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Conserved domains on  [gi|149040955|gb|EDL94912|]
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bisphosphate 3'-nucleotidase 1, isoform CRA_a, partial [Rattus norvegicus]

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 ...
11-275 1.11e-128

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


:

Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 367.42  E-value: 1.11e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  11 LVASAYSIAQKAGTIVRCVIAEGDLGIVQ-----KTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILLvegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  86 LIEDGQSEEILKQPCPSQYSAIKEEDLVVWVDPVDGTKEYTEGLLDNVTVLIGIAYEGKAIAGIINQPYYNYQnnekekl 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKT------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 166 rehrneakAGPDAVLGRTIWGVLGLGAFGFQLKE-APAGKHIITTTRSHSNKLVTdCIAAMNPDNVLRVGGAGNKIIQLI 244
Cdd:cd01640  154 --------AGAGAWLGRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVL 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 149040955 245 EGKASAYVFASPGCKKWDTCAPEVILHAVGG 275
Cdd:cd01640  225 EGLADAYVHSTGGIKKWDICAPEAILRALGG 255
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-275 1.11e-128

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 367.42  E-value: 1.11e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  11 LVASAYSIAQKAGTIVRCVIAEGDLGIVQ-----KTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILLvegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  86 LIEDGQSEEILKQPCPSQYSAIKEEDLVVWVDPVDGTKEYTEGLLDNVTVLIGIAYEGKAIAGIINQPYYNYQnnekekl 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKT------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 166 rehrneakAGPDAVLGRTIWGVLGLGAFGFQLKE-APAGKHIITTTRSHSNKLVTdCIAAMNPDNVLRVGGAGNKIIQLI 244
Cdd:cd01640  154 --------AGAGAWLGRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVL 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 149040955 245 EGKASAYVFASPGCKKWDTCAPEVILHAVGG 275
Cdd:cd01640  225 EGLADAYVHSTGGIKKWDICAPEAILRALGG 255
Inositol_P pfam00459
Inositol monophosphatase family;
15-275 2.31e-49

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 164.44  E-value: 2.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   15 AYSIAQKAGTIVRCVIAEgDLGIVQKT--SATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVdqeliedgqs 92
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQ---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   93 eeilkqpcpsqySAIKEEDLVVWVDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPYynyqnnekeklrehrnea 172
Cdd:pfam00459  78 ------------TELTDDGPTWIIDPIDGTKNFVHG-IPQFAVSIGLAVNGEPVLGVIYQPF------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  173 kagpdavLGRTIWGVLGLGAF----GFQLKEAPA--GKHIITTTRSHSNKLVTDC--IAAMNPDN----VLRVGGAGNKI 240
Cdd:pfam00459 127 -------AGQLYSAAKGKGAFlngqPLPVSRAPPlsEALLVTLFGVSSRKDTSEAsfLAKLLKLVrapgVRRVGSAALKL 199
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 149040955  241 IQLIEGKASAYVFaSPGCKKWDTCAPEVILHAVGG 275
Cdd:pfam00459 200 AMVAAGKADAYIE-FGRLKPWDHAAGVAILREAGG 233
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-275 3.32e-26

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 103.70  E-value: 3.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  10 RLVASAYSIAQKAGTIVRCvIAEGDLGIVQKTSATDLqTKADRMVQMSICSSLSRKFPKLTIIGEEDlppgeVDQELIED 89
Cdd:COG1218    3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEES-----AAIPYEER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  90 GQSEEilkqpcpsqysaikeedlvVW-VDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPyynyqnnekeklreh 168
Cdd:COG1218   76 KSWDR-------------------FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP--------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 169 rneakagpdaVLGRTIWGVLGLGAF----GFQLKE------APAGKHIITTTRSHSNKLVTDCIAAMNPDNVLRVgGAGN 238
Cdd:COG1218  121 ----------ALGRLYYAAKGQGAFketgGGERQPirvrdrPPAEPLRVVASRSHRDEETEALLARLGVAELVSV-GSSL 189
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 149040955 239 KIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGG 275
Cdd:COG1218  190 KFCLVAEGEADLYPRLGPTM-EWDTAAGQAILEAAGG 225
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-275 1.37e-20

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: 88.28  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   18 IAQKAGTIVRCVIAEGdLGIVQKTSATDLqTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGevdqeliedgqseeilk 97
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDASIP----------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   98 qpcpsqysaIKEEDlvVW-----VDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQP-----YYNYQNNekeklre 167
Cdd:TIGR01331  69 ---------LTPRQ--TWqrfwlVDPLDGTKEFINR-NGDFTVNIALVEHGVPVLGVVYAPatgvtYFATAGK------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  168 hrNEAKAGPDAVLGRTIwgvlglgafgfQLKEAPAGKHIITTTRSHSNKLVTDCIAAMNPDNVLrVGGAGNKIIQLIEGK 247
Cdd:TIGR01331 130 --AAKREGDGQALKAPI-----------HVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGS 195
                         250       260
                  ....*....|....*....|....*...
gi 149040955  248 ASAYVFASPgCKKWDTCAPEVILHAVGG 275
Cdd:TIGR01331 196 ADIYPRLGP-TGEWDTAAGHAVLAAAGG 222
PLN02911 PLN02911
inositol-phosphate phosphatase
1-153 4.30e-10

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 59.35  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   1 MASSHNVLMRLVASAYSIAQKAGTIVRC-------VIAEGDLGIVqktsatdlqTKADRMVQMSICSSLSRKFPKLTIIG 73
Cdd:PLN02911  26 SALSDAVLDRFVDVAHKLADAAGEVTRKyfrtkfeIIDKEDLSPV---------TIADRAAEEAMRSIILENFPSHAIFG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  74 EEDlppGEVdqelIEDGQSEeilkqpcpsqysaikeedlVVWV-DPVDGTKEYTEG--LLDnvtVLIGIAYEGKAIAGII 150
Cdd:PLN02911  97 EEH---GLR----CGEGSSD-------------------YVWVlDPIDGTKSFITGkpLFG---TLIALLYKGKPVLGII 147

                 ...
gi 149040955 151 NQP 153
Cdd:PLN02911 148 DQP 150
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
11-275 1.11e-128

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 367.42  E-value: 1.11e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  11 LVASAYSIAQKAGTIVRCVIAEGDLGIVQ-----KTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVDQE 85
Cdd:cd01640    1 LLRSLLAVAEKAGGIARDVVKKGRLLILLvegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  86 LIEDGQSEEILKQPCPSQYSAIKEEDLVVWVDPVDGTKEYTEGLLDNVTVLIGIAYEGKAIAGIINQPYYNYQnnekekl 165
Cdd:cd01640   81 SRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKPIAGVIHQPFYEKT------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 166 rehrneakAGPDAVLGRTIWGVLGLGAFGFQLKE-APAGKHIITTTRSHSNKLVTdCIAAMNPDNVLRVGGAGNKIIQLI 244
Cdd:cd01640  154 --------AGAGAWLGRTIWGLSGLGAHSSDFKErEDAGKIIVSTSHSHSVKEVQ-LITAGNKDEVLRAGGAGYKVLQVL 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 149040955 245 EGKASAYVFASPGCKKWDTCAPEVILHAVGG 275
Cdd:cd01640  225 EGLADAYVHSTGGIKKWDICAPEAILRALGG 255
Inositol_P pfam00459
Inositol monophosphatase family;
15-275 2.31e-49

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 164.44  E-value: 2.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   15 AYSIAQKAGTIVRCVIAEgDLGIVQKT--SATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVdqeliedgqs 92
Cdd:pfam00459   9 AVELAAKAGEILREAFSN-KLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQ---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   93 eeilkqpcpsqySAIKEEDLVVWVDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPYynyqnnekeklrehrnea 172
Cdd:pfam00459  78 ------------TELTDDGPTWIIDPIDGTKNFVHG-IPQFAVSIGLAVNGEPVLGVIYQPF------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  173 kagpdavLGRTIWGVLGLGAF----GFQLKEAPA--GKHIITTTRSHSNKLVTDC--IAAMNPDN----VLRVGGAGNKI 240
Cdd:pfam00459 127 -------AGQLYSAAKGKGAFlngqPLPVSRAPPlsEALLVTLFGVSSRKDTSEAsfLAKLLKLVrapgVRRVGSAALKL 199
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 149040955  241 IQLIEGKASAYVFaSPGCKKWDTCAPEVILHAVGG 275
Cdd:pfam00459 200 AMVAAGKADAYIE-FGRLKPWDHAAGVAILREAGG 233
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
10-275 3.32e-26

