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Conserved domains on  [gi|2195004471|ref|NP_001388537|]
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nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 isoform 6 [Homo sapiens]

Protein Classification

nucleotidyl transferase family protein( domain architecture ID 117)

nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 7-115 2.16e-72

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


The actual alignment was detected with superfamily member cd09286:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 225  Bit Score: 217.17  E-value: 2.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471   7 VVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESE 86
Cdd:cd09286     1 VVLLACGSFNPITNMHLRMFELARDHLHETGRYEVVGGIISPVNDAYGKKGLASAKHRVAMCRLAVQSSDWIRVDDWESL 80

                          90       100
                  ....*....|....*....|....*....
gi 2195004471  87 QAQWMETVKVLRHHHSKLLRSPPQMEGPD 115
Cdd:cd09286    81 QPEWMRTAKVLRHHREEINNKYGGIEGAA 109
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 7-115 2.16e-72

Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs.


Pssm-ID: 185681 [Multi-domain]  Cd Length: 225  Bit Score: 217.17  E-value: 2.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471   7 VVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESE 86
Cdd:cd09286     1 VVLLACGSFNPITNMHLRMFELARDHLHETGRYEVVGGIISPVNDAYGKKGLASAKHRVAMCRLAVQSSDWIRVDDWESL 80

                          90       100
                  ....*....|....*....|....*....
gi 2195004471  87 QAQWMETVKVLRHHHSKLLRSPPQMEGPD 115
Cdd:cd09286    81 QPEWMRTAKVLRHHREEINNKYGGIEGAA 109
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 1-114 1.82e-41

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 138.67  E-value: 1.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471   1 MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGmYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRV 80
Cdd:PLN02945   17 TGPRTRVVLVATGSFNPPTYMHLRMFELARDALMSEG-YHVLGGYMSPVNDAYKKKGLASAEHRIQMCQLACEDSDFIMV 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2195004471  81 DPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGP 114
Cdd:PLN02945   96 DPWEARQSTYQRTLTVLARVETSLNNNGLASEES 129
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 10-104 4.57e-35

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 121.27  E-value: 4.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  10 LACGSFNPITNMHLRMFEVARDHLHQTgMYQVIQGIISPVNDTYGKkdlAASHHRVAMARLALQTSDWIRVDPWESEQAQ 89
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLD-KVIFVPTANPPHKKTYEA---ASSHHRLAMLKLAIEDNPKFEVDDFEIKRGG 76

                          90
                  ....*....|....*
gi 2195004471  90 WMETVKVLRHHHSKL 104
Cdd:TIGR00482  77 PSYTIDTLKHLKKKY 91
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 10-87 8.08e-17

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 72.35  E-value: 8.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2195004471  10 LACGSFNPITNMHLRMFEVARDHLHQTgmyqVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQ 87
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED----LIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR 74
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 13-101 1.47e-08

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 51.66  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  13 GSFNPITNMHLRMFEVARDHLhqtGMYQViqgIISPVNDTYGK--KDLAASHHRVAMARLALQTSDWIRVDPWESEQAQ- 89
Cdd:COG1057     9 GTFDPIHIGHLALAEEAAEQL---GLDEV---IFVPAGQPPHKkhKPLASAEHRLAMLRLAIADNPRFEVSDIELERPGp 82

                          90
                  ....*....|....
gi 2195004471  90 -WM-ETVKVLRHHH 101
Cdd:COG1057    83 sYTiDTLRELREEY 96
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 7-115 2.16e-72

Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs.


Pssm-ID: 185681 [Multi-domain]  Cd Length: 225  Bit Score: 217.17  E-value: 2.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471   7 VVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESE 86
Cdd:cd09286     1 VVLLACGSFNPITNMHLRMFELARDHLHETGRYEVVGGIISPVNDAYGKKGLASAKHRVAMCRLAVQSSDWIRVDDWESL 80

                          90       100
                  ....*....|....*....|....*....
gi 2195004471  87 QAQWMETVKVLRHHHSKLLRSPPQMEGPD 115
Cdd:cd09286    81 QPEWMRTAKVLRHHREEINNKYGGIEGAA 109
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 1-114 1.82e-41

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 138.67  E-value: 1.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471   1 MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGmYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRV 80
Cdd:PLN02945   17 TGPRTRVVLVATGSFNPPTYMHLRMFELARDALMSEG-YHVLGGYMSPVNDAYKKKGLASAEHRIQMCQLACEDSDFIMV 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2195004471  81 DPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGP 114
Cdd:PLN02945   96 DPWEARQSTYQRTLTVLARVETSLNNNGLASEES 129
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 10-104 4.57e-35

