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Conserved domains on  [gi|767990392|ref|XP_011521577|]
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terminal nucleotidyltransferase 4B isoform X1 [Homo sapiens]

Protein Classification

nucleotidyltransferase domain-containing protein( domain architecture ID 1001423)

nucleotidyltransferase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
200-472 5.45e-65

DNA polymerase sigma [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG5260:

Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 223.11  E-value: 5.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 200 LHEEISDFYEYMSPRPEEEKMRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVF----GKWENLPLWTLE 275
Cdd:COG5260   57 LTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLALPKSDIDLCIIsdprGYKETRNAGSLA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 276 EALRKHKVADEdsVKVLDKATVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDFTKKYPVLPYLVLVLKQFLLQRDLNE 355
Cdd:COG5260  137 SHLFKKNLAKE--VVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALND 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 356 VFTGGIGSYSLFLMAVSFLQLHPR-----------EDACIPNTNYGVLLIEFFELYGRHFNYLKTGIRIKDGGSYVAKDE 424
Cdd:COG5260  215 VATGTLSSYTISCMVLSFLQMHPPflffdngllspLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYE 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 767990392 425 vqKNMLDGYRPSMLYIEDP-LQPGNDVGRSSYGAMQVKQAFDYAYVVLS 472
Cdd:COG5260  295 --KGWLKPSKPNSLSIQDPgTDRNNDISAVSFNIKDIKAAFIRAFELLS 341
 
Name Accession Description Interval E-value
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
200-472 5.45e-65

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 223.11  E-value: 5.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 200 LHEEISDFYEYMSPRPEEEKMRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVF----GKWENLPLWTLE 275
Cdd:COG5260   57 LTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLALPKSDIDLCIIsdprGYKETRNAGSLA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 276 EALRKHKVADEdsVKVLDKATVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDFTKKYPVLPYLVLVLKQFLLQRDLNE 355
Cdd:COG5260  137 SHLFKKNLAKE--VVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALND 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 356 VFTGGIGSYSLFLMAVSFLQLHPR-----------EDACIPNTNYGVLLIEFFELYGRHFNYLKTGIRIKDGGSYVAKDE 424
Cdd:COG5260  215 VATGTLSSYTISCMVLSFLQMHPPflffdngllspLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYE 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 767990392 425 vqKNMLDGYRPSMLYIEDP-LQPGNDVGRSSYGAMQVKQAFDYAYVVLS 472
Cdd:COG5260  295 --KGWLKPSKPNSLSIQDPgTDRNNDISAVSFNIKDIKAAFIRAFELLS 341
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 220-330 2.54e-38

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 137.69  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 220 MRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVFG----KWENLPLWTLEEALRKHKVADEdsVKVLDKA 295
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGpnhrVDREDFLRKLAKLLKKSGEVVE--VEPIINA 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767990392 296 TVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDF 330
Cdd:cd05402   79 RVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAY 113
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 388-448 2.25e-17

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 76.46  E-value: 2.25e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990392  388 NYGVLLIEFFELYGRHFNYLKTGIRIKDGGsYVAKDEVQKNMLDGYRPSMLYIEDPLQPGN 448
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGG-ILSKKEKGWLRNEGRRPFLLCIEDPFDLDN 60
PRK13300 PRK13300
CCA tRNA nucleotidyltransferase;
208-348 4.54e-04

CCA tRNA nucleotidyltransferase;


Pssm-ID: 237340 [Multi-domain]  Cd Length: 447  Bit Score: 43.34  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 208 YEYMSPRPEEEKMRMEVVN----RIESVIKELWPSADVQIFGSFKTGLYLP-TSDIDLVVFgkwenLPLWTLEEALRK-- 280
Cdd:PRK13300   7 LERIKPTEEEREKLKKVAEelieRLEEAIKELGLDAEVELVGSTARGTWLSgDRDIDIFVL-----FPKDTSREELEEkg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 281 ----HKVADEDSVKVLDK-ATVPIIKLTdsFTEVKVDI--SFNVQNGVR---AAD--------LIKDFTKKypvLPYLVL 342
Cdd:PRK13300  82 leigKEVAKELLGDYEERyAEHPYVTGE--IDGFEVDIvpCYKVESGEEiisAVDrtpfhtkyVKERLKGK---LEDEVR 156


                 ....*.
gi 767990392 343 VLKQFL 348
Cdd:PRK13300 157 LLKQFL 162
 
Name Accession Description Interval E-value
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
200-472 5.45e-65

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 223.11  E-value: 5.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 200 LHEEISDFYEYMSPRPEEEKMRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVF----GKWENLPLWTLE 275
Cdd:COG5260   57 LTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLALPKSDIDLCIIsdprGYKETRNAGSLA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 276 EALRKHKVADEdsVKVLDKATVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDFTKKYPVLPYLVLVLKQFLLQRDLNE 355
Cdd:COG5260  137 SHLFKKNLAKE--VVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALND 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 356 VFTGGIGSYSLFLMAVSFLQLHPR-----------EDACIPNTNYGVLLIEFFELYGRHFNYLKTGIRIKDGGSYVAKDE 424
Cdd:COG5260  215 VATGTLSSYTISCMVLSFLQMHPPflffdngllspLKYNKNIDNLGVLFDDFFELYGKSFNYSLVVLSINSGDFYLPKYE 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 767990392 425 vqKNMLDGYRPSMLYIEDP-LQPGNDVGRSSYGAMQVKQAFDYAYVVLS 472
Cdd:COG5260  295 --KGWLKPSKPNSLSIQDPgTDRNNDISAVSFNIKDIKAAFIRAFELLS 341
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 220-330 2.54e-38

