NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446660516|ref|WP_000737862|]
View 

MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-134 2.57e-13

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 63.48  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   1 MKKLYLKAIDKNNWEEAIRLSVKEEQQTFIASNLYSIAEVQ-----FLDNFYAKGIYF-------DEKMIGFTTF-GIDP 67
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARawlerLLADWADGGALPfaiedkeDGELIGVVGLyDIDR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446660516  68 DDNNYWIyRLMIDEKFQGKGIGKQAIYLVIDEIRRNNNANisIIMIGYAPENLTAKFVYKKAGFIET 134
Cdd:COG1670   85 ANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLH--RVEAEVDPDNTASIRVLEKLGFRLE 148
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-134 2.57e-13

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 63.48  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   1 MKKLYLKAIDKNNWEEAIRLSVKEEQQTFIASNLYSIAEVQ-----FLDNFYAKGIYF-------DEKMIGFTTF-GIDP 67
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARawlerLLADWADGGALPfaiedkeDGELIGVVGLyDIDR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446660516  68 DDNNYWIyRLMIDEKFQGKGIGKQAIYLVIDEIRRNNNANisIIMIGYAPENLTAKFVYKKAGFIET 134
Cdd:COG1670   85 ANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLH--RVEAEVDPDNTASIRVLEKLGFRLE 148
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-131 7.26e-11

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 55.99  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   14 WEEAIRLSVKEEQQTFIASNLYSIAEVQFLDNFYAKGIYFDEKMIGFTTFGIDPDDNNY-WIYRLMIDEKFQGKGIGKQA 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446660516   93 IYLVIDEIRrnnNANISIIMIGYAPENLTAKFVYKKAGF 131
Cdd:pfam00583  81 LQALLEWAR---ERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-104 2.29e-06

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 42.65  E-value: 2.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446660516  54 DEKMIGFTTFGIDPDDNNY-WIYRLMIDEKFQGKGIGKQAIYLVIDEIRRNN 104
Cdd:cd04301    7 DGEIVGFASLSPDGSGGDTaYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 36-131 3.25e-03

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 35.38  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   36 SIAEVQFLDNFYAKGIYFDEKMIGFTTFGIDPDdnNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRrnnNANISIIMIGY 115
Cdd:TIGR01575  21 QFAEELANYHLCYLLARIGGKVVGYAGVQIVLD--EAHILNIAVKPEYQGQGIGRALLRELIDEAK---GRGVNEIFLEV 95

                          90
                  ....*....|....*.
gi 446660516  116 APENLTAKFVYKKAGF 131
Cdd:TIGR01575  96 RVSNIAAQALYKKLGF 111
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-134 2.57e-13

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 63.48  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   1 MKKLYLKAIDKNNWEEAIRLSVKEEQQTFIASNLYSIAEVQ-----FLDNFYAKGIYF-------DEKMIGFTTF-GIDP 67
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARawlerLLADWADGGALPfaiedkeDGELIGVVGLyDIDR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446660516  68 DDNNYWIyRLMIDEKFQGKGIGKQAIYLVIDEIRRNNNANisIIMIGYAPENLTAKFVYKKAGFIET 134
Cdd:COG1670   85 ANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLH--RVEAEVDPDNTASIRVLEKLGFRLE 148
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 59-135 6.52e-11

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 6.52e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446660516  59 GFTTFGIDPDDNNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRRnnnANISIIMIGYAPENLTAKFVYKKAGFIETE 135
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE---RGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-131 7.26e-11

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 55.99  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   14 WEEAIRLSVKEEQQTFIASNLYSIAEVQFLDNFYAKGIYFDEKMIGFTTFGIDPDDNNY-WIYRLMIDEKFQGKGIGKQA 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446660516   93 IYLVIDEIRrnnNANISIIMIGYAPENLTAKFVYKKAGF 131
Cdd:pfam00583  81 LQALLEWAR---ERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-133 1.77e-07

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.29  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   51 IYFDEKMIGFTTFGIDPDDNNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRRNNnanisIIMIGYAPENLTAKFvYKKAG 130
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGG-----IKLLELETTNRAAAF-YEKLG 81


                  ...
gi 446660516  131 FIE 133
Cdd:pfam13508  82 FEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
54-135 3.66e-07

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 46.62  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516  54 DEKMIG---FTTFGIDPDDNNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRRnnnANISIIMIGYAPENLtaKFvYKKAG 130
Cdd:COG3153   47 DGEIVGhvaLSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARE---RGARAVVLLGDPSLL--PF-YERFG 120


                 ....*
gi 446660516 131 FIETE 135
Cdd:COG3153  121 FRPAG 125
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 54-135 2.16e-06

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 44.18  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   54 DEKMIGFTTFgidpDDNNYwIYRLMIDEKFQGKGIGKQAIYLVIDEIRRNNNANISIIMIgyapENLTAKFVYKKAGFIE 133
Cdd:pfam13673  39 GGQIVGVIAL----RDRGH-ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN----ASPYAVPFYEKLGFRA 109


                  ..
gi 446660516  134 TE 135
Cdd:pfam13673 110 TG 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-104 2.29e-06

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 42.65  E-value: 2.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446660516  54 DEKMIGFTTFGIDPDDNNY-WIYRLMIDEKFQGKGIGKQAIYLVIDEIRRNN 104
Cdd:cd04301    7 DGEIVGFASLSPDGSGGDTaYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 9-135 8.22e-05

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.04  E-value: 8.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   9 IDKNNWEEAIRLSVKEEQQTFIASNLYSIAEVQFLdnfyakGIYFDEKMIGFTTFGIDPDDNNYwIYRLMIDEKFQGKGI 88
Cdd:COG0454    3 IRKATPEDINFILLIEALDAELKAMEGSLAGAEFI------AVDDKGEPIGFAGLRRLDDKVLE-LKRLYVLPEYRGKGI 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446660516  89 GKQAIYLVIDEIRRNnnaNISIIMIGYAPENLTAKFVYKKAGFIETE 135
Cdd:COG0454   76 GKALLEALLEWARER---GCTALELDTLDGNPAAIRFYERLGFKEIE 119
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 24-131 6.38e-04

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 37.71  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   24 EEQQTFIASNLYSIAEVQ-FLDNFYA-----KGIYF-----DEKMIGFTTFgIDPDDNN------YWIYRlmideKFQGK 86
Cdd:pfam13302  22 PEVMRYGVPWPLTLEEAReWLARIWAadeaeRGYGWaielkDTGFIGSIGL-YDIDGEPeraelgYWLGP-----DYWGK 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446660516   87 GIGKQAIYLVIDEIRRnnNANISIIMIGYAPENLTAKFVYKKAGF 131
Cdd:pfam13302  96 GYATEAVRALLEYAFE--ELGLPRLVARIDPENTASRRVLEKLGF 138
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
54-134 1.36e-03

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 36.90  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516  54 DEKMIGFTTFGIDPDDNNY-WIY--RLMIDEKFQGKGIGKQAIYLVIDEIRRnnnANISIIMIGYAPENLTAKFVYKKAG 130
Cdd:COG1247   60 DGEVVGFASLGPFRPRPAYrGTAeeSIYVDPDARGRGIGRALLEALIERARA---RGYRRLVAVVLADNEASIALYEKLG 136


                 ....
gi 446660516 131 FIET 134
Cdd:COG1247  137 FEEV 140
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 54-104 2.19e-03

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 35.19  E-value: 2.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446660516   54 DEKMIGFTTFgiDPDDNNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRRNN 104
Cdd:pfam14542   8 GGAEVAFLTY--RRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEG 56
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 36-131 3.25e-03

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 35.38  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516   36 SIAEVQFLDNFYAKGIYFDEKMIGFTTFGIDPDdnNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRrnnNANISIIMIGY 115
Cdd:TIGR01575  21 QFAEELANYHLCYLLARIGGKVVGYAGVQIVLD--EAHILNIAVKPEYQGQGIGRALLRELIDEAK---GRGVNEIFLEV 95

                          90
                  ....*....|....*.
gi 446660516  116 APENLTAKFVYKKAGF 131
Cdd:TIGR01575  96 RVSNIAAQALYKKLGF 111
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
50-134 4.46e-03

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.16  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516  50 GIYFDEKMIGFTTFgIDPDDNNYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRRNNNANISIimigYAPENLTaKFvYKKA 129
Cdd:COG2153   38 LAYDDGELVATARL-LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL----SAQAHAV-GF-YEKL 110


                 ....*
gi 446660516 130 GFIET 134
Cdd:COG2153  111 GFVPV 115
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 54-135 4.65e-03

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 34.97  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660516  54 DEKMIGFTTFGIDPDDNnYWIYRLMIDEKFQGKGIGKQAIYLVIDEIRRnnnANISIIMIGYAPEnlTAKFvYKKAGFIE 133
Cdd:COG1246   36 DGEIVGCAALHPLDEDL-AELRSLAVHPDYRGRGIGRRLLEALLAEARE---LGLKRLFLLTTSA--AIHF-YEKLGFEE 108


                 ..
gi 446660516 134 TE 135
Cdd:COG1246  109 ID 110
 
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