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Conserved domains on  [gi|767997684|ref|XP_011523961|]
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inositol monophosphatase 2 isoform X1 [Homo sapiens]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108155)

inositol monophosphatase family protein such as inositol monophosphatase, which catalyzes the hydrolysis of several inositol monophosphates and the artificial substrate p-nitrophenyl-phosphate to inorganic phosphate and inositol

CATH:  3.40.190.80
EC:  3.1.3.-
Gene Ontology:  GO:0008934|GO:0006020|GO:0046872
PubMed:  7890024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 62-249 1.26e-89

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: 265.94  E-value: 1.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEEaaaSGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRL 141
Cdd:cd01639   61 FLGEE---SGAAGGLTDEPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 142 RVSGETDLSKALVLTEIGPKRdPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATV 221
Cdd:cd01639  138 RVSGRKELKDALVATGFPYDR-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGAL 216

                        170       180
                 ....*....|....*....|....*...
gi 767997684 222 IIREAGGIVIDTSGGPLDLMACRVVAAS 249
Cdd:cd01639  217 IVREAGGLVTDFDGGPFDLMSGNILAGN 244
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 62-249 1.26e-89

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: 265.94  E-value: 1.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEEaaaSGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRL 141
Cdd:cd01639   61 FLGEE---SGAAGGLTDEPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 142 RVSGETDLSKALVLTEIGPKRdPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATV 221
Cdd:cd01639  138 RVSGRKELKDALVATGFPYDR-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGAL 216

                        170       180
                 ....*....|....*....|....*...
gi 767997684 222 IIREAGGIVIDTSGGPLDLMACRVVAAS 249
Cdd:cd01639  217 IVREAGGLVTDFDGGPFDLMSGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
61-264 1.85e-78

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 238.40  E-value: 1.85e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684   61 RFIAEEAAASGAKCVLTHS-PTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQ 139
Cdd:pfam00459  65 KIIGEEGGAKGDQTELTDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQ 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  140 RLRVSGETDLSKALVLTEIGPKRDPATL-KLFLSNMERLLHakAHGVRVIGSSTLALCHLASGAADAYYQFG-LHCWDLA 217
Cdd:pfam00459 145 PLPVSRAPPLSEALLVTLFGVSSRKDTSeASFLAKLLKLVR--APGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHA 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767997684  218 AATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTI 264
Cdd:pfam00459 223 AGVAILREAGGVVTDADGGPFDLLAGRVIAANPKVLHELLAAALEEI 269
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 61-265 2.99e-65

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: 204.31  E-value: 2.99e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  61 RFIAEEAAASGAKcvlTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQR 140
Cdd:COG0483   61 GILGEESGASEGR---DSGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 141 LRVSGETDLSKALVLTEIGPKRDPATlklFLSNMERLLhAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAAT 220
Cdd:COG0483  138 LRVSARTDLEDALVATGFPYLRDDRE---YLAALAALL-PRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGA 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767997684 221 VIIREAGGIVIDTSGGPLDLMACRVVAASTRemamLIAQALQTIN 265
Cdd:COG0483  214 LIVREAGGVVTDLDGEPLDLGSGSLVAANPA----LHDELLALLR 254
PLN02553 PLN02553
inositol-phosphate phosphatase
 62-249 1.58e-64

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 203.00  E-value: 1.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEE-AAASGAKcVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQR 140
Cdd:PLN02553  68 FIGEEtTAASGGT-ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 141 LRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLhAKAHGVRVIGSSTLALCHLASGAADAYYQFGL-HCWDLAAA 219
Cdd:PLN02553 147 IKASSQSELGKALLATEVGTKRDKATVDATTNRINALL-YKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAG 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 767997684 220 TVIIREAGGIVIDTSGGPLDLMACRVVAAS 249
Cdd:PLN02553 226 AVIVKEAGGLVFDPSGGPFDIMSRRVAASN 255
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 81-262 3.73e-23

histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273949 [Multi-domain]  Cd Length: 251  Bit Score: 94.68  E-value: 3.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684   81 TWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEigp 160
Cdd:TIGR02067  76 VWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTT--- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  161 krDPATL--KLFLSNMERLlhAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPL 238
Cdd:TIGR02067 153 --SPDLLddPGNRPAFERL--RRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA 228

                         170       180
                  ....*....|....*....|....
gi 767997684  239 dLMACRVVAASTREMAMLIAQALQ 262
Cdd:TIGR02067 229 -PDGGGAVAAGNAMLHDEALEILN 251
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 62-249 1.26e-89

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: 265.94  E-value: 1.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEEaaaSGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRL 141
Cdd:cd01639   61 FLGEE---SGAAGGLTDEPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 142 RVSGETDLSKALVLTEIGPKRdPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATV 221
Cdd:cd01639  138 RVSGRKELKDALVATGFPYDR-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGAL 216

                        170       180
                 ....*....|....*....|....*...
gi 767997684 222 IIREAGGIVIDTSGGPLDLMACRVVAAS 249
Cdd:cd01639  217 IVREAGGLVTDFDGGPFDLMSGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
61-264 1.85e-78

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 238.40  E-value: 1.85e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684   61 RFIAEEAAASGAKCVLTHS-PTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQ 139
Cdd:pfam00459  65 KIIGEEGGAKGDQTELTDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQ 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  140 RLRVSGETDLSKALVLTEIGPKRDPATL-KLFLSNMERLLHakAHGVRVIGSSTLALCHLASGAADAYYQFG-LHCWDLA 217
Cdd:pfam00459 145 PLPVSRAPPLSEALLVTLFGVSSRKDTSeASFLAKLLKLVR--APGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHA 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767997684  218 AATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTI 264
Cdd:pfam00459 223 AGVAILREAGGVVTDADGGPFDLLAGRVIAANPKVLHELLAAALEEI 269
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 61-265 2.99e-65

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: 204.31  E-value: 2.99e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  61 RFIAEEAAASGAKcvlTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQR 140
Cdd:COG0483   61 GILGEESGASEGR---DSGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 141 LRVSGETDLSKALVLTEIGPKRDPATlklFLSNMERLLhAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAAT 220
Cdd:COG0483  138 LRVSARTDLEDALVATGFPYLRDDRE---YLAALAALL-PRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGA 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767997684 221 VIIREAGGIVIDTSGGPLDLMACRVVAASTRemamLIAQALQTIN 265
Cdd:COG0483  214 LIVREAGGVVTDLDGEPLDLGSGSLVAANPA----LHDELLALLR 254
PLN02553 PLN02553
inositol-phosphate phosphatase
 62-249 1.58e-64

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 203.00  E-value: 1.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEE-AAASGAKcVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQR 140
Cdd:PLN02553  68 FIGEEtTAASGGT-ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 141 LRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLhAKAHGVRVIGSSTLALCHLASGAADAYYQFGL-HCWDLAAA 219
Cdd:PLN02553 147 IKASSQSELGKALLATEVGTKRDKATVDATTNRINALL-YKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAG 225

                        170       180       190
                 ....*....|....*....|....*....|
gi 767997684 220 TVIIREAGGIVIDTSGGPLDLMACRVVAAS 249
Cdd:PLN02553 226 AVIVKEAGGLVFDPSGGPFDIMSRRVAASN 255
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 61-249 8.01e-60

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: 189.83  E-value: 8.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  61 RFIAEEAAASGAkcVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQR 140
Cdd:cd01637   58 GILGEEGGGSGN--VSDGGRVWVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 141 LRVSGETDLSKALVLTEIGPKRDPATLKLflsnmeRLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAAT 220
Cdd:cd01637  136 LPLSKDTPLNDALLSTNASMLRSNRAAVL------ASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGA 209

                        170       180
                 ....*....|....*....|....*....
gi 767997684 221 VIIREAGGIVIDTSGGPLDLMACRVVAAS 249
Cdd:cd01637  210 LIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
PLN02737 PLN02737
inositol monophosphatase family protein
 82-237 6.49e-35

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 128.76  E-value: 6.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  82 WIIDPIDGTCNFVHRFPTVAVSIGFAVRQE------LEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVL 155
Cdd:PLN02737 154 WCIDPLDGTTNFAHGYPSFAVSVGVLFRGTpaaatvVEFVGGPMCWNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLV 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 156 TEIGPKRD---PATLKLFLSNMERllhakAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVID 232
Cdd:PLN02737 234 TGFGYEHDdawATNIELFKEFTDV-----SRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTR 308


                 ....*
gi 767997684 233 TSGGP 237
Cdd:PLN02737 309 MDGGK 313
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
59-240 6.28e-34

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 123.48  E-value: 6.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  59 CRRFIAEEAAasgakCVLTHSPTW--IIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFC 136
Cdd:PRK12676  64 CVNIISEELG-----EIVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 137 NGQRLRVSGETDLsKALVLTEIGPKRDPATLKLFLSNMERllhakahgVRVIGSSTLALCHLASGAADAYYQFG--LHCW 214
Cdd:PRK12676 139 NGKPIKVSKTSEL-NESAVSIYGYRRGKERTVKLGRKVRR--------VRILGAIALELCYVASGRLDAFVDVRnyLRVT 209

                        170       180
                 ....*....|....*....|....*.
gi 767997684 215 DLAAATVIIREAGGIVIDTSGGPLDL 240
Cdd:PRK12676 210 DIAAGKLICEEAGGIVTDEDGNELKL 235
PRK10757 PRK10757
inositol-1-monophosphatase;
82-258 1.50e-33