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 137.69  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 220 MRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVFG----KWENLPLWTLEEALRKHKVADEdsVKVLDKA 295
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGpnhrVDREDFLRKLAKLLKKSGEVVE--VEPIINA 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767990392 296 TVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDF 330
Cdd:cd05402   79 RVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAY 113
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 388-448 2.25e-17

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 76.46  E-value: 2.25e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990392  388 NYGVLLIEFFELYGRHFNYLKTGIRIKDGGsYVAKDEVQKNMLDGYRPSMLYIEDPLQPGN 448
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGG-ILSKKEKGWLRNEGRRPFLLCIEDPFDLDN 60
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 225-337 6.38e-12

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 62.05  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392  225 VNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVFGkwenlplwtleealrkhkvaDEDSVKVLDKATVPIIKLTD 304
Cdd:pfam01909   1 LRKLREILKELFPVAEVVLFGSYARGTALPGSDIDLLVVF--------------------PEPVEEERLLKLAKIIKELE 60

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767990392  305 SFTEVKVDISFNvqNGVRAADLIKDFTKKYPVL 337
Cdd:pfam01909  61 ELLGLEVDLVTR--EKIEFPLVKIDILEERILL 91
PAP_central pfam04928
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural ...
 215-315 3.72e-04

Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural similarity with the allosteric activity domain of ribonucleotide reductase R1, which comprises a four-helix bundle and a three-stranded mixed beta- sheet. Even though the two enzymes bind ATP, the ATP-recognition motifs are different.


Pssm-ID: 461486 [Multi-domain]  Cd Length: 344  Bit Score: 43.27  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392  215 PEEEKMRMEVVNRIESVIKEL-----------WPSADVQI-----FGSFKTGLYLPTSDID-LVVFGK---WENLPLwTL 274
Cdd:pfam04928  35 EEETQKREEVLGKLNKLVKEFvkrvskekglpESVAKEAGgkiftFGSYRLGVHGPGSDIDtLCVVPKhvtREDFFT-SF 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767990392  275 EEALRKHKVADEDSVkVLDkATVPIIKLtdSFTEVKVDISF 315
Cdd:pfam04928 114 LEMLRERPEVTELTA-VPD-AFVPVIKF--KFSGISIDLLF 150
PRK13300 PRK13300
CCA tRNA nucleotidyltransferase;
208-348 4.54e-04

CCA tRNA nucleotidyltransferase;


Pssm-ID: 237340 [Multi-domain]  Cd Length: 447  Bit Score: 43.34  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 208 YEYMSPRPEEEKMRMEVVN----RIESVIKELWPSADVQIFGSFKTGLYLP-TSDIDLVVFgkwenLPLWTLEEALRK-- 280
Cdd:PRK13300   7 LERIKPTEEEREKLKKVAEelieRLEEAIKELGLDAEVELVGSTARGTWLSgDRDIDIFVL-----FPKDTSREELEEkg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 281 ----HKVADEDSVKVLDK-ATVPIIKLTdsFTEVKVDI--SFNVQNGVR---AAD--------LIKDFTKKypvLPYLVL 342
Cdd:PRK13300  82 leigKEVAKELLGDYEERyAEHPYVTGE--IDGFEVDIvpCYKVESGEEiisAVDrtpfhtkyVKERLKGK---LEDEVR 156


                 ....*.
gi 767990392 343 VLKQFL 348
Cdd:PRK13300 157 LLKQFL 162
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
 222-299 1.98e-03

Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.


Pssm-ID: 143393  Cd Length: 93  Bit Score: 37.78  E-value: 1.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990392 222 MEVVNRIESVIKELWPS-ADVQIFGSFKTGLYLPTSDIDLVVFGKwENLPLWTLEEALRKHKVADEDSVKVLDKATVPI 299
Cdd:cd05403    1 EEILEEILEILRELLGGvEKVYLFGSYARGDARPDSDIDLLVIFD-DPLDPLELARLLEELELLLGRPVDLVVLNALEL 78
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 216-313 3.49e-03

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this family.


Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 38.53  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990392 216 EEEKMRMEVVNRIESVIKEL-WPSADVQIFGSFKTGLYL-PTSDIDLVVF---------GKWENLpLWTLEEALRKHKVA 284
Cdd:cd05400    4 EAKERYREIREALKESLSELaGRVAEVFLQGSYARGTALrGDSDIDLVVVlpddtsfaeYGPAEL-LDELGEALKEYYGA 82

                         90       100
                 ....*....|....*....|....*....
gi 767990392 285 DEDsvkvlDKATVPIIKLTDSFTEVKVDI 313
Cdd:cd05400   83 NEE-----VKAQHRSVTVKFKGQGFHVDV 106
MJ0435 COG1669
Predicted nucleotidyltransferase MJ0435 [General function prediction only];
221-291 4.99e-03

Predicted nucleotidyltransferase MJ0435 [General function prediction only];


Pssm-ID: 441275  Cd Length: 96  Bit Score: 36.82  E-value: 4.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990392 221 RMEVVNRIESVIKELWPSADVQ---IFGSFKTGLYLPTSDIDLVVFGKwENLPLWTLEEAlrKHKVADEDSVKV 291
Cdd:COG1669    3 REEILEILREVIEELAERYGVSrlgLFGSVARGEAREDSDIDLLVEFD-EPTSLFDLFEL--EEELEELLGRKV 73
 
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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