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Conserved domains on  [gi|6320454|ref|NP_010534|]
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gluconokinase [Saccharomyces cerevisiae S288C]

Protein Classification

nucleoside/nucleotide kinase family protein; thymidylate kinase( domain architecture ID 10796813)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars| thymidylate kinase with a major facilitator superfamily (MFS) transporter domain may function in the phosphorylation of thymidine monophosphate and the transport across cytoplasmic or internal membranes of various substrates including sugar phosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 14-186 1.01e-89

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


:

Pssm-ID: 273551  Cd Length: 163  Bit Score: 260.03  E-value: 1.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     14 IVLAGTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEhlS 93
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLG-----AKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKV--G 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     94 IVACSSLKKKYRDLIRhtCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDInDETDCDIVPLDFKT 173
Cdd:TIGR01313  74 IITCSALKRHYRDILR--EAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLA-DETDVLRVDIDQPL 150

                         170
                  ....*....|...
gi 6320454    174 FYQIEKDVIQVVK 186
Cdd:TIGR01313 151 EGVEEDCIAVVLK 163
 
Name Accession Description Interval E-value
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 14-186 1.01e-89

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 260.03  E-value: 1.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     14 IVLAGTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEhlS 93
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLG-----AKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKV--G 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     94 IVACSSLKKKYRDLIRhtCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDInDETDCDIVPLDFKT 173
Cdd:TIGR01313  74 IITCSALKRHYRDILR--EAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLA-DETDVLRVDIDQPL 150

                         170
                  ....*....|...
gi 6320454    174 FYQIEKDVIQVVK 186
Cdd:TIGR01313 151 EGVEEDCIAVVLK 163
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 13-171 8.76e-68

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 203.64  E-value: 8.76e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454   13 VIVLAGTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEHL 92
Cdd:cd02021   1 IIVVMGVSGSGKSTVGKALAERLG-----APFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLASAGEGV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320454   93 sIVACSSLKKKYRDLIRHTCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPdinDETDCDIVPLDF 171
Cdd:cd02021  76 -VVACSALKRIYRDILRGGAANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPP---GEDEEDVIVIDV 150
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 12-170 2.58e-60

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 185.33  E-value: 2.58e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454   12 KVIVLAGTAGTGKSTIAGELIHEFkdiypDLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAAstKEH 91
Cdd:COG3265   2 MVIVVMGVSGSGKSTVGQALAERL-----GWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLA--AGE 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320454   92 LSIVACSSLKKKYRDLIRHTCPesEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDIndetDCDIVPLD 170
Cdd:COG3265  75 GAVLACSALKRSYRDRLREGNP--DVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGP----DEDAIVVD 147
gntK PRK11545
gluconokinase;
18-187 4.91e-39

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 131.38  E-value: 4.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454    18 GTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKkvAVESTKAAASTKEHLSIVAC 97
Cdd:PRK11545   2 GVSGSGKSAVASEVAHQLH-----AAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQ--ALNDAAFAMQRTNKVSLIVC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454    98 SSLKKKYRDLIRHTCPesEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDiNDETDCDIV----PLDfkt 173
Cdd:PRK11545  75 SALKKHYRDLLREGNP--NLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPG-ADETDVLVVdidqPLE--- 148

                        170
                 ....*....|....
gi 6320454   174 fyQIEKDVIQVVKS 187
Cdd:PRK11545 149 --GVVASTIEVIKK 160
AAA_18 pfam13238
AAA domain;
14-142 6.37e-05

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     14 IVLAGTAGTGKSTIAGEL--IHEFKDIYPDLKF---IEGDDLHPPANVEKMtrgiplnDDDRWDWLKKvavESTKAAAST 88
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELskRLGFGDNVRDLALengLVLGDDPETRESKRL-------DEDKLDRLLD---LLEENAALE 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6320454     89 KEHLSIV-ACSSLKKKYRDLIRhtcpesefHFIFLYASKIEVLKRLKTRKGHFMK 142
Cdd:pfam13238  71 EGGNLIIdGHLAELEPERAKDL--------VGIVLRASPEELLERLEKRGYEEAK 117
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 10-51 2.27e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 2.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 6320454      10 KFKVIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDDLH 51
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL 42
 
Name Accession Description Interval E-value
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 14-186 1.01e-89

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 260.03  E-value: 1.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     14 IVLAGTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEhlS 93
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLG-----AKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKV--G 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     94 IVACSSLKKKYRDLIRhtCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDInDETDCDIVPLDFKT 173
Cdd:TIGR01313  74 IITCSALKRHYRDILR--EAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLA-DETDVLRVDIDQPL 150

                         170
                  ....*....|...
gi 6320454    174 FYQIEKDVIQVVK 186
Cdd:TIGR01313 151 EGVEEDCIAVVLK 163
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 13-171 8.76e-68

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 203.64  E-value: 8.76e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454   13 VIVLAGTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEHL 92
Cdd:cd02021   1 IIVVMGVSGSGKSTVGKALAERLG-----APFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLASAGEGV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320454   93 sIVACSSLKKKYRDLIRHTCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPdinDETDCDIVPLDF 171
Cdd:cd02021  76 -VVACSALKRIYRDILRGGAANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPP---GEDEEDVIVIDV 150
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 12-170 2.58e-60

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 185.33  E-value: 2.58e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454   12 KVIVLAGTAGTGKSTIAGELIHEFkdiypDLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAAstKEH 91
Cdd:COG3265   2 MVIVVMGVSGSGKSTVGQALAERL-----GWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLA--AGE 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320454   92 LSIVACSSLKKKYRDLIRHTCPesEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDIndetDCDIVPLD 170
Cdd:COG3265  75 GAVLACSALKRSYRDRLREGNP--DVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGP----DEDAIVVD 147
gntK PRK11545
gluconokinase;
18-187 4.91e-39

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 131.38  E-value: 4.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454    18 GTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKkvAVESTKAAASTKEHLSIVAC 97
Cdd:PRK11545   2 GVSGSGKSAVASEVAHQLH-----AAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQ--ALNDAAFAMQRTNKVSLIVC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454    98 SSLKKKYRDLIRHTCPesEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDiNDETDCDIV----PLDfkt 173
Cdd:PRK11545  75 SALKKHYRDLLREGNP--NLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPG-ADETDVLVVdidqPLE--- 148

                        170
                 ....*....|....
gi 6320454   174 fyQIEKDVIQVVKS 187
Cdd:PRK11545 149 --GVVASTIEVIKK 160
idnK PRK09825
gluconokinase;
15-170 1.16e-37

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 128.22  E-value: 1.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454    15 VLAGTAGTGKSTIAGELIHEFKdiypdLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKvaVESTKAAASTKEHLSI 94
Cdd:PRK09825   7 ILMGVSGSGKSLIGSKIAALFS-----AKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLER--LNDASYSLYKKNETGF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320454    95 VACSSLKKKYRDLIRHTCPesEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDINDEtdcDIVPLD 170
Cdd:PRK09825  80 IVCSSLKKQYRDILRKSSP--NVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEH---DIARID 150
AAA_18 pfam13238
AAA domain;
14-142 6.37e-05

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     14 IVLAGTAGTGKSTIAGEL--IHEFKDIYPDLKF---IEGDDLHPPANVEKMtrgiplnDDDRWDWLKKvavESTKAAAST 88
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELskRLGFGDNVRDLALengLVLGDDPETRESKRL-------DEDKLDRLLD---LLEENAALE 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6320454     89 KEHLSIV-ACSSLKKKYRDLIRhtcpesefHFIFLYASKIEVLKRLKTRKGHFMK 142
Cdd:pfam13238  71 EGGNLIIdGHLAELEPERAKDL--------VGIVLRASPEELLERLEKRGYEEAK 117
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 13-143 3.98e-04

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 39.00  E-value: 3.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454   13 VIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDdlhppaNV-EKMTRGIPLNDDDRWDWLKK---VAVESTKAAAst 88
Cdd:cd02027   1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGD------NVrHGLNKDLGFSREDREENIRRiaeVAKLLADAGL-- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6320454   89 kehLSIVACSSLKKKYRDLIRHTCPESEFHFIFLYASkIEVLKRlKTRKGHFMKA 143
Cdd:cd02027  73 ---IVIAAFISPYREDREAARKIIGGGDFLEVFVDTP-LEVCEQ-RDPKGLYKKA 122
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 10-51 2.27e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 2.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 6320454      10 KFKVIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDDLH 51
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL 42
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 13-50 4.44e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 36.19  E-value: 4.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 6320454    13 VIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDDL 50
Cdd:PRK05541   9 VIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDEL 46
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 13-121 4.45e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 36.14  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320454     13 VIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDdlhppaNVE-KMTRGIPLNDDDRWDWLKKVAVESTKAAASTkeH 91
Cdd:pfam01583   4 TIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGD------NVRhGLNKDLGFSEEDRTENIRRIGEVAKLFADAG--L 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 6320454     92 LSIVACSSLKKKYRDLIRHTCPESEFHFIF 121
Cdd:pfam01583  76 IVITAFISPYREDREQARELHEEGKFIEVF 105
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 8-31 8.15e-03

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 35.69  E-value: 8.15e-03
                        10        20
                ....*....|....*....|....
gi 6320454    8 MGKFKVIVLAGTAGTGKSTIAGEL 31
Cdd:COG2074   3 MKRPRIILIGGASGVGKSTIAAEL 26
 
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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