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Conserved domains on  [gi|447025417|ref|WP_001102673|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

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
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 ...
22-135 2.74e-13

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: 62.15  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   22 KEDQRKFVPAVAVSLAKVYIKPDGDNVEYIPFAIYDGDLmVGFVMHAVVIETSDMYWINGFIIDQSQQGNGYGKAALQES 101
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGEL-VGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQAL 84
                          90       100       110
                  ....*....|....*....|....*....|....
gi 447025417  102 INIIKNtfKACKEIRLTVHKDNISAKKLYERYGF 135
Cdd:pfam00583  85 LEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
22-135 2.74e-13

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: 62.15  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   22 KEDQRKFVPAVAVSLAKVYIKPDGDNVEYIPFAIYDGDLmVGFVMHAVVIETSDMYWINGFIIDQSQQGNGYGKAALQES 101
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGEL-VGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQAL 84
                          90       100       110
                  ....*....|....*....|....*....|....
gi 447025417  102 INIIKNtfKACKEIRLTVHKDNISAKKLYERYGF 135
Cdd:pfam00583  85 LEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-135 1.53e-12

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: 61.55  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   1 MNVQLKVVTRDNWEDALKLQVKEDQRKFVPAVAVSLAKV-----YIKPDGDNVEYIPFAIYD--GDLMVGFVMHAVVIET 73
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEArawleRLLADWADGGALPFAIEDkeDGELIGVVGLYDIDRA 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447025417  74 SDMYWInGFIIDQSQQGNGYGKAALQESINIIKNTFKaCKEIRLTVHKDNISAKKLYERYGF 135
Cdd:COG1670   86 NRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELG-LHRVEAEVDPDNTASIRVLEKLGF 145
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
56-135 5.04e-09

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: 51.56  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   56 YDGDLMVGFvmhAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDNISAKKLYERYGF 135
Cdd:TIGR01575  37 RIGGKVVGY---AGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKG--RGVNEIFLEVRVSNIAAQALYKKLGF 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
53-118 6.01e-04

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: 36.10  E-value: 6.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447025417  53 FAIYDGDLMVGFVMHAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLT 118
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE--RGAKRLRLE 65
PRK10140 PRK10140
N-acetyltransferase;
81-135 5.58e-03

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 35.34  E-value: 5.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447025417  81 GFIIDQSQQGNGYGKAALQESINIIKNTFKAcKEIRLTVHKDNISAKKLYERYGF 135
Cdd:PRK10140  83 GICVDSRWKNRGVASALMREMIEMCDNWLRV-DRIELTVFVDNAPAIKVYKKYGF 136
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
22-135 2.74e-13

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: 62.15  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   22 KEDQRKFVPAVAVSLAKVYIKPDGDNVEYIPFAIYDGDLmVGFVMHAVVIETSDMYWINGFIIDQSQQGNGYGKAALQES 101
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGEL-VGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQAL 84
                          90       100       110
                  ....*....|....*....|....*....|....
gi 447025417  102 INIIKNtfKACKEIRLTVHKDNISAKKLYERYGF 135
Cdd:pfam00583  85 LEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-135 1.53e-12

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: 61.55  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   1 MNVQLKVVTRDNWEDALKLQVKEDQRKFVPAVAVSLAKV-----YIKPDGDNVEYIPFAIYD--GDLMVGFVMHAVVIET 73
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEArawleRLLADWADGGALPFAIEDkeDGELIGVVGLYDIDRA 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447025417  74 SDMYWInGFIIDQSQQGNGYGKAALQESINIIKNTFKaCKEIRLTVHKDNISAKKLYERYGF 135
Cdd:COG1670   86 NRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELG-LHRVEAEVDPDNTASIRVLEKLGF 145
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
63-151 5.82e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.13  E-value: 5.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417  63 GFVMhAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDNISAKKLYERYGFISLGQEY 142
Cdd:COG0456    1 GFAL-LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                 ....*....
gi 447025417 143 DGEQVYRLF 151
Cdd:COG0456   78 NYYGDDALV 86
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
56-135 5.04e-09

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: 51.56  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   56 YDGDLMVGFvmhAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDNISAKKLYERYGF 135
Cdd:TIGR01575  37 RIGGKVVGY---AGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKG--RGVNEIFLEVRVSNIAAQALYKKLGF 111
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
53-151 2.36e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.00  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417  53 FAIYDGDLMVGFVM--HAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDNISakkLY 130
Cdd:COG3153   42 LVAEDDGEIVGHVAlsPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARE--RGARAVVLLGDPSLLP---FY 116
                         90       100
                 ....*....|....*....|.
gi 447025417 131 ERYGFISLGQEYDGEQVYRLF 151
Cdd:COG3153  117 ERFGFRPAGELGLTLGPDEVF 137
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
68-139 2.52e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.67  E-value: 2.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447025417  68 AVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNTFkaCKEIRLTVHKDNISAKKLYERYGFISLG 139
Cdd:COG3393    7 GVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARG--ARTPFLYVDADNPAARRLYERLGFRPVG 76
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
49-141 2.95e-07

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: 46.50  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   49 EYIPFAIYDGDLMVGfvmhavVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDNiSAKK 128
Cdd:pfam13673  30 EYFFFVAFEGGQIVG------VIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK--DGIKLSELTVNASP-YAVP 100
                          90
                  ....*....|...
gi 447025417  129 LYERYGFISLGQE 141
Cdd:pfam13673 101 FYEKLGFRATGPE 113
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
53-135 6.02e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 44.75  E-value: 6.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417   53 FAIYDGDLMVGFVMHAVVIETSDMYWINgFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDnisAKKLYER 132
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELR-LAVHPEYRGQGIGRALLEAAEAAAKE--GGIKLLELETTNR---AAAFYEK 79

                  ...
gi 447025417  133 YGF 135
Cdd:pfam13508  80 LGF 82
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
44-135 1.04e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 45.43  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417  44 DGDNVEYIPFAIYDGDLMVGFV-MHAV---VIETSDMYwingfiIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTV 119
Cdd:COG0454   28 EGSLAGAEFIAVDDKGEPIGFAgLRRLddkVLELKRLY------VLPEYRGKGIGKALLEALLEWARE--RGCTALELDT 99
                         90
                 ....*....|....*.
gi 447025417 120 HKDNISAKKLYERYGF 135
Cdd:COG0454  100 LDGNPAAIRFYERLGF 115
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
53-143 2.98e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.02  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417  53 FAIYDGDLMVGFVmhAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHkdnISAKKLYER 132
Cdd:COG2153   37 LLAYDDGELVATA--RLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARE--RGARRIVLSAQ---AHAVGFYEK 109
                         90
                 ....*....|.
gi 447025417 133 YGFISLGQEYD 143
Cdd:COG2153  110 LGFVPVGEEFL 120
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
82-151 8.93e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.06  E-value: 8.93e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417  82 FIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVHKDNISAKKLYERYGFISLGQEydgEQVYRLF 151
Cdd:COG1247   86 IYVDPDARGRGIGRALLEALIERARA--RGYRRLVAVVLADNEASIALYEKLGFEEVGTL---PEVGFKF 150
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
81-135 2.09e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.87  E-value: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 447025417   81 GFIIDQSQQGNGYGKAALQESINIIKNTFKAcKEIRLTVHKDNISAKKLYERYGF 135
Cdd:pfam13302  85 GYWLGPDYWGKGYATEAVRALLEYAFEELGL-PRLVARIDPENTASRRVLEKLGF 138
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
53-118 6.01e-04

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: 36.10  E-value: 6.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447025417  53 FAIYDGDLMVGFVMHAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLT 118
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE--RGAKRLRLE 65
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
54-141 3.52e-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: 35.35  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025417  54 AIYDGDLmVGFVmhAVVIETSDMYWINGFIIDQSQQGNGYGKAALQESINIIKNtfKACKEIRLTVhkdNISAKKLYERY 133
Cdd:COG1246   33 AEEDGEI-VGCA--ALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARE--LGLKRLFLLT---TSAAIHFYEKL 104

                 ....*...
gi 447025417 134 GFISLGQE 141
Cdd:COG1246  105 GFEEIDKE 112
PRK10140 PRK10140
N-acetyltransferase;
81-135 5.58e-03

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 35.34  E-value: 5.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447025417  81 GFIIDQSQQGNGYGKAALQESINIIKNTFKAcKEIRLTVHKDNISAKKLYERYGF 135
Cdd:PRK10140  83 GICVDSRWKNRGVASALMREMIEMCDNWLRV-DRIELTVFVDNAPAIKVYKKYGF 136
 
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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