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 122.99  E-value: 1.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  82 WIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPK 161
Cdd:PRK10757  81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 162 RDPATLKLFlsNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLM 241
Cdd:PRK10757 161 AKQHATTYI--NIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYML 238

                        170
                 ....*....|....*..
gi 767997684 242 ACRVVAASTREMAMLIA 258
Cdd:PRK10757 239 TGNIVAGNPRVVKAMLA 255
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 63-239 2.45e-31

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 116.80  E-value: 2.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  63 IAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFC-----N 137
Cdd:COG1218   63 LSEESAAIPYEERKSWDRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggE 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 138 GQRLRVSGETDLSKALVLteiGPK--RDPATLKLflsnMERLlhaKAHGVRVIGSStLALCHLASGAADAYYQFGLHC-W 214
Cdd:COG1218  143 RQPIRVRDRPPAEPLRVV---ASRshRDEETEAL----LARL---GVAELVSVGSS-LKFCLVAEGEADLYPRLGPTMeW 211

                        170       180
                 ....*....|....*....|....*
gi 767997684 215 DLAAATVIIREAGGIVIDTSGGPLD 239
Cdd:COG1218  212 DTAAGQAILEAAGGRVTDLDGKPLR 236
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 63-238 2.50e-31

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 116.17  E-value: 2.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  63 IAEEAAASGAkcVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLR 142
Cdd:cd01638   60 LSEESADDPL--RLGWDRFWLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 143 VSGETDLSKALVLTEIGPK--RDPATLKLFLSnmerllhAKAHGVRVIGSStLALCHLASGAADAYYQFGLHC-WDLAAA 219
Cdd:cd01638  138 VSLQARPPPLQPLRVVASRshPDEELEALLAA-------LGVAEVVSIGSS-LKFCLVAEGEADIYPRLGPTMeWDTAAG 209

                        170
                 ....*....|....*....
gi 767997684 220 TVIIREAGGIVIDTSGGPL 238
Cdd:cd01638  210 DAVLRAAGGAVSDLDGSPL 228
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 81-231 1.24e-30

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: 114.35  E-value: 1.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  81 TWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGqrlrvsgetdlsKALVLTEIGP 160
Cdd:cd01643   73 YWVIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNG------------KPLALHPPLQ 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767997684 161 KRDPATLKLF---LSNMERLLHAKAH---GVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVI 231
Cdd:cd01643  141 LPDCNVGFNRssrASARAVLRVILRRfpgKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWT 217
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 81-240 3.17e-30

Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.


Pssm-ID: 238773 [Multi-domain]  Cd Length: 257  Bit Score: 113.63  E-value: 3.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  81 TWIIDPIDGTCNFVHRFPTVAVSIGFAVRQE--LEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEI 158
Cdd:cd01515   78 TVVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 159 GPKRDPATLKLFlSNMERllhakahgVRVIGSSTLALCHLASGAADAYYQF--GLHCWDLAAATVIIREAGGIVIDTSGG 236
Cdd:cd01515  158 YGKNHDRTFKIC-RKVRR--------VRIFGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGK 228


                 ....
gi 767997684 237 PLDL 240
Cdd:cd01515  229 ELKL 232
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 62-252 2.25e-26

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: 103.49  E-value: 2.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEEAAASGakcvlTHSP-TWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYH-CTEERLYtGRRGRGAFCN-- 137
Cdd:cd01641   59 ILGEEFGNEG-----GDAGyVWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQpALGERWI-GARGGGTFLNga 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 138 -GQRLRVSGETDLSKALVLTEiGPKRDPATLKlflSNMERLlhAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDL 216
Cdd:cd01641  133 gGRPLRVRACADLAEAVLSTT-DPHFFTPGDR---AAFERL--ARAVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDV 206

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767997684 217 AAATVIIREAGGIVIDTSGGPLDLMACRVVAASTRE 252
Cdd:cd01641  207 AALIPIIEGAGGVITDWDGGPLTGGSGRVVAAGDAE 242
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 81-262 3.73e-23

histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273949 [Multi-domain]  Cd Length: 251  Bit Score: 94.68  E-value: 3.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684   81 TWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEigp 160
Cdd:TIGR02067  76 VWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTT--- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  161 krDPATL--KLFLSNMERLlhAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPL 238
Cdd:TIGR02067 153 --SPDLLddPGNRPAFERL--RRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA 228

                         170       180
                  ....*....|....*....|....
gi 767997684  239 dLMACRVVAASTREMAMLIAQALQ 262
Cdd:TIGR02067 229 -PDGGGAVAAGNAMLHDEALEILN 251
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 62-232 7.21e-23

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: 92.46  E-value: 7.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAvrqelefgviyhcteerlytgrrgrgafcngqrl 141
Cdd:cd01636   61 IVGEESGVAEEVMGRRDEYTWVIDPIDGTKNFINGLPFVAVVIAVY---------------------------------- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 142 rvsgetdlsKALVLTEIGPKRDPatlklflSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFG--LHCWDLAAA 219
Cdd:cd01636  107 ---------VILILAEPSHKRVD-------EKKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGgkRRAWDVAAS 170

                        170
                 ....*....|...
gi 767997684 220 TVIIREAGGIVID 232
Cdd:cd01636  171 AAIVREAGGIMTD 183
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 63-239 2.32e-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: 92.51  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684   63 IAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAF--CNGQR 140
Cdd:TIGR01331  60 LSEEDASIPLTPRQTWQRFWLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  141 LRVS---GETDLSKALVLteIGPKRDPATLKLFLSNMERLLHakahgvrVIGSSTLALCHLASGAADAYYQFG-LHCWDL 216
Cdd:TIGR01331 140 LKAPihvRPWPSGPLLVV--ISRSHAEEKTTEYLANLGYDLR-------TSGGSSLKFCLVAEGSADIYPRLGpTGEWDT 210

                         170       180
                  ....*....|....*....|...
gi 767997684  217 AAATVIIREAGGIVIDTSGGPLD 239
Cdd:TIGR01331 211 AAGHAVLAAAGGAIFDLDGSPLL 233
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
63-240 2.13e-21

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 93.25  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  63 IAEEAaasGAKCVLTHSPTWI--IDPIDGTCNFVHRFPTVAVSIGFAVR-----------------QELEFGVIYHCTEE 123
Cdd:PRK14076  66 ISEEI---GFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIAIAKIdgfdkkikefigknltiNDLEVGVVKNIATG 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 124 RLYTGRRGRGAF----CNGQRLRVSGETDLSKAlvlteigpkrdpaTLKLF---LSN--MERLLHAKAHGVRVIGSSTLA 194
Cdd:PRK14076 143 DTYYAEKGEGAYllkkGEKKKIEISNISNLKDA-------------SIGLFaygLSLdtLKFIKDRKVRRIRLFGSIALE 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767997684 195 LCHLASGAADAYYQF--GLHCWDLAAATVIIREAGGIVIDTSGGPLDL 240
Cdd:PRK14076 210 MCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPLNM 257
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 62-240 5.56e-20

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 86.60  E-value: 5.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  62 FIAEEAAAsgakcvlTHSPTWIIDPIDGTCNFVhRFPTVAVSIGFAVRQELEFGVIYHC-------TEERLYTGRRGRGA 134
Cdd:cd01517   62 IVGEEDSA-------ALGRFWVLDPIDGTKGFL-RGDQFAVALALIEDGEVVLGVIGCPnlplddgGGGDLFSAVRGQGA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 135 FCNGQR---LRVSGETDLSKALVLTEIGPkRDPATLKLFLSNMERLLHAKAHGVRVigSSTLALCHLASGAADAYYQFGL 211
Cdd:cd01517  134 WLRPLDgssLQPLSVRQLTNAARASFCES-VESAHSSHRLQAAIKALGGTPQPVRL--DSQAKYAAVARGAADFYLRLPL 210

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767997684 212 HC------WDLAAATVIIREAGGIVIDTSGGPLDL 240
Cdd:cd01517  211 SMsyrekiWDHAAGVLIVEEAGGKVTDADGKPLDF 245
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 82-239 1.65e-10

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 59.71  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  82 WIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRgAF--CNGQRLRVsGETDLSKALVLteIG 159
Cdd:PRK10931  80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI-QVRDARPPLVV--IS 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 160 PKRDPATLKLFLSnmerllHAKAHGVRVIGSStLALCHLASGAADAYYQFG-LHCWDLAAATVIIREAGGIVIDTSGGPL 238
Cdd:PRK10931 156 RSHADAELKEYLQ------QLGEHQTTSIGSS-LKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHDWQGKTL 228


                 .
gi 767997684 239 D 239
Cdd:PRK10931 229 D 229
PLN02911 PLN02911
inositol-phosphate phosphatase
 81-264 9.62e-10

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 57.81  E-value: 9.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684  81 TWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHC-TEERlYTGRRGRGAFCNGQRLRVSGETDLSKALVLTeig 159
Cdd:PLN02911 111 VWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPvLKER-WVGVAGRATTLNGEEISTRSCASLKDAYLYT--- 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997684 160 pkrdpATLKLFLSNMERLLHAKAHGVRV--IGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGP 237
Cdd:PLN02911 187 -----TSPHMFSGDAEDAFARVRDKVKVplYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRK 261

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767997684 238 LDLMACR--------VVAASTREmamLIAQALQTI 264
Cdd:PLN02911 262 LRWEPSPgslatsfnVVAAGDAR---LHKQALDIL 293
 
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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