NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2108433429|gb|UCH90373|]
View 

MAG: diphthine--ammonia ligase [Thermoplasmata archaeon]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
6-221 1.01e-87

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member TIGR03679:

Pssm-ID: 469708  Cd Length: 218  Bit Score: 258.34  E-value: 1.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   6 GALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKTALK 85
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVPENEDSYMFHTPNIELTRLQAEALGIPLVEIETSGEKEKEVEDLKGALK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  86 AAmDQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRKFDL 165
Cdd:TIGR03679  81 EL-KEEGVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFIIVSVSAYGLDESWLGREIDE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2108433429 166 ETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEV 221
Cdd:TIGR03679 160 KYIEELKALNKRYGINPAGEGGEYETLVLDAPLFKRRIEIVEYEKKWSGGGGYLII 215
 
Name Accession Description Interval E-value
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
6-221 1.01e-87

arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; This protein consists of an N-terminal possible metal-binding domain (pfam04068) followed by a 4Fe-4S cluster binding domain (pfam00037) followed by a C-terminal ABC transporter, ATP-binding domain (pfam00005). This combination of N-terminal domains is observed in the RNase L inhibitor, RLI. This model has the same scope as an archaeal COG (arCOG00187) and is found in all completely sequenced archaea and does not recognize any known non-archaeal genes.


Pssm-ID: 188368  Cd Length: 218  Bit Score: 258.34  E-value: 1.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   6 GALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKTALK 85
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVPENEDSYMFHTPNIELTRLQAEALGIPLVEIETSGEKEKEVEDLKGALK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  86 AAmDQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRKFDL 165
Cdd:TIGR03679  81 EL-KEEGVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFIIVSVSAYGLDESWLGREIDE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2108433429 166 ETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEV 221
Cdd:TIGR03679 160 KYIEELKALNKRYGINPAGEGGEYETLVLDAPLFKRRIEIVEYEKKWSGGGGYLII 215
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
7-199 5.73e-82

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 243.49  E-value: 5.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   7 ALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKTALKA 86
Cdd:COG2102     3 VSWSGGKDSALALYRALQEGYEVVGLLTTVPEDFDRVMFHGPNLELLEAQAEALGIPLIEIELSGSNEEYEEELEEALKE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  87 AMDQyQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRKFDLE 166
Cdd:COG2102    83 LKAE-GIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAIIVCVDAEGLDESWLGRELDEE 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2108433429 167 TIDELCELH-NTCyvctgGEGGEFETLVLDAPFF 199
Cdd:COG2102   162 LLEELPAYGvDPC-----GEGGEFHTFVLDGPLF 190
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
7-199 2.41e-76

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 229.09  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   7 ALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKT-----------EGVKEE 75
Cdd:cd01994     4 ALISGGKDSIYALLHAIRNGHEVVALANLRPEDKDSYMFQTVGHELLELQAEALGLPLIRREIrgksvtqelgyEGEEED 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  76 ELEDLKTALKAAMDQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLG 155
Cdd:cd01994    84 EVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARIVKVAAMGLD 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2108433429 156 PEWLGRKFDLETIDELCELHNTCYVCTGGEGGEFETLVLDAPFF 199
Cdd:cd01994   164 EEWLGRRLDEDQPEELLKLNEKYGVHVCGEGGEYETLVLDGPLF 207
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
3-221 7.08e-69

Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.


Pssm-ID: 280139  Cd Length: 219  Bit Score: 210.43  E-value: 7.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   3 MRLGALFSGGKDSLLSLHRARSDgHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKT 82
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALKE-MEVDSLVCVMSENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGEEEKEVEDLKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  83 ALKaamdQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRK 162
Cdd:pfam01902  80 ILH----RLDVEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEAYVVAVKAEGLDESWLGRR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2108433429 163 FDLETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEV 221
Cdd:pfam01902 156 IDRKFIDELKKLNEKYGIHPAGEGGEFETLVLDGPIFKKRLEVKELEKYWGERYGHLGI 214
 
Name Accession Description Interval E-value
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
6-221 1.01e-87

arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; This protein consists of an N-terminal possible metal-binding domain (pfam04068) followed by a 4Fe-4S cluster binding domain (pfam00037) followed by a C-terminal ABC transporter, ATP-binding domain (pfam00005). This combination of N-terminal domains is observed in the RNase L inhibitor, RLI. This model has the same scope as an archaeal COG (arCOG00187) and is found in all completely sequenced archaea and does not recognize any known non-archaeal genes.


