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Conserved domains on  [gi|446332879|ref|WP_000410734|]
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four-carbon acid sugar kinase family protein [Escherichia coli]

Protein Classification

four-carbon acid sugar kinase family protein( domain architecture ID 11465537)

four-carbon acid sugar kinase family protein similar to Haemophilus influenzae 3-oxo-tetronate kinase OtnK, which catalyzes the ATP-dependent phosphorylation of 3-oxo-tetronate to form 3-oxo-tetronate 4-phosphate and to Salmonella enterica D-threonate kinase which catalyzes the ATP-dependent phosphorylation of D-threonate to D-threonate 4-phosphate

EC:  2.7.1.-
Gene Ontology:  GO:0005524|GO:0016301
PubMed:  27402745

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OtnK COG3395
D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family ...
10-408 3.66e-127

D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442622 [Multi-domain]  Cd Length: 415  Bit Score: 373.00  E-value: 3.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  10 ILIVADDFTGANDAGVSLAQVGHTVDVAFEMP---YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLpLANNPPLVIKK 86
Cdd:COG3395    2 LGVIADDFTGATDVAVQLARAGLRTVLLLGVPtlaLADDADAVVIATKSRSLPPEEAVARVREALAWL-KAAGARLVYKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  87 IDSTLRGNIGAEIEALMKACGITGAVVAPAFPQAGRTTVAGECWVNGVRITETEFASDPKTPVLSARIADIIRLQTAIPC 166
Cdd:COG3395   81 FDSTLRGNIGAETDALLDALGADAAVVVPAFPENGRTTVGGHLFVGGVPLHETEMARDPVTPMTESDLPRLLAEQTKGPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 167 QPVTVSQ-----------LSHLSYEQPWIGVIDAQTDSDLDRIAAAVMQAKQPLLLVGSAGICDAVARRSAIMPPPT--V 233
Cdd:COG3395  161 GLVDLADvragaealraaLAALAAEGARIVVVDAVTDADLDAIAEALADLAERVLVVGSSGLAAALAAAPAALPPAGgpV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 234 LAIIGSMSEIAQRQIATLHSHPRITQIYVDVEHILAGNASDYDARIV----QALQKGDHCIVHTCNDSVARHQIDTlcqr 309
Cdd:COG3395  241 LVVVGSCSPVTRRQLAALLAEPGVPVVELDVERLLDGEAEAEVERALawalAALAAGRTVLIYTSRDPEDVADAQE---- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 310 wQMSRAALGEKICRFLGELTRQVLLCAMPDALYLSGGDVAMATASALGATGFRITGKVAQCVPYGHFLGGVWSR-SVMTK 388
Cdd:COG3395  317 -RLGRLAAGERIEAALAEIARRLLEEAGVRRLIVAGGDTSGAVLKALGIRGLRILGEIAPGVPLGRAIGGDFDGlPVVLK 395
                        410       420
                 ....*....|....*....|
gi 446332879 389 AGGFGDETTLHQVLNFIEEK 408
Cdd:COG3395  396 GGNFGDEDFFARALEGLEGK 415
 
Name Accession Description Interval E-value
OtnK COG3395
D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family ...
10-408 3.66e-127

D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate transport and metabolism];


Pssm-ID: 442622 [Multi-domain]  Cd Length: 415  Bit Score: 373.00  E-value: 3.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  10 ILIVADDFTGANDAGVSLAQVGHTVDVAFEMP---YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLpLANNPPLVIKK 86
Cdd:COG3395    2 LGVIADDFTGATDVAVQLARAGLRTVLLLGVPtlaLADDADAVVIATKSRSLPPEEAVARVREALAWL-KAAGARLVYKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  87 IDSTLRGNIGAEIEALMKACGITGAVVAPAFPQAGRTTVAGECWVNGVRITETEFASDPKTPVLSARIADIIRLQTAIPC 166
Cdd:COG3395   81 FDSTLRGNIGAETDALLDALGADAAVVVPAFPENGRTTVGGHLFVGGVPLHETEMARDPVTPMTESDLPRLLAEQTKGPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 167 QPVTVSQ-----------LSHLSYEQPWIGVIDAQTDSDLDRIAAAVMQAKQPLLLVGSAGICDAVARRSAIMPPPT--V 233
Cdd:COG3395  161 GLVDLADvragaealraaLAALAAEGARIVVVDAVTDADLDAIAEALADLAERVLVVGSSGLAAALAAAPAALPPAGgpV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 234 LAIIGSMSEIAQRQIATLHSHPRITQIYVDVEHILAGNASDYDARIV----QALQKGDHCIVHTCNDSVARHQIDTlcqr 309
Cdd:COG3395  241 LVVVGSCSPVTRRQLAALLAEPGVPVVELDVERLLDGEAEAEVERALawalAALAAGRTVLIYTSRDPEDVADAQE---- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 310 wQMSRAALGEKICRFLGELTRQVLLCAMPDALYLSGGDVAMATASALGATGFRITGKVAQCVPYGHFLGGVWSR-SVMTK 388
Cdd:COG3395  317 -RLGRLAAGERIEAALAEIARRLLEEAGVRRLIVAGGDTSGAVLKALGIRGLRILGEIAPGVPLGRAIGGDFDGlPVVLK 395
                        410       420
                 ....*....|....*....|
gi 446332879 389 AGGFGDETTLHQVLNFIEEK 408
Cdd:COG3395  396 GGNFGDEDFFARALEGLEGK 415
SBD_N pfam07005
Sugar-binding N-terminal domain; This is the N-terminal domain found in proteins in a range of ...
10-217 1.35e-60

Sugar-binding N-terminal domain; This is the N-terminal domain found in proteins in a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. Structural analysis of the whole protein indicates the N- and C-termini act together to produce a surface into which a threonate-ADP complex is bound, demonstrating that a sugar binding site is on the N-terminal domain, and a nucleotide binding site is in the C-terminal domain. There is a critical motif, DDXTG, at approximately residues 22-25. Proteins containing this domain have been predicted as kinases. Some members are associated with PdxA2 by physical clustering and gene fusion with PdxA2. Some members that are fused with PdxA2 have been shown to be involved in L-4-hydroxythreonine (4HT) phosphorylation, part of the alternative pathway to make PLP (pyridoxal 5'-phosphate) out of a toxic metabolite, 4HT. However, 4HT phosphorylation might not be the main function of this group of proteins. Moreover, some members that are not associated with pdxA2, and even one that is associated with pdxA2, have lost 4HT kinase activity. Functional analysis demonstrate that family members include D-Threonate kinases (DtnK), D-Erythronate kinases (DenK) and 3-Oxo-tetronate kinases (OtnK).


Pssm-ID: 462065  Cd Length: 229  Bit Score: 195.84  E-value: 1.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   10 ILIVADDFTGANDAGVSLAQVGHTVDVAFEMP---YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLpLANNPPLVIK- 85
Cdd:pfam07005   1 LGVIADDFTGAQDVGVQLAKHGLRTLVFLGVPdaaRLPDADAVVIATNSRSLPPEEAVARVREALKWL-AALGARLYYKv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   86 --KIDSTLRGNIGAEIEALMKACG-ITGAVVAPAFPQAGRTTVAGECWVNGVRITETEFASDPKTPVLSARIADIIRLQT 162
Cdd:pfam07005  80 csRFDSTLRGNIGAETDALLDALGaFDAAVVAPAFPEGGRTTIGGVLFVNGVPLAETEFARDPVTPMTESDLRRLLAEQT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446332879  163 AIPCQPVTVSQLS-----------HLSYEQPWIGVIDAQTDSDLDRIAAAVMQAKQPLLLVGSAGI 217
Cdd:pfam07005 160 KLPVGLIDLDTLAdgpealrealaALLAQGVRVVVVDAVTDEDLAVIAEALLALGKRFLLVGSAGL 225
PLN02858 PLN02858
fructose-bisphosphate aldolase
10-287 1.56e-07

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 53.70  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   10 ILIVADDF-TGAndagvslaQVGHTVDVAFEMP-------YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLPLA---- 77
Cdd:PLN02858  658 TLVVLDDDpTGT--------QTVHDVEVLTEWSvesiseqFRKKPACFFILTNSRSLSPEKASELIKDICRNLCAAaksv 729
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   78 -NNPPLVIKKIDSTLRGNIGAEIEALMKACGITGA-VVAPAFPQAGRTTVAGECWV-NGVRIT---ETEFASDPKTPVLS 151
Cdd:PLN02858  730 gNVDYTIVLRGDSTLRGHFPEEADAAVSVLGEMDAwIICPFFLQGGRYTINDIHYVaDSDRLVpagETEFAKDASFGYKS 809
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  152 ARIADIIRLQTA--IPCQPVTVSQLSHLSYEQP-------------WIGVIDAQTDSDLDRIAAAVMQA--KQPLLLVGS 214
Cdd:PLN02858  810 SNLREWVEEKTKgrISANSVQSISIQLLRKGGPdavcehlcslkkgSTCIVNAASERDMAVFAAGMIQAelKGKRFLCRT 889
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  215 AGicDAVARRSAIMPPPTV--------------LAIIGSMSEIAQRQIATLHSH--PRITQIYVDVEHILAGNASDYDAR 278
Cdd:PLN02858  890 AA--SFVSARIGIIPKPPVlpkdlesnkessggLIVVGSYVPKTTKQVEELKSQcgQSLRSIEVSVEKVAMKSSEVRDEE 967

                  ....*....
gi 446332879  279 IVQALQKGD 287
Cdd:PLN02858  968 ISRAVEMAD 976
 
Name Accession Description Interval E-value
OtnK COG3395
D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family ...
10-408 3.66e-127

D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate transport and metabolism];


Pssm-ID: 442622 [Multi-domain]  Cd Length: 415  Bit Score: 373.00  E-value: 3.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  10 ILIVADDFTGANDAGVSLAQVGHTVDVAFEMP---YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLpLANNPPLVIKK 86
Cdd:COG3395    2 LGVIADDFTGATDVAVQLARAGLRTVLLLGVPtlaLADDADAVVIATKSRSLPPEEAVARVREALAWL-KAAGARLVYKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  87 IDSTLRGNIGAEIEALMKACGITGAVVAPAFPQAGRTTVAGECWVNGVRITETEFASDPKTPVLSARIADIIRLQTAIPC 166
Cdd:COG3395   81 FDSTLRGNIGAETDALLDALGADAAVVVPAFPENGRTTVGGHLFVGGVPLHETEMARDPVTPMTESDLPRLLAEQTKGPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 167 QPVTVSQ-----------LSHLSYEQPWIGVIDAQTDSDLDRIAAAVMQAKQPLLLVGSAGICDAVARRSAIMPPPT--V 233
Cdd:COG3395  161 GLVDLADvragaealraaLAALAAEGARIVVVDAVTDADLDAIAEALADLAERVLVVGSSGLAAALAAAPAALPPAGgpV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 234 LAIIGSMSEIAQRQIATLHSHPRITQIYVDVEHILAGNASDYDARIV----QALQKGDHCIVHTCNDSVARHQIDTlcqr 309
Cdd:COG3395  241 LVVVGSCSPVTRRQLAALLAEPGVPVVELDVERLLDGEAEAEVERALawalAALAAGRTVLIYTSRDPEDVADAQE---- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879 310 wQMSRAALGEKICRFLGELTRQVLLCAMPDALYLSGGDVAMATASALGATGFRITGKVAQCVPYGHFLGGVWSR-SVMTK 388
Cdd:COG3395  317 -RLGRLAAGERIEAALAEIARRLLEEAGVRRLIVAGGDTSGAVLKALGIRGLRILGEIAPGVPLGRAIGGDFDGlPVVLK 395
                        410       420
                 ....*....|....*....|
gi 446332879 389 AGGFGDETTLHQVLNFIEEK 408
Cdd:COG3395  396 GGNFGDEDFFARALEGLEGK 415
SBD_N pfam07005
Sugar-binding N-terminal domain; This is the N-terminal domain found in proteins in a range of ...
10-217 1.35e-60

Sugar-binding N-terminal domain; This is the N-terminal domain found in proteins in a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. Structural analysis of the whole protein indicates the N- and C-termini act together to produce a surface into which a threonate-ADP complex is bound, demonstrating that a sugar binding site is on the N-terminal domain, and a nucleotide binding site is in the C-terminal domain. There is a critical motif, DDXTG, at approximately residues 22-25. Proteins containing this domain have been predicted as kinases. Some members are associated with PdxA2 by physical clustering and gene fusion with PdxA2. Some members that are fused with PdxA2 have been shown to be involved in L-4-hydroxythreonine (4HT) phosphorylation, part of the alternative pathway to make PLP (pyridoxal 5'-phosphate) out of a toxic metabolite, 4HT. However, 4HT phosphorylation might not be the main function of this group of proteins. Moreover, some members that are not associated with pdxA2, and even one that is associated with pdxA2, have lost 4HT kinase activity. Functional analysis demonstrate that family members include D-Threonate kinases (DtnK), D-Erythronate kinases (DenK) and 3-Oxo-tetronate kinases (OtnK).