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 121.27  E-value: 4.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  10 LACGSFNPITNMHLRMFEVARDHLHQTgMYQVIQGIISPVNDTYGKkdlAASHHRVAMARLALQTSDWIRVDPWESEQAQ 89
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLD-KVIFVPTANPPHKKTYEA---ASSHHRLAMLKLAIEDNPKFEVDDFEIKRGG 76

                          90
                  ....*....|....*
gi 2195004471  90 WMETVKVLRHHHSKL 104
Cdd:TIGR00482  77 PSYTIDTLKHLKKKY 91
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 8-109 1.80e-18

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 77.10  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471   8 VLLACGSFNPITNMHLRMFEVARDHLhqtgmyqVIQGIISPVNDTYGK---KDLAASHHRVAMARLALQtsDWIRVDPWE 84
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEEA-------LDEVIIIIVSNPPKKkrnKDPFSLHERVEMLKEILK--DRLKVVPVD 71

                          90       100
                  ....*....|....*....|....*
gi 2195004471  85 SEQAQWMETVKVlrhHHSKLLRSPP 109
Cdd:cd02039    72 FPEVKILLAVVF---ILKILLKVGP 93
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 10-87 8.08e-17

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 72.35  E-value: 8.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2195004471  10 LACGSFNPITNMHLRMFEVARDHLHQTgmyqVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQ 87
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED----LIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR 74
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
13-101 7.69e-09

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 52.53  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  13 GSFNPITNMHLRMFEVARDHLHQTgmyQVIQgIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQA--QW 90
Cdd:PRK00071   11 GTFDPPHYGHLAIAEEAAERLGLD---EVWF-LPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELERPgpSY 86

                          90
                  ....*....|..
gi 2195004471  91 M-ETVKVLRHHH 101
Cdd:PRK00071   87 TiDTLRELRARY 98
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 13-101 1.47e-08

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 51.66  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  13 GSFNPITNMHLRMFEVARDHLhqtGMYQViqgIISPVNDTYGK--KDLAASHHRVAMARLALQTSDWIRVDPWESEQAQ- 89
Cdd:COG1057     9 GTFDPIHIGHLALAEEAAEQL---GLDEV---IFVPAGQPPHKkhKPLASAEHRLAMLRLAIADNPRFEVSDIELERPGp 82

                          90
                  ....*....|....
gi 2195004471  90 -WM-ETVKVLRHHH 101
Cdd:COG1057    83 sYTiDTLRELREEY 96
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 13-99 9.22e-07

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 46.47  E-value: 9.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  13 GSFNPITNMHLRMFEVARDHLHQTgmyQVIqgIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWME 92
Cdd:cd02165     6 GSFDPPHLGHLAIAEEALEELGLD---RVL--LLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80


                  ....*..
gi 2195004471  93 TVKVLRH 99
Cdd:cd02165    81 TIDTLEE 87
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 13-85 2.27e-04

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 39.56  E-value: 2.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2195004471  13 GSFNPITNMHLRMFEVARdhlhqtGMY-QVIQGI-ISPvndtyGKKDLAASHHRVAMARLALQTSDWIRVDPWES 85
Cdd:TIGR01510   6 GSFDPVTNGHLDIIKRAA------ALFdEVIVAVaKNP-----SKKPLFSLEERVELIKDATKHLPNVRVDVFDG 69
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 13-85 6.86e-03

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 35.13  E-value: 6.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2195004471  13 GSFNPITNMHLRMFEVArdhlhqTGMY-QVIQGI-ISPvndtyGKKDLAASHHRVAMARLALQTSDWIRVDPWES 85
Cdd:cd02163     6 GSFDPITNGHLDIIERA------SKLFdEVIVAVaVNP-----SKKPLFSLEERVELIREATKHLPNVEVDGFDG 69
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
12-103 7.07e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 36.08  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004471  12 CGSFNPITNMHLRMFEVARDHLHQTGMYqVIQGIISPVNDtygKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWM 91
Cdd:PRK07152    7 GGSFDPIHKGHINIAKKAIKKLKLDKLF-FVPTYINPFKK---KQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQNVS 82

                          90
                  ....*....|..
gi 2195004471  92 ETVKVLRHHHSK 103
Cdd:PRK07152   83 YTIDTIKYFKKK 94
 
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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