGASEGRDSGYV----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  97 kscpaqytgikeeelviWV-DPLDGTKEYTEGlLDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTIWGVLGIG 175
Cdd:COG0483    79 -----------------WViDPIDGTTNFVHG-LPLFAVSIALVRDGEPVAGVVYDP----------ALGELFTAARGGG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 176 AF--GFQL---TEVPAGKHIIVTTRSHGSTLVN--DCISALNPD--SVIRVGGAGNKIIQLIEGKASAYVfaSPGCKKWD 246
Cdd:COG0483   131 AFlnGRRLrvsARTDLEDALVATGFPYLRDDREylAALAALLPRvrRVRRLGSAALDLAYVAAGRLDAFV--EAGLKPWD 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2024390618 247 TCAPEAILHAVGGKITDIHGNSFqynkevkHMNSAGVLAT 286
Cdd:COG0483   209 IAAGALIVREAGGVVTDLDGEPL-------DLGSGSLVAA 241
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
14-269 3.99e-24

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: 97.99  E-value: 3.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  14 AYSVAEKAATIVRKVMAGGDLGIVEKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEElppeeVNEELIEDGYCee 93
Cdd:cd01639     5 AIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES-----GAAGGLTDEPT-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  94 ilkkscpaqytgikeeelviW-VDPLDGTKEYTEGlLDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTIWGVL 172
Cdd:cd01639    78 --------------------WiIDPLDGTTNFVHG-FPHFAVSIALAVKGEPVVGVVYDP----------IRNELFTAVR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 173 GIGAFgfqLTevpaGKHIIVTTRSHgstlVNDCISA--LNPDSVIRVGGAGNKIIQLIE---------GKAS---AYV-- 236
Cdd:cd01639   127 GQGAF---LN----GRRIRVSGRKE----LKDALVAtgFPYDRGDNFDRYLNNFAKLLAkavrgvrrlGSAAldlAYVaa 195
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2024390618 237 -----FASPGCKKWDTCAPEAILHAVGGKITDIHGNSF 269
Cdd:cd01639   196 grldgYWERGLKPWDVAAGALIVREAGGLVTDFDGGPF 233
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
17-273 6.05e-21

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: 89.43  E-value: 6.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  17 VAEKAATIVRKVMAGGdLGIVEKSGANDLqTKADRLVQMSICASLTRKFPKATIIGEEELPPeevneeliedgyceeilk 96
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDASI------------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  97 kscpaqytGIKEEELviW-----VDPLDGTKEYTEGLLDhVTVLIGIAYGGKAIAGVINQP-----YYNYEAGADAVLGR 166
Cdd:TIGR01331  68 --------PLTPRQT--WqrfwlVDPLDGTKEFINRNGD-FTVNIALVEHGVPVLGVVYAPatgvtYFATAGKAAKREGD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 167 TIWGVLGIgafgfQLTEVPAGKHIIVTTRSHGSTLVNDCISALNPDSVIrVGGAGNKIIQLIEGKASAYVFASPgCKKWD 246
Cdd:TIGR01331 137 GQALKAPI-----HVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGSADIYPRLGP-TGEWD 209
                         250       260
                  ....*....|....*....|....*..
gi 2024390618 247 TCAPEAILHAVGGKITDIHGNSFQYNK 273
Cdd:TIGR01331 210 TAAGHAVLAAAGGAIFDLDGSPLLYGK 236
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
17-286 1.26e-19

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: 86.60  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  17 VAEKAATIVRKVMAG-GDLGIVEKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEELppeevneeliedgyceeil 95
Cdd:cd01517     8 AVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS------------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  96 kkscpaqytgiKEEELVIWVDPLDGTKEYTEGLLdhVTVLIGIAYGGKAIAGVINQPYYNYEagaDAVLGRTIWGVLGIG 175
Cdd:cd01517    69 -----------AALGRFWVLDPIDGTKGFLRGDQ--FAVALALIEDGEVVLGVIGCPNLPLD---DGGGGDLFSAVRGQG 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 176 AF--------GFQLTEVPAGKHIIVT-----TRSHGSTLVNDCISALNPDSVIRVGGAGNKIIQLIEGKASAYV-FASPG 241
Cdd:cd01517   133 AWlrpldgssLQPLSVRQLTNAARASfcesvESAHSSHRLQAAIKALGGTPQPVRLDSQAKYAAVARGAADFYLrLPLSM 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2024390618 242 CKK---WDTCAPEAILHAVGGKITDIHGNSFQYNKEVKHMNSAGVLAT 286
Cdd:cd01517   213 SYRekiWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIAA 260
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
17-263 3.98e-19

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: 83.21  E-value: 3.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  17 VAEKAATIVRKVMAGGDLGIVE-KSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEElppEEVNEELIEDGyceeil 95
Cdd:cd01636     7 VAKEAGLAILKAFGRELSGKVKiTKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEES---GVAEEVMGRRD------ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  96 kkscpaqytgikeeELVIWVDPLDGTKEYTEGlLDHVTVLIGIayggkaiaGVINqpyynyeagadavlgrtiwgvlgig 175
Cdd:cd01636    78 --------------EYTWVIDPIDGTKNFING-LPFVAVVIAV--------YVIL------------------------- 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 176 afgfqltevpagkhiIVTTRSHGSTLVNDCISALNPDSVIR-VGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEAIL 254
Cdd:cd01636   110 ---------------ILAEPSHKRVDEKKAELQLLAVYRIRiVGSAVAKMCLVALGLADIYYEPGGKRRAWDVAASAAIV 174

                  ....*....
gi 2024390618 255 HAVGGKITD 263
Cdd:cd01636   175 REAGGIMTD 183
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
18-275 1.79e-13

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: 68.82  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  18 AEKAATIVRKvMAGGDLGIVEKSGAnDLQTKADRLVQMSICASLTRKFPKATIIGEEELPPEEVNEEliedgyceeilkk 97
Cdd:cd01641     9 ADAAGQITLP-YFRTRLQVETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGY------------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  98 scpaqytgikeeelvIWV-DPLDGTKEYTEGLlDHVTVLIGIAYGGKAIAGVINQPYynyeagadavLGRTIWGVLGIGA 176
Cdd:cd01641    74 ---------------VWVlDPIDGTKSFIRGL-PVWGTLIALLHDGRPVLGVIDQPA----------LGERWIGARGGGT 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 177 FGFQLTEVPA--------GKHIIVTTRSHGSTLVNDCISALNPDSV--IRVGGAGNKIIQLIEGKASayVFASPGCKKWD 246
Cdd:cd01641   128 FLNGAGGRPLrvracadlAEAVLSTTDPHFFTPGDRAAFERLARAVrlTRYGGDCYAYALVASGRVD--LVVEAGLKPYD 205
                         250       260
                  ....*....|....*....|....*....
gi 2024390618 247 TCAPEAILHAVGGKITDIHGNSFQYNKEV 275
Cdd:cd01641   206 VAALIPIIEGAGGVITDWDGGPLTGGSGR 234
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
37-262 4.09e-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: 64.66  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  37 VEKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEElppeevNEELIEDGYCeeilkkscpaqytgikeeelviWV- 115
Cdd:cd01643    25 AETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG------GGIFPSSGWY----------------------WVi 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 116 DPLDGTKEYTEGlLDHVTVLIGIAYGGKAIAGVINQPyynyeagadaVLGRTIWGVLGIGAFgfqLTEVPAGKHIIVTTR 195
Cdd:cd01643    77 DPIDGTTNFARG-IPIWAISIALLYRGEPVFGVIALP----------ALNQTFVAFKGGGAF---LNGKPLALHPPLQLP 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390618 196 ShGSTLVNDCISALnPDSVIRVG--GAGNKIIQLieGKAS---AYVFA-------SPGCKKWDTCAPEAILHAVGGKIT 262
Cdd:cd01643   143 D-CNVGFNRSSRAS-ARAVLRVIlrRFPGKIRML--GSASlnlASVAAgqtlgyvEATPKIWDIAAAWVILREAGGSWT 217
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
114-271 9.84e-09

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 55.08  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 114 W-VDPLDGTKEYTE--GlldHVTVLIGIAYGGKAIAGVINQPYYN--YeAGADAVLGRTIWGVLgigafgFQLTEVPAGK 188
Cdd:PRK10931   80 WlVDPLDGTKEFIKrnG---EFTVNIALIEQGKPVLGVVYAPVMNvmY-SAAEGKAWKEECGVR------KQIQVRDARP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 189 HIIVTTRSHGSTLVNDCISALNPDSVIRVgGAGNKIIQLIEGKASAYVFASPGCkKWDTCAPEAILHAVGGKITDIHGNS 268
Cdd:PRK10931  150 PLVVISRSHADAELKEYLQQLGEHQTTSI-GSSLKFCLVAEGQAQLYPRFGPTN-IWDTAAGHAVAIAAGAHVHDWQGKT 227

                  ...
gi 2024390618 269 FQY 271
Cdd:PRK10931  228 LDY 230
PLN02911 PLN02911
inositol-phosphate phosphatase
1-152 1.44e-07

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 52.03  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618   1 MASPTLLM-RVVASAYSVAEKAATIVRKVMAGGdLGIVEKSGANDLqTKADRLVQMSICASLTRKFPKATIIGEEElppe 79
Cdd:PLN02911   26 SALSDAVLdRFVDVAHKLADAAGEVTRKYFRTK-FEIIDKEDLSPV-TIADRAAEEAMRSIILENFPSHAIFGEEH---- 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024390618  80 evneeliedgyceEILKKSCPAQYTgikeeelviWV-DPLDGTKEYTEGLLDHVTvLIGIAYGGKAIAGVINQP 152
Cdd:PLN02911  100 -------------GLRCGEGSSDYV---------WVlDPIDGTKSFITGKPLFGT-LIALLYKGKPVLGIIDQP 150
PRK10757 PRK10757
inositol-1-monophosphatase;
14-285 3.35e-07

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 50.58  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  14 AYSVAEKAATIVRKVMAGGDLGIVEKSGANDLQTKADRLVQMSICASLTRKFPKATIIGEEelppeevneeliedgyCEE 93
Cdd:PRK10757    8 AVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEE----------------SGE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618  94 ILKkscpaqytgikEEELVIWV-DPLDGTKEYTEgLLDHVTVLIGIAYGGKAIAGVINQPYYN--YEA--GADAVL---- 164
Cdd:PRK10757   72 LEG-----------EDQDVQWViDPLDGTTNFIK-RLPHFAVSIAVRIKGRTEVAVVYDPMRNelFTAtrGQGAQLngyr 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390618 165 -----GRTIWGVLGIGAFGFQltevpAGKHIIVTTRSHGStLVNDCIsalnpdSVIRVGGAGNKIIQLIEGKASAYVfaS 239
Cdd:PRK10757  140 lrgstARDLDGTILATGFPFK-----AKQHATTYINIVGK-LFTECA------DFRRTGSAALDLAYVAAGRVDGFF--E 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2024390618 240 PGCKKWDTCAPEAILHAVGGKITDIHGNSfqynkevKHMNSAGVLA 285
Cdd:PRK10757  206 IGLKPWDFAAGELLVREAGGIVSDFTGGH-------NYMLTGNIVA 244
 
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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