NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515706349|ref|WP_017138949|]
View 

MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-164 4.08e-27

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 99.68  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   1 MIRDALPKDAKHIAQVHvsswqQAYVDLMPADFlaslsTTLPQKEANWARLIESQDAG---VLVAEVDGNVIGWLSLGLC 77
Cdd:COG1247    3 TIRPATPEDAPAIAAIY-----NEAIAEGTATF-----ETEPPSEEEREAWFAAILAPgrpVLVAEEDGEVVGFASLGPF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  78 RDTDTPEvASGEVmAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFGGTEDPGSRRTLVRG 157
Cdd:COG1247   73 RPRPAYR-GTAEE-SIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKF 150


                 ....*..
gi 515706349 158 GVTLEEV 164
Cdd:COG1247  151 GRWLDLV 157
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-164 4.08e-27

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 99.68  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   1 MIRDALPKDAKHIAQVHvsswqQAYVDLMPADFlaslsTTLPQKEANWARLIESQDAG---VLVAEVDGNVIGWLSLGLC 77
Cdd:COG1247    3 TIRPATPEDAPAIAAIY-----NEAIAEGTATF-----ETEPPSEEEREAWFAAILAPgrpVLVAEEDGEVVGFASLGPF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  78 RDTDTPEvASGEVmAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFGGTEDPGSRRTLVRG 157
Cdd:COG1247   73 RPRPAYR-GTAEE-SIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKF 150


                 ....*..
gi 515706349 158 GVTLEEV 164
Cdd:COG1247  151 GRWLDLV 157
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-143 4.06e-19

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: 77.94  E-value: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   23 QAYVDLMPADFLASLSTTLPQKEANWARLiesQDAGVLVAEVDGNVIGWLSLGLCRDtdtpEVASGEVMAIYVLADYWGH 102
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDED---ASEGFFVAEEDGELVGFASLSIIDD----EPPVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 515706349  103 GIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFG 143
Cdd:pfam00583  75 GIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-127 3.92e-10

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: 53.05  E-value: 3.92e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515706349  59 VLVAEVDGNVIGWLSLGLCRDTDTpevaSGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLW 127
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGD----TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 60-143 7.65e-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: 48.48  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   60 LVAEVDGNVIGWLSLGLCRDTdtpevasGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFY 139
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDE-------AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALY 106


                  ....
gi 515706349  140 TRFG 143
Cdd:TIGR01575 107 KKLG 110
PRK03624 PRK03624
putative acetyltransferase; Provisional
 45-148 1.11e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.99  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  45 EANWARLIESQDAGVLVAEVDGNVIGwlslglcrdtdtpevasgEVMA--------IYVLA---DYWGHGIGAQLWQAGF 113
Cdd:PRK03624  33 EMDIERKLNHDPSLFLVAEVGGEVVG------------------TVMGgydghrgwAYYLAvhpDFRGRGIGRALVARLE 94

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515706349 114 QRLVEQGYKRISLWVLAANQRAVRFYTRFGGTEDP 148
Cdd:PRK03624  95 KKLIARGCPKINLQVREDNDAVLGFYEALGYEEQD 129
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-164 4.08e-27

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 99.68  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   1 MIRDALPKDAKHIAQVHvsswqQAYVDLMPADFlaslsTTLPQKEANWARLIESQDAG---VLVAEVDGNVIGWLSLGLC 77
Cdd:COG1247    3 TIRPATPEDAPAIAAIY-----NEAIAEGTATF-----ETEPPSEEEREAWFAAILAPgrpVLVAEEDGEVVGFASLGPF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  78 RDTDTPEvASGEVmAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFGGTEDPGSRRTLVRG 157
Cdd:COG1247   73 RPRPAYR-GTAEE-SIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKF 150


                 ....*..
gi 515706349 158 GVTLEEV 164
Cdd:COG1247  151 GRWLDLV 157
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-143 4.06e-19

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: 77.94  E-value: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   23 QAYVDLMPADFLASLSTTLPQKEANWARLiesQDAGVLVAEVDGNVIGWLSLGLCRDtdtpEVASGEVMAIYVLADYWGH 102
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDED---ASEGFFVAEEDGELVGFASLSIIDD----EPPVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 515706349  103 GIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFG 143
Cdd:pfam00583  75 GIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-143 4.09e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.58  E-value: 4.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   2 IRDALPKDAKHIAQVHvsswQQAYVDLMPADFLASLSTTLpqkeanwarliesQDAGVLVAEVDGNVIGwlSLGLCRDTD 81
Cdd:COG3153    1 IRPATPEDAEAIAALL----RAAFGPGREAELVDRLREDP-------------AAGLSLVAEDDGEIVG--HVALSPVDI 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515706349  82 TPEVASGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRIslwVLAANQRAVRFYTRFG 143
Cdd:COG3153   62 DGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFG 120
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 70-162 3.38e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.68  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  70 GWLSLGLCRDTDTpevasGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFGGTEDPG 149
Cdd:COG0456    1 GFALLGLVDGGDE-----AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75

                         90
                 ....*....|...
gi 515706349 150 SRRTLVRGGVTLE 162
Cdd:COG0456   76 RPNYYGDDALVME 88
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 51-143 6.10e-14

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: 65.01  E-value: 6.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  51 LIESQDAGVLVAEVDGNVIGWLSLGLCRDTDtpevasGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWvla 130
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAALHPLDEDL------AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL--- 92

                         90
                 ....*....|...
gi 515706349 131 ANQRAVRFYTRFG 143
Cdd:COG1246   93 TTSAAIHFYEKLG 105
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 49-143 1.10e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 61.61  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  49 ARLIESQDAGVLVAEVDGNVIGWLSLGLCRDTdtpevaSGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWV 128
Cdd:COG0454   26 AMEGSLAGAEFIAVDDKGEPIGFAGLRRLDDK------VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDT 99

                         90
                 ....*....|....*
gi 515706349 129 LAANQRAVRFYTRFG 143
Cdd:COG0454  100 LDGNPAAIRFYERLG 114
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-143 2.16e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.39  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   55 QDAGVLVAEVDGNVIGWLSLGLCRDTDTpevasGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKrisLWVLAANQR 134
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGA-----LAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIK---LLELETTNR 72


                  ....*....
gi 515706349  135 AVRFYTRFG 143
Cdd:pfam13508  73 AAAFYEKLG 81
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-170 1.83e-11

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: 59.24  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   2 IRDALPKDAKHIAQVHVSSWQQAYVDLMP---ADFLASLsttlpqkeANWARLIESQDAGVLVAE--VDGNVIGWLslGL 76
Cdd:COG1670   10 LRPLRPEDAEALAELLNDPEVARYLPGPPyslEEARAWL--------ERLLADWADGGALPFAIEdkEDGELIGVV--GL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  77 CRDTDTPEVASgevMAIYVLADYWGHGIGAQLWQA----GFQRLveqGYKRISLWVLAANQRAVRFYTRFGGTEDPGSRR 152
Cdd:COG1670   80 YDIDRANRSAE---IGYWLAPAYWGKGYATEALRAlldyAFEEL---GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153

                        170
                 ....*....|....*...
gi 515706349 153 TLVRGGVTLEEVRYVWTR 170
Cdd:COG1670  154 ALVIDGRYRDHVLYSLLR 171
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
88-143 5.90e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 55.69  E-value: 5.90e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515706349  88 GEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFYTRFG 143
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-127 3.92e-10

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: 53.05  E-value: 3.92e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515706349  59 VLVAEVDGNVIGWLSLGLCRDTDTpevaSGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLW 127
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGD----TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 46-143 2.49e-09

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: 52.66  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   46 ANWARLIESQDAGVLVAEVDGNVIGWLSLG----LCRdtdtpevasgevmaIYVLADYWGHGIGAQLWQAGFQRLVEQGY 121
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVIALRdrghISL--------------LFVDPDYQGQGIGKALLEAVEDYAEKDGI 85

                          90       100
                  ....*....|....*....|..
gi 515706349  122 KRISLWVLAANQrAVRFYTRFG 143
Cdd:pfam13673  86 KLSELTVNASPY-AVPFYEKLG 106
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 60-143 7.65e-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: 48.48  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   60 LVAEVDGNVIGWLSLGLCRDTdtpevasGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKRISLWVLAANQRAVRFY 139
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDE-------AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALY 106


                  ....
gi 515706349  140 TRFG 143
Cdd:TIGR01575 107 KKLG 110
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
60-143 2.96e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 47.10  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  60 LVAEVDGNVIGWLSLglcRDTDtPEVASGEVMAiyVLADYWGHGIGAQLWQAGFQRLVEQGYKRIslwVLAANQRAVRFY 139
Cdd:COG2153   37 LLAYDDGELVATARL---LPPG-DGEAKIGRVA--VLPEYRGQGLGRALMEAAIEEARERGARRI---VLSAQAHAVGFY 107


                 ....
gi 515706349 140 TRFG 143
Cdd:COG2153  108 EKLG 111
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 73-152 1.05e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 41.93  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   73 SLGLCRDtDTPEVA-------SGEVMAIYVLADYWGHGIGAQLWQAGFQRLVEQGYKrISLWVLAANQRAVRFYTRFGGT 145
Cdd:pfam08445   1 VLGIYRG-DTGELAawclrlpGGELGALQTLPEHRRRGLGSRLVAALARGIAERGIT-PFAVVVAGNTPSRRLYEKLGFR 78


                  ....*..
gi 515706349  146 EDPGSRR 152
Cdd:pfam08445  79 KIDETYW 85
PRK03624 PRK03624
putative acetyltransferase; Provisional
 45-148 1.11e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.99  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  45 EANWARLIESQDAGVLVAEVDGNVIGwlslglcrdtdtpevasgEVMA--------IYVLA---DYWGHGIGAQLWQAGF 113
Cdd:PRK03624  33 EMDIERKLNHDPSLFLVAEVGGEVVG------------------TVMGgydghrgwAYYLAvhpDFRGRGIGRALVARLE 94

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515706349 114 QRLVEQGYKRISLWVLAANQRAVRFYTRFGGTEDP 148
Cdd:PRK03624  95 KKLIARGCPKINLQVREDNDAVLGFYEALGYEEQD 129
PRK10140 PRK10140
N-acetyltransferase;
1-158 1.04e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 40.73  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349   1 MIRDALPKDAKHIAQVHVSswqqayvdlmPADFLASLSTTLPQKEANWARLIESQDAGVLVAEVDGNVIGWLSLGLCRDT 80
Cdd:PRK10140   5 VIRHAETRDYEAIRQIHAQ----------PEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515706349  81 DTPEVASgevMAIYVLADYWGHGIGAQLwqagFQRLVEQ-----GYKRISLWVLAANQRAVRFYTRFGGTEDPGSRRTLV 155
Cdd:PRK10140  75 RRSHVAD---FGICVDSRWKNRGVASAL----MREMIEMcdnwlRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYAL 147


                 ...
gi 515706349 156 RGG 158
Cdd:PRK10140 148 RNG 150
PRK10562 PRK10562
putative acetyltransferase; Provisional
 61-139 1.08e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.44  E-value: 1.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515706349  61 VAEVDGNVIGWLSLglcrdtdtpeVASGEVMAIYVLADYWGHGIGAQLWQAgfqrlVEQGYKRISLWVLAANQRAVRFY 139
Cdd:PRK10562  52 VWEEDGKLLGFVSV----------LEGRFVGALFVAPKAVRