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Conserved domains on  [gi|1301392469|gb|PKB60392|]
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MAG: pantetheine-phosphate adenylyltransferase [SAR202 cluster bacterium Ae2-Chloro-G1]

Protein Classification

pantetheine-phosphate adenylyltransferase( domain architecture ID 10786277)

pantetheine-phosphate adenylyltransferase catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway

CATH:  3.40.50.620
EC:  2.7.7.3
Gene Ontology:  GO:0005524|GO:0015937|GO:0004595
PubMed:  33271445

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-158 3.12e-86

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440433  Cd Length: 159  Bit Score: 249.53  E-value: 3.12e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   1 MVTAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREV 80
Cdd:COG0669     1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392469  81 GAAVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNAKFG 158
Cdd:COG0669    81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFA 158
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-158 3.12e-86

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 249.53  E-value: 3.12e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   1 MVTAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREV 80
Cdd:COG0669     1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392469  81 GAAVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNAKFG 158
Cdd:COG0669    81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFA 158
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-155 3.45e-78

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: 228.89  E-value: 3.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   3 TAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREVGA 82
Cdd:cd02163     1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1301392469  83 AVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNA 155
Cdd:cd02163    81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-157 1.53e-65

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: 197.11  E-value: 1.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   3 TAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREVGA 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469  83 AVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNAKF 157
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-134 1.79e-25

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: 94.69  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   5 IYPGSFDPVTMGHLDITTRGSALF-ERVIVAVYSTPS----KDLLFSTDERVELFqESIVDLPNVEVMRFSGLVVRFARE 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFdEDLIVGVPSDEPphklKRPLFSAEERLEML-ELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469  80 VGAAVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEV 134
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-66 3.02e-03

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 36.45  E-value: 3.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469   12 PVTMGHLDITTRGSALFERVIVAVYSTPSKdlLFSTDERVELFQESIVDLPNVEV 66
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSEDAS--LFSFDERFALVKKGTKDLDNVTV 62
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-158 3.12e-86

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 249.53  E-value: 3.12e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   1 MVTAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREV 80
Cdd:COG0669     1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392469  81 GAAVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNAKFG 158
Cdd:COG0669    81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFA 158
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-155 3.45e-78

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: 228.89  E-value: 3.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   3 TAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREVGA 82
Cdd:cd02163     1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1301392469  83 AVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNA 155
Cdd:cd02163    81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-157 1.53e-65

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: 197.11  E-value: 1.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   3 TAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTPSKDLLFSTDERVELFQESIVDLPNVEVMRFSGLVVRFAREVGA 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469  83 AVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEVARLGGDVTGMVPPHVVKAVNAKF 157
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-134 1.79e-25

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: 94.69  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   5 IYPGSFDPVTMGHLDITTRGSALF-ERVIVAVYSTPS----KDLLFSTDERVELFqESIVDLPNVEVMRFSGLVVRFARE 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFdEDLIVGVPSDEPphklKRPLFSAEERLEML-ELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469  80 VGAAVILRGLRSGADFEYEYDMAFMNRRLERSVDMVSFMTSQDYMFVSSSLLKEV 134
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-63 3.23e-11

cytidyltransferase-like domain; 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. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 55.78  E-value: 3.23e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469   4 AIYPGSFDPVTMGHLDITTRGSALFERVIVAVYST----PSKDL-LFSTDERVELFQESIVDLPN 63
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDqfvnPLKGEpVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-133 1.08e-07

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: 48.21  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   4 AIYPGSFDPVTMGHLDITTRG-SALFERVIVAVYS-TPSKDL---LFSTDERVELFQESIVDLPNVEVMRFSG----LVV 74
Cdd:cd02039     2 GIIIGRFEPFHLGHLKLIKEAlEEALDEVIIIIVSnPPKKKRnkdPFSLHERVEMLKEILKDRLKVVPVDFPEvkilLAV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469  75 RFARE----VGAAVILRG--LRSGADFEYEYDMAFMNRRLErsvdMVSFMTSQDYMFVSSSLLKE 133
Cdd:cd02039    82 VFILKillkVGPDKVVVGedFAFGKNASYNKDLKELFLDIE----IVEVPRVRDGKKISSTLIRE 142
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 3-59 1.05e-04

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.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 39.44  E-value: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392469   3 TAIYPGSFDPVTMGHLDITTRGSALFERVIVAVYSTP---SKDLLFSTDERVELFQESIV 59
Cdd:cd02156     1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPpvkVWQDPHELEERKESIEEDIS 60
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-69 1.42e-04

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: 40.30  E-value: 1.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1301392469   3 TAIYPGSFDPVTMGHLDITTRGSALFE--RVI-VAVYSTPSKDL-LFSTDERVELFQESIVDLPNVEVMRF 69
Cdd:cd02165     1 IALFGGSFDPPHLGHLAIAEEALEELGldRVLlLPSANPPHKPPkPASFEHRLEMLKLAIEDNPKFEVSDI 71
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-66 3.02e-03

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 36.45  E-value: 3.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469   12 PVTMGHLDITTRGSALFERVIVAVYSTPSKdlLFSTDERVELFQESIVDLPNVEV 66
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSEDAS--LFSFDERFALVKKGTKDLDNVTV 62
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 12-66 3.69e-03

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 36.47  E-value: 3.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1301392469  12 PVTMGHLDITTRGSALFERVIVAVYSTPSKdlLFSTDERVELFQESIVDLPNVEV 66
Cdd:cd02169   125 PFTLGHRYLVEKAAAENDWVHLFVVSEDKS--LFSFADRFKLVKKGTKHLKNVTV 177
 
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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