Pssm-ID: 188368  Cd Length: 218  Bit Score: 258.34  E-value: 1.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   6 GALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKTALK 85
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVPENEDSYMFHTPNIELTRLQAEALGIPLVEIETSGEKEKEVEDLKGALK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  86 AAmDQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRKFDL 165
Cdd:TIGR03679  81 EL-KEEGVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFIIVSVSAYGLDESWLGREIDE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2108433429 166 ETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEV 221
Cdd:TIGR03679 160 KYIEELKALNKRYGINPAGEGGEYETLVLDAPLFKRRIEIVEYEKKWSGGGGYLII 215
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
7-199 5.73e-82

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 243.49  E-value: 5.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   7 ALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKTALKA 86
Cdd:COG2102     3 VSWSGGKDSALALYRALQEGYEVVGLLTTVPEDFDRVMFHGPNLELLEAQAEALGIPLIEIELSGSNEEYEEELEEALKE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  87 AMDQyQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRKFDLE 166
Cdd:COG2102    83 LKAE-GIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAIIVCVDAEGLDESWLGRELDEE 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2108433429 167 TIDELCELH-NTCyvctgGEGGEFETLVLDAPFF 199
Cdd:COG2102   162 LLEELPAYGvDPC-----GEGGEFHTFVLDGPLF 190
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
7-199 2.41e-76

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 229.09  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   7 ALFSGGKDSLLSLHRARSDGHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKT-----------EGVKEE 75
Cdd:cd01994     4 ALISGGKDSIYALLHAIRNGHEVVALANLRPEDKDSYMFQTVGHELLELQAEALGLPLIRREIrgksvtqelgyEGEEED 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  76 ELEDLKTALKAAMDQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLG 155
Cdd:cd01994    84 EVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARIVKVAAMGLD 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2108433429 156 PEWLGRKFDLETIDELCELHNTCYVCTGGEGGEFETLVLDAPFF 199
Cdd:cd01994   164 EEWLGRRLDEDQPEELLKLNEKYGVHVCGEGGEYETLVLDGPLF 207
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
3-229 1.39e-72

MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.


Pssm-ID: 273000  Cd Length: 223  Bit Score: 220.04  E-value: 1.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   3 MRLGALFSGGKDSLLSLHRARSDgHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKT 82
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVNIMPENEESYMFHGVNAHLTDLQAESIGIPLIKLYTEGTEEDEVEELKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  83 ALKaamdQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRK 162
Cdd:TIGR00290  80 ILH----TLDVEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEARIIAVAAEGLDESWLGRR 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108433429 163 FDLETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEVLKTDLVPK 229
Cdd:TIGR00290 156 IDRKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIFKKRLEVKEIEKYWDGRNGHLGIKRAALVSK 222
TIGR00289 TIGR00289
TIGR00289 family protein; Homologous proteins related to MJ0570 of Methanococcus jannaschii ...
3-229 3.45e-70

TIGR00289 family protein; Homologous proteins related to MJ0570 of Methanococcus jannaschii include both the apparent orthologs found by this model above the trusted cutoff, the much longer protein YLR143W from Saccharomyces cerevisiae, and second homologous proteins from Archaeoglobus fulgidus and Pyrococcus horikoshii that appear to represent a second orthologous group. [Hypothetical proteins, Conserved]


Pssm-ID: 129390  Cd Length: 222  Bit Score: 213.96  E-value: 3.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   3 MRLGALFSGGKDSLLSLHRARSDgHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKT 82
Cdd:TIGR00289   1 MKVAVLYSGGKDSILALYKALEE-HEVISLVGVFSENEESYMFHSPNLHLTDLVAEAVGIPLIKLYTSGEEEKEVEDLAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  83 ALKaamdQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPrDMLTEMIGEGFEVIISAVAAGGLGPEWLGRK 162
Cdd:TIGR00289  80 QLG----ELDVEALCIGAIESNYQKSRIDKVCRELGLKSIAPLWHADP-EKLMYEVAEKFEVIIVSVSAMGLDESWLGRR 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108433429 163 FDLETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEVLKTDLVPK 229
Cdd:TIGR00289 155 IDKECIDDLKRLNEKYGIHLAFEGGEAETLVLDAPLFKKRIEVDEIEKFWDGVRGYCLIKRASLVDK 221
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
3-221 7.08e-69

Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.


Pssm-ID: 280139  Cd Length: 219  Bit Score: 210.43  E-value: 7.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429   3 MRLGALFSGGKDSLLSLHRARSDgHEVAVLISIVSSNPESYMFHVPNIVLTEMQAKAMELPIIIQKTEGVKEEELEDLKT 82
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALKE-MEVDSLVCVMSENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGEEEKEVEDLKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433429  83 ALKaamdQYQIEGIVSGAIYSNYQRSRIDKLAGELGLQSLSPLWKARPRDMLTEMIGEGFEVIISAVAAGGLGPEWLGRK 162
Cdd:pfam01902  80 ILH----RLDVEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEAYVVAVKAEGLDESWLGRR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2108433429 163 FDLETIDELCELHNTCYVCTGGEGGEFETLVLDAPFFKKKLVVKKSEKKWDGQAGTFEV 221
Cdd:pfam01902 156 IDRKFIDELKKLNEKYGIHPAGEGGEFETLVLDGPIFKKRLEVKELEKYWGERYGHLGI 214
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH