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MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11450351)

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

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List of domain hits

 Name Accession Description Interval E-value
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
16-144 5.40e-55

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


:

Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 168.82  E-value: 5.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  16 DAVRIRHQVFVVEQGVPLSREIDKDEAHCIHFVLYsDKKEPQGTVRLLPLENGKMKLQRMAILSEYRHQGLGKLLIEEAE 95
Cdd:COG2153    6 DALALRREVFVVEQGVPPYLELDGKDEDARHLLAY-DDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAI 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488239138  96 TFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:COG2153   85 EEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPL 133
 
Name Accession Description Interval E-value
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
16-144 5.40e-55

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 168.82  E-value: 5.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  16 DAVRIRHQVFVVEQGVPLSREIDKDEAHCIHFVLYsDKKEPQGTVRLLPLENGKMKLQRMAILSEYRHQGLGKLLIEEAE 95
Cdd:COG2153    6 DALALRREVFVVEQGVPPYLELDGKDEDARHLLAY-DDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAI 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488239138  96 TFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:COG2153   85 EEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPL 133
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 33-144 4.00e-20

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: 80.01  E-value: 4.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138   33 LSREIDKDEAHcihFVLYSDKKEPQGTVRLLplenGKMKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNT--ILLGA 110
Cdd:pfam13673  22 LRERIDQGEYF---FFVAFEGGQIVGVIALR----DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLseLTVNA 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488239138  111 QSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:pfam13673  95 SPYAVPFYEKLGFRATGPEQEFNGIRFVPMEKEL 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-108 1.30e-08

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: 48.43  E-value: 1.30e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239138  47 FVLYSDKKEPQGTVRLLPLENGK--MKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILL 108
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 76-133 3.28e-08

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: 48.86  E-value: 3.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239138   76 AILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQST---AEAFYEKLGY--IA-----YGEPFEDA 133
Cdd:TIGR01575  61 AVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGFneIAirrnyYPDPGEDA 128
PRK10314 PRK10314
GNAT family N-acetyltransferase;
9-142 5.95e-07

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 45.99  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138   9 TMSNIYlDAVRIRHQVFVVEQGVPLsREIDKDE--AHCIHFVLYSDKkEPQGTVRLLPLENG--KMKLQRMAILSEYRHQ 84
Cdd:PRK10314  13 SVSQLY-ALLQLRCAVFVVEQNCPY-QDIDGDDltGDNRHILGWKND-ELVAYARILKSDDDlePVVIGRVIVSEALRGE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488239138  85 GLGKLLIEEA-ETFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKK 142
Cdd:PRK10314  90 KVGQQLMSKTlESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAR 148
 
Name Accession Description Interval E-value
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
16-144 5.40e-55

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 168.82  E-value: 5.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  16 DAVRIRHQVFVVEQGVPLSREIDKDEAHCIHFVLYsDKKEPQGTVRLLPLENGKMKLQRMAILSEYRHQGLGKLLIEEAE 95
Cdd:COG2153    6 DALALRREVFVVEQGVPPYLELDGKDEDARHLLAY-DDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAI 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488239138  96 TFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:COG2153   85 EEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPL 133
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 33-144 4.00e-20

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: 80.01  E-value: 4.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138   33 LSREIDKDEAHcihFVLYSDKKEPQGTVRLLplenGKMKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNT--ILLGA 110
Cdd:pfam13673  22 LRERIDQGEYF---FFVAFEGGQIVGVIALR----DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLseLTVNA 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488239138  111 QSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:pfam13673  95 SPYAVPFYEKLGFRATGPEQEFNGIRFVPMEKEL 128
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
18-144 5.09e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 74.74  E-value: 5.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  18 VRIRHQVFVVEQGVPLSREIDKDEAHCIHFVLYSDKkEPQGTVRLLPL----ENGKMKLQRMAILSEYRHQGLGKLLIEE 93
Cdd:COG3153   13 AALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDG-EIVGHVALSPVdidgEGPALLLGPLAVDPEYRGQGIGRALMRA 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488239138  94 AETFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:COG3153   92 ALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 46-144 5.27e-17

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: 71.95  E-value: 5.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  46 HFVLYSDKKEPQGTVRLLPLENGKMKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQSTAEAFYEKLGYIA 125
Cdd:COG1246   29 EFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEE 108

                         90       100
                 ....*....|....*....|...
gi 488239138 126 YGE---PFEDAGMPH-IYMKKTL 144
Cdd:COG1246  109 IDKedlPYAKVWQRDsVVMEKDL 131
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 35-144 1.91e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 70.85  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  35 REIDKDEAHCiHFVLYSDKKEPQGTVRLLPLENGKMKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLG---AQ 111
Cdd:COG0454   25 KAMEGSLAGA-EFIAVDDKGEPIGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDtldGN 103

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488239138 112 STAEAFYEKLGYIAYGEPFEDAGMPhiyMKKTL 144
Cdd:COG0454  104 PAAIRFYERLGFKEIERYVAYVGGE---FEKEL 133
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-123 1.61e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 64.40  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138   43 HCIHFVLYSDKKEPqGTVRLLPLENGKMKLQ-RMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQSTAEAFYEKL 121
Cdd:pfam13508   2 GGRFFVAEDDGKIV-GFAALLPLDDEGALAElRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKL 80


                  ..
gi 488239138  122 GY 123
Cdd:pfam13508  81 GF 82
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-144 1.66e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.29  E-value: 1.66e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239138  72 LQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQST---AEAFYEKLGYIAYGEPFEDAGMPHIYMKKTL 144
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERPNYYGDDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-123 1.17e-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: 60.22  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138   32 PLSREIDKDEAHCIHFVLYSDKKEPQGTVRLLPL--ENGKMKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLG 109
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIddEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLE 99

                          90
                  ....*....|....*..
gi 488239138  110 AQST---AEAFYEKLGY 123
Cdd:pfam00583 100 VAADnlaAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
77-144 2.36e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 52.69  E-value: 2.36e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239138  77 ILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQST---AEAFYEKLGYIAYGEPFEDAGMPH-----IYMKKTL 144
Cdd:COG1247   88 VDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneaSIALYEKLGFEEVGTLPEVGFKFGrwldlVLMQKRL 163
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
72-128 1.27e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.14  E-value: 1.27e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138  72 LQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQS---TAEAFYEKLGYIAYGE 128
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDAdnpAARRLYERLGFRPVGE 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-108 1.30e-08

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: 48.43  E-value: 1.30e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239138  47 FVLYSDKKEPQGTVRLLPLENGK--MKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILL 108
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 76-133 3.28e-08

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: 48.86  E-value: 3.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239138   76 AILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQST---AEAFYEKLGY--IA-----YGEPFEDA 133
Cdd:TIGR01575  61 AVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGFneIAirrnyYPDPGEDA 128
PRK10314 PRK10314
GNAT family N-acetyltransferase;
9-142 5.95e-07

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 45.99  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239138   9 TMSNIYlDAVRIRHQVFVVEQGVPLsREIDKDE--AHCIHFVLYSDKkEPQGTVRLLPLENG--KMKLQRMAILSEYRHQ 84
Cdd:PRK10314  13 SVSQLY-ALLQLRCAVFVVEQNCPY-QDIDGDDltGDNRHILGWKND-ELVAYARILKSDDDlePVVIGRVIVSEALRGE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488239138  85 GLGKLLIEEA-ETFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEPFEDAGMPHIYMKK 142
Cdd:PRK10314  90 KVGQQLMSKTlESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAR 148
Acetyltransf_5 pfam13444
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 20-64 1.08e-05

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


Pssm-ID: 463880  Cd Length: 102  Bit Score: 41.83  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488239138   20 IRHQVFVVE-----QGVPLSREIDKDEAHCIHFVLYsDKKEPQ--GTVRLLP 64
Cdd:pfam13444   1 LRYRVFREEmgatgPAALPGLDIDRFDAYCDHLLVW-DDDTGEvvGTYRLLP 51
LasI COG3916
N-acyl-homoserine lactone synthase LasI (autoinducer biosynthesis) [Signal transduction ...
 19-64 1.35e-05

N-acyl-homoserine lactone synthase LasI (autoinducer biosynthesis) [Signal transduction mechanisms];


Pssm-ID: 443121 [Multi-domain]  Cd Length: 201  Bit Score: 43.00  E-value: 1.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488239138  19 RIRHQVFVVEQG----VPLSREIDK-DEAHCIHFVLYSDKKEPQGTVRLLP 64
Cdd:COG3916   21 RLRHRVFVEELGwevpVPDGLEIDQyDDPSAHYLLAHDEDGRVVGCVRLLP 71
ELP3 COG1243
tRNA U34 5-carboxymethylaminomethylation enzyme Elp3 (RNA elongator complex protein 3), ...
 80-144 3.73e-05

tRNA U34 5-carboxymethylaminomethylation enzyme Elp3 (RNA elongator complex protein 3), contains radical SAM and acetyltransferase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440856 [Multi-domain]  Cd Length: 432  Bit Score: 42.20  E-value: 3.73e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239138  80 EYRHQGLGKLLIEEAETFAKNQGYNTILLGAQSTAEAFYEKLGYIAYGEpfedagmphiYMKKTL 144
Cdd:COG1243  378 SWQHRGYGKRLLEEAEEIAREEGYKKLAVISGIGVREYYRKLGYERDGP----------YMSKDL 432
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
44-111 7.38e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 34.91  E-value: 7.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239138  44 CIhfVLYSDKKEPQGTVRLLPLENGKMKLQRMAILSEYRHQGLGKLLIEEAETFAKNQGYNTILLGAQ 111
Cdd:PRK10975 103 CL--LLRDASGQIQGFVTLRELNDTDARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQ 168
 
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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