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 103.70  E-value: 3.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  10 RLVASAYSIAQKAGTIVRCvIAEGDLGIVQKTSATDLqTKADRMVQMSICSSLSRKFPKLTIIGEEDlppgeVDQELIED 89
Cdd:COG1218    3 ALLEAAIEIAREAGEAILE-IYRADFEVEEKADDSPV-TEADLAAHAIILAGLAALTPDIPVLSEES-----AAIPYEER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  90 GQSEEilkqpcpsqysaikeedlvVW-VDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPyynyqnnekeklreh 168
Cdd:COG1218   76 KSWDR-------------------FWlVDPLDGTKEFIKR-NGEFTVNIALIEDGRPVLGVVYAP--------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 169 rneakagpdaVLGRTIWGVLGLGAF----GFQLKE------APAGKHIITTTRSHSNKLVTDCIAAMNPDNVLRVgGAGN 238
Cdd:COG1218  121 ----------ALGRLYYAAKGQGAFketgGGERQPirvrdrPPAEPLRVVASRSHRDEETEALLARLGVAELVSV-GSSL 189
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 149040955 239 KIIQLIEGKASAYVFASPGCkKWDTCAPEVILHAVGG 275
Cdd:COG1218  190 KFCLVAEGEADLYPRLGPTM-EWDTAAGQAILEAAGG 225
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
18-275 1.66e-25

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: 101.24  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  18 IAQKAGTIVRCVIAEGdLGIVQKTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDlppGEVDQELIEDGqseeilk 97
Cdd:cd01637    7 AVREAGALILEAFGEE-LTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG---GGSGNVSDGGR------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  98 qpcpsqysaikeedlVVWVDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPyynyqnnekeklrehrneakagpd 177
Cdd:cd01637   76 ---------------VWVIDPIDGTTNFVAG-LPNFAVSIALYEDGKPVLGVIYDP------------------------ 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 178 aVLGRTIWGVLGLGAFGF-----QLKEAPAGKHIITTTRSHSNKLVTDCIAAMN--PDNVLRVGGAGNKIIQLIEGKASA 250
Cdd:cd01637  116 -MLDELYYAGRGKGAFLNgkklpLSKDTPLNDALLSTNASMLRSNRAAVLASLVnrALGIRIYGSAGLDLAYVAAGRLDA 194
                        250       260
                 ....*....|....*....|....*
gi 149040955 251 YVfaSPGCKKWDTCAPEVILHAVGG 275
Cdd:cd01637  195 YL--SSGLNPWDYAAGALIVEEAGG 217
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
11-275 1.42e-22

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: 93.44  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  11 LVASAYSIAQKAGTIVRCVIAEGDLgiVQKTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVdqeliedg 90
Cdd:cd01638    1 LLELLIRIAREAGDAILEVYRGGFT--VERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLR-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  91 qseeiLKQPCpsqysaikeedlvVW-VDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPyynyqnnekeklrehr 169
Cdd:cd01638   71 -----LGWDR-------------FWlVDPLDGTREFIKG-NGEFAVNIALVEDGRPVLGVVYAP---------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 170 neakagpdaVLGRTIWGVLGLGAF--------GFQLKEAPAGKHIITTTRSHSNKLVTDCIAAMNPDNVLRVGGaGNKII 241
Cdd:cd01638  116 ---------ALGELYYALRGGGAYkngrpgavSLQARPPPLQPLRVVASRSHPDEELEALLAALGVAEVVSIGS-SLKFC 185
                        250       260       270
                 ....*....|....*....|....*....|....
gi 149040955 242 QLIEGKASAYVFASPGCkKWDTCAPEVILHAVGG 275
Cdd:cd01638  186 LVAEGEADIYPRLGPTM-EWDTAAGDAVLRAAGG 218
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
18-275 1.37e-20

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: 88.28  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   18 IAQKAGTIVRCVIAEGdLGIVQKTSATDLqTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGevdqeliedgqseeilk 97
Cdd:TIGR01331   8 IARAAGEEILPVYQKE-LAVAQKADNSPV-TEADRAAHRFILEGLRALTPDIPVLSEEDASIP----------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   98 qpcpsqysaIKEEDlvVW-----VDPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQP-----YYNYQNNekeklre 167
Cdd:TIGR01331  69 ---------LTPRQ--TWqrfwlVDPLDGTKEFINR-NGDFTVNIALVEHGVPVLGVVYAPatgvtYFATAGK------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  168 hrNEAKAGPDAVLGRTIwgvlglgafgfQLKEAPAGKHIITTTRSHSNKLVTDCIAAMNPDNVLrVGGAGNKIIQLIEGK 247
Cdd:TIGR01331 130 --AAKREGDGQALKAPI-----------HVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRT-SGGSSLKFCLVAEGS 195
                         250       260
                  ....*....|....*....|....*...
gi 149040955  248 ASAYVFASPgCKKWDTCAPEVILHAVGG 275
Cdd:TIGR01331 196 ADIYPRLGP-TGEWDTAAGHAVLAAAGG 222
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
9-276 1.45e-19

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: 85.67  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   9 MRLVASAYSIAQKAGTIVRCVIAEGDLGIVQKtSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDlppGEVDQElie 88
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRELDLEVETK-GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGR--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  89 dgqseeilkqpcPSQYsaikeedlvVWV-DPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPyynyqnnekeklre 167
Cdd:COG0483   74 ------------DSGY---------VWViDPIDGTTNFVHG-LPLFAVSIALVRDGEPVAGVVYDP-------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 168 hrneakagpdaVLGRTIWGVLGLGAF--GFQLK---EAPAGKHIITTTRSH--SNKLVTDCIAAMNPD--NVLRVGGAGN 238
Cdd:COG0483  118 -----------ALGELFTAARGGGAFlnGRRLRvsaRTDLEDALVATGFPYlrDDREYLAALAALLPRvrRVRRLGSAAL 186
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 149040955 239 KIIQLIEGKASAYVfaSPGCKKWDTCAPEVILHAVGGL 276
Cdd:COG0483  187 DLAYVAAGRLDAFV--EAGLKPWDIAAGALIVREAGGV 222
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
18-276 1.62e-13

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: 67.42  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  18 IAQKAGTIVR-CVIAEGDLGIVQKTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLPPGEVdqeliedgqseeil 96
Cdd:cd01636    7 VAKEAGLAILkAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEV-------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  97 kqpcpsqysAIKEEDLVVWVDPVDGTKEYTEGlLDNVTVLIGIayegkaiaGIINQPYYnyqnnekeklrehrneakAGP 176
Cdd:cd01636   73 ---------MGRRDEYTWVIDPIDGTKNFING-LPFVAVVIAV--------YVILILAE------------------PSH 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 177 DAVLGRTIwgvlglgafgFQLKEAPAGkhiitttrshsnklvtdciaamnpdnVLRVGGAGNKIIQLIEGKASAYVFASP 256
Cdd:cd01636  117 KRVDEKKA----------ELQLLAVYR--------------------------IRIVGSAVAKMCLVALGLADIYYEPGG 160
                        250       260
                 ....*....|....*....|
gi 149040955 257 GCKKWDTCAPEVILHAVGGL 276
Cdd:cd01636  161 KRRAWDVAASAAIVREAGGI 180
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
9-165 4.36e-12

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: 65.03  E-value: 4.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   9 MRLVASAysIAQKAGTIVRCVIAE-GDLGIVQKTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDLppgevdqeli 87
Cdd:cd01517    1 ELEVAIL--AVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS---------- 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149040955  88 edgqseeilkqpcpsqysaiKEEDLVVWVDPVDGTKEYTEGLLdnVTVLIGIAYEGKAIAGIINQPYYNYQNNEKEKL 165
Cdd:cd01517   69 --------------------AALGRFWVLDPIDGTKGFLRGDQ--FAVALALIEDGEVVLGVIGCPNLPLDDGGGGDL 124
PLN02911 PLN02911
inositol-phosphate phosphatase
1-153 4.30e-10

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 59.35  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955   1 MASSHNVLMRLVASAYSIAQKAGTIVRC-------VIAEGDLGIVqktsatdlqTKADRMVQMSICSSLSRKFPKLTIIG 73
Cdd:PLN02911  26 SALSDAVLDRFVDVAHKLADAAGEVTRKyfrtkfeIIDKEDLSPV---------TIADRAAEEAMRSIILENFPSHAIFG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  74 EEDlppGEVdqelIEDGQSEeilkqpcpsqysaikeedlVVWV-DPVDGTKEYTEG--LLDnvtVLIGIAYEGKAIAGII 150
Cdd:PLN02911  97 EEH---GLR----CGEGSSD-------------------YVWVlDPIDGTKSFITGkpLFG---TLIALLYKGKPVLGII 147

                 ...
gi 149040955 151 NQP 153
Cdd:PLN02911 148 DQP 150
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
48-193 6.15e-10

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: 58.42  E-value: 6.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  48 TKADRMVQMSICSSLSRKFPKLTIIGEEdlppgevdqeliedgqseeilkqpcpsqYSAIKEEDLVVWV-DPVDGTKEYT 126
Cdd:cd01641   36 TEADRAAEAAMRELIAAAFPDHGILGEE----------------------------FGNEGGDAGYVWVlDPIDGTKSFI 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149040955 127 EGLlDNVTVLIGIAYEGKAIAGIINQPYynyqnnekeklrehrneakagpdavLGRTIWGVLGLGAF 193
Cdd:cd01641   88 RGL-PVWGTLIALLHDGRPVLGVIDQPA-------------------------LGERWIGARGGGTF 128
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
13-278 6.47e-08

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: 52.34  E-value: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  13 ASAYSIAQKAGTivRCVIAEGDLGIVQKTSATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEdlppgevdqeliedgqs 92
Cdd:cd01643    2 SLAEAIAQEAGD--RALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  93 eeilkqpcpsqYSAIKEEDLVVWV-DPVDGTKEYTEGlLDNVTVLIGIAYEGKAIAGIINQPyynyqnnekeklrehrne 171
Cdd:cd01643   63 -----------GGGIFPSSGWYWViDPIDGTTNFARG-IPIWAISIALLYRGEPVFGVIALP------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955 172 akagpdaVLGRTIWGVLGLGAF--GFQLKEAPAgkhiitTTRSHSNKLVTDCIAAMnPDNVLRVG--GAGNKIIQLieGK 247
Cdd:cd01643  113 -------ALNQTFVAFKGGGAFlnGKPLALHPP------LQLPDCNVGFNRSSRAS-ARAVLRVIlrRFPGKIRML--GS 176
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 149040955 248 AS---AYVFA-------SPGCKKWDTCAPEVILHAVGGLWL 278
Cdd:cd01643  177 ASlnlASVAAgqtlgyvEATPKIWDIAAAWVILREAGGSWT 217
PLN02737 PLN02737
inositol monophosphatase family protein
43-148 2.34e-03

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 39.01  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040955  43 ATDLQTKADRMVQMSICSSLSRKFPKLTIIGEEDlppgevdqELIEDGQSEeilkqpcpsqysaikeedlVVW-VDPVDG 121
Cdd:PLN02737 109 LTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG--------GVIGDSSSD-------------------YLWcIDPLDG 161
                         90       100
                 ....*....|....*....|....*..
gi 149040955 122 TKEYTEGlLDNVTVLIGIAYEGKAIAG 148
Cdd:PLN02737 162 TTNFAHG-YPSFAVSVGVLFRGTPAAA 187
 
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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