Pssm-ID: 462065  Cd Length: 229  Bit Score: 195.84  E-value: 1.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   10 ILIVADDFTGANDAGVSLAQVGHTVDVAFEMP---YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLpLANNPPLVIK- 85
Cdd:pfam07005   1 LGVIADDFTGAQDVGVQLAKHGLRTLVFLGVPdaaRLPDADAVVIATNSRSLPPEEAVARVREALKWL-AALGARLYYKv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   86 --KIDSTLRGNIGAEIEALMKACG-ITGAVVAPAFPQAGRTTVAGECWVNGVRITETEFASDPKTPVLSARIADIIRLQT 162
Cdd:pfam07005  80 csRFDSTLRGNIGAETDALLDALGaFDAAVVAPAFPEGGRTTIGGVLFVNGVPLAETEFARDPVTPMTESDLRRLLAEQT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446332879  163 AIPCQPVTVSQLS-----------HLSYEQPWIGVIDAQTDSDLDRIAAAVMQAKQPLLLVGSAGI 217
Cdd:pfam07005 160 KLPVGLIDLDTLAdgpealrealaALLAQGVRVVVVDAVTDEDLAVIAEALLALGKRFLLVGSAGL 225
NBD_C pfam17042
Nucleotide-binding C-terminal domain; This is the C-terminal domain found in proteins in a ...
234-398 6.95e-32

Nucleotide-binding C-terminal domain; This is the C-terminal domain found in proteins in a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. Structural analysis of the whole protein indicates the N- and C-termini act together to produce a surface into which a threonate-ADP complex is bound, demonstrating that a sugar binding site is on the N-terminal domain, and a nucleotide binding site is in the C-terminal domain. There is a critical motif, DDXTG, at approximately residues 22-25. Proteins containing this domain have been predicted as kinases. Some members are associated with PdxA2 by physical clustering and gene fusion with PdxA2. Some members that are fused with PdxA2 have been shown to be involved in L-4-hydroxythreonine (4HT) phosphorylation, part of the alternative pathway to make PLP (pyridoxal 5'-phosphate) out of a toxic metabolite, 4HT. However, 4HT phosphorylation might not be the main function of this group of proteins. Moreover, some members that are not associated with pdxA2, and even one that is associated with pdxA2, have lost 4HT kinase activity. Functional analysis demonstrate that family members include D-Threonate kinases (DtnK), D-Erythronate kinases (DenK) and 3-Oxo-tetronate kinases (OtnK).


Pssm-ID: 465337  Cd Length: 166  Bit Score: 118.83  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  234 LAIIGSMSEIAQRQIATLHSHPRITQIYVDVEHILAGNASDYD-----ARIVQALQKGDHCIVHTCNDSVARHQIDTLCQ 308
Cdd:pfam17042   1 LVVVGSCSPKTTAQLAALLAERGVVVVELDVEALLDEEAREEEieralAEALAALASGKDVVVYTSRGPEDVAALDSLQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  309 RWQMSRAalGEKICRFLGELTRQvLLCAMPDALYLSGGDVAMATASALGATGFRITGKVAQCVPYGHFLG--GVWsrsVM 386
Cdd:pfam17042  81 ALGLSRA--GARISAALAEIARG-LLARGVRGLVVAGGDTSGAVLKALGIRGLRVLGEIAPGVPLGRLIGapGLP---VV 154
                         170
                  ....*....|..
gi 446332879  387 TKAGGFGDETTL 398
Cdd:pfam17042 155 LKGGNFGDEDAL 166
PLN02858 PLN02858
fructose-bisphosphate aldolase
10-287 1.56e-07

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 53.70  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   10 ILIVADDF-TGAndagvslaQVGHTVDVAFEMP-------YRGDASVWVINSDSRAMDPKLAAMKITSLMSHLPLA---- 77
Cdd:PLN02858  658 TLVVLDDDpTGT--------QTVHDVEVLTEWSvesiseqFRKKPACFFILTNSRSLSPEKASELIKDICRNLCAAaksv 729
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879   78 -NNPPLVIKKIDSTLRGNIGAEIEALMKACGITGA-VVAPAFPQAGRTTVAGECWV-NGVRIT---ETEFASDPKTPVLS 151
Cdd:PLN02858  730 gNVDYTIVLRGDSTLRGHFPEEADAAVSVLGEMDAwIICPFFLQGGRYTINDIHYVaDSDRLVpagETEFAKDASFGYKS 809
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  152 ARIADIIRLQTA--IPCQPVTVSQLSHLSYEQP-------------WIGVIDAQTDSDLDRIAAAVMQA--KQPLLLVGS 214
Cdd:PLN02858  810 SNLREWVEEKTKgrISANSVQSISIQLLRKGGPdavcehlcslkkgSTCIVNAASERDMAVFAAGMIQAelKGKRFLCRT 889
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332879  215 AGicDAVARRSAIMPPPTV--------------LAIIGSMSEIAQRQIATLHSH--PRITQIYVDVEHILAGNASDYDAR 278
Cdd:PLN02858  890 AA--SFVSARIGIIPKPPVlpkdlesnkessggLIVVGSYVPKTTKQVEELKSQcgQSLRSIEVSVEKVAMKSSEVRDEE 967

                  ....*....
gi 446332879  279 IVQALQKGD 287
Cdd:PLN02858  968 ISRAVEMAD 976
 
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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