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GNAT family N-acetyltransferase [Lactobacillus johnsonii]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-141 1.03e-12

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: 60.99  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   23 QKTYVATNTVSLLEAYATQNENERVETFAVYEKDILVGFIMINFNVFNWdgapkvarNNYCIWRFMIDQRYQGKGLGKKA 102
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--------PVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499475415  103 LNKLIDYIRAKplgEGKKIYLSYVPGNEWAEKLYKEAGF 141
Cdd:pfam00583  81 LQALLEWARER---GCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-141 1.03e-12

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: 60.99  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   23 QKTYVATNTVSLLEAYATQNENERVETFAVYEKDILVGFIMINFNVFNWdgapkvarNNYCIWRFMIDQRYQGKGLGKKA 102
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--------PVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499475415  103 LNKLIDYIRAKplgEGKKIYLSYVPGNEWAEKLYKEAGF 141
Cdd:pfam00583  81 LQALLEWARER---GCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 60-158 7.91e-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: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  60 GFIMINFNvfnwdGAPKVARnnycIWRFMIDQRYQGKGLGKKALNKLIDYIRAKPLgegKKIYLSYVPGNEWAEKLYKEA 139
Cdd:COG0456    1 GFALLGLV-----DGGDEAE----IEDLAVDPEYRGRGIGRALLEAALERARERGA---RRLRLEVREDNEAAIALYEKL 68

                         90       100
                 ....*....|....*....|...
gi 499475415 140 GFVPNGEKDG----EEIVLVLDL 158
Cdd:COG0456   69 GFEEVGERPNyygdDALVMEKEL 91
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-124 7.15e-07

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: 44.19  E-value: 7.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499475415  50 FAVYEKDILVGFIMINFNVFNWDGApkvarnnyCIWRFMIDQRYQGKGLGKKALNKLIDYIRAKplgEGKKIYLS 124
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTA--------YIGDLAVLPEYRGKGIGSALLEAAEEEARER---GAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-141 5.62e-04

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: 38.08  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   53 YEKDILVGFIMINFNVFNWDgapkvarnnycIWRFMIDQRYQGKGLGKKALNKLIDYIRAKPLGEgkkIYLSYVPGNEWA 132
Cdd:TIGR01575  37 RIGGKVVGYAGVQIVLDEAH-----------ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNE---IFLEVRVSNIAA 102


                  ....*....
gi 499475415  133 EKLYKEAGF 141
Cdd:TIGR01575 103 QALYKKLGF 111
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-141 1.03e-12

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: 60.99  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   23 QKTYVATNTVSLLEAYATQNENERVETFAVYEKDILVGFIMINFNVFNWdgapkvarNNYCIWRFMIDQRYQGKGLGKKA 102
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--------PVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499475415  103 LNKLIDYIRAKplgEGKKIYLSYVPGNEWAEKLYKEAGF 141
Cdd:pfam00583  81 LQALLEWARER---GCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 60-158 7.91e-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: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  60 GFIMINFNvfnwdGAPKVARnnycIWRFMIDQRYQGKGLGKKALNKLIDYIRAKPLgegKKIYLSYVPGNEWAEKLYKEA 139
Cdd:COG0456    1 GFALLGLV-----DGGDEAE----IEDLAVDPEYRGRGIGRALLEAALERARERGA---RRLRLEVREDNEAAIALYEKL 68

                         90       100
                 ....*....|....*....|...
gi 499475415 140 GFVPNGEKDG----EEIVLVLDL 158
Cdd:COG0456   69 GFEEVGERPNyygdDALVMEKEL 91
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 34-153 5.97e-10

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: 55.01  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  34 LLEAYATQNENERVETFAVYEK--DILVGFIminfNVFNWDGAPKVARnnyciWRFMIDQRYQGKGLGKKALNKLIDYIR 111
Cdd:COG1670   47 WLERLLADWADGGALPFAIEDKedGELIGVV----GLYDIDRANRSAE-----IGYWLAPAYWGKGYATEALRALLDYAF 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499475415 112 AKPlgEGKKIYLSYVPGNEWAEKLYKEAGFVPNGEKDGEEIV 153
Cdd:COG1670  118 EEL--GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
11-156 1.62e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.85  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  11 LWDVVNLQVKANQKTY-VATNTVSLLEAYATQNENERVETFAVYEKDILVGFIMinfnVFNWDGAPkvARNNYCIWRFMI 89
Cdd:COG1247   15 IAAIYNEAIAEGTATFeTEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFAS----LGPFRPRP--AYRGTAEESIYV 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499475415  90 DQRYQGKGLGKKALNKLIDYIRAKPLgegKKIYLSYVPGNEWAEKLYKEAGFVPNGE------KDGEEIVLVL 156
Cdd:COG1247   89 DPDARGRGIGRALLEALIERARARGY---RRLVAVVLADNEASIALYEKLGFEEVGTlpevgfKFGRWLDLVL 158
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-159 2.55e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.05  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  50 FAVYEKDILVGFImiNFNVFNWDGApkvarnnyCIWRFMIDQRYQGKGLGKKALNKLIDYIRAKPLgegKKIYLSYVPGN 129
Cdd:COG0454   37 IAVDDKGEPIGFA--GLRRLDDKVL--------ELKRLYVLPEYRGKGIGKALLEALLEWARERGC---TALELDTLDGN 103

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499475415 130 EWAEKLYKEAGFVPNGE---KDGEEIVLVLDLG 159
Cdd:COG0454  104 PAAIRFYERLGFKEIERyvaYVGGEFEKELSLS 136
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
34-158 2.57e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.08  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  34 LLEAYATQNENERVE----------TFAVYEKDILVGFIMinFNVFNWDGAPKVArnnyCIWRFMIDQRYQGKGLGKKAL 103
Cdd:COG3153   16 LRAAFGPGREAELVDrlredpaaglSLVAEDDGEIVGHVA--LSPVDIDGEGPAL----LLGPLAVDPEYRGQGIGRALM 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499475415 104 NKLIDyiRAKPLGEgKKIYLSyvpGNEWAEKLYKEAGFVPNGEKD----GEEIVLVLDL 158
Cdd:COG3153   90 RAALE--AARERGA-RAVVLL---GDPSLLPFYERFGFRPAGELGltlgPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-158 4.94e-08

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: 49.22  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415  34 LLEAYATQNENERvetFAVYEKD-ILVGFIMInfnVFNWDGAPKvarnnycIWRFMIDQRYQGKGLGKKALNKLIDYIRA 112
Cdd:COG1246   17 LIRPYALEEEIGE---FWVAEEDgEIVGCAAL---HPLDEDLAE-------LRSLAVHPDYRGRGIGRRLLEALLAEARE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499475415 113 KPLgegKKIYLSYvpgNEWAEKLYKEAGFVPNGEKD--------GEEIVLVLDL 158
Cdd:COG1246   84 LGL---KRLFLLT---TSAAIHFYEKLGFEEIDKEDlpyakvwqRDSVVMEKDL 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-124 7.15e-07

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: 44.19  E-value: 7.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499475415  50 FAVYEKDILVGFIMINFNVFNWDGApkvarnnyCIWRFMIDQRYQGKGLGKKALNKLIDYIRAKplgEGKKIYLS 124
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTA--------YIGDLAVLPEYRGKGIGSALLEAAEEEARER---GAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
86-146 1.76e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.79  E-value: 1.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499475415  86 RFMIDQRYQGKGLGKKALNKLIDYIRAKPlgeGKKIYLS---YvpgnewAEKLYKEAGFVPNGE 146
Cdd:COG2153   63 RVAVLPEYRGQGLGRALMEAAIEEARERG---ARRIVLSaqaH------AVGFYEKLGFVPVGE 117
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-149 1.91e-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: 44.57  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   36 EAYATQNENERVETFAVYEKDILVGFIMInfnvfnwdgapkvaRNNYCIWRFMIDQRYQGKGLGKKALNKLIDYIRAKpl 115
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVIAL--------------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKD-- 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499475415  116 gEGKKIYLSyVPGNEWAEKLYKEAGFV---PNGEKDG 149
Cdd:pfam13673  84 -GIKLSELT-VNASPYAVPFYEKLGFRatgPEQEFNG 118
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-143 4.91e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.44  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   45 ERVETFAVYEKDILVGFIMInfnvfnwdgAPKVARNNYCIWRFMIDQRYQGKGLGKkalnKLIDYIRAkpLGEGKKIYLS 124
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAAL---------LPLDDEGALAELRLAVHPEYRGQGIGR----ALLEAAEA--AAKEGGIKLL 65

                          90
                  ....*....|....*....
gi 499475415  125 YVPGNEWAEKLYKEAGFVP 143
Cdd:pfam13508  66 ELETTNRAAAFYEKLGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
84-146 2.04e-05

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.05  E-value: 2.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499475415  84 IWRFMIDQRYQGKGLGKKALNKLIDYIRAkplgEGKK-IYLSYVPGNEWAEKLYKEAGFVPNGE 146
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALA----RGARtPFLYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 31-142 2.75e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.87  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   31 TVSLLEAYATQNENERVETFAVYEKD-ILVGFIMINfNVFNWDGAPKVArnnyciwrFMIDQRYQGKGLGKKALNKLIDY 109
Cdd:pfam13302  38 AREWLARIWAADEAERGYGWAIELKDtGFIGSIGLY-DIDGEPERAELG--------YWLGPDYWGKGYATEAVRALLEY 108

                          90       100       110
                  ....*....|....*....|....*....|...
gi 499475415  110 IRAKPlgEGKKIYLSYVPGNEWAEKLYKEAGFV 142
Cdd:pfam13302 109 AFEEL--GLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-141 5.62e-04

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: 38.08  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499475415   53 YEKDILVGFIMINFNVFNWDgapkvarnnycIWRFMIDQRYQGKGLGKKALNKLIDYIRAKPLGEgkkIYLSYVPGNEWA 132
Cdd:TIGR01575  37 RIGGKVVGYAGVQIVLDEAH-----------ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNE---IFLEVRVSNIAA 102


                  ....*....
gi 499475415  133 EKLYKEAGF 141
Cdd:TIGR01575 103 QALYKKLGF 111
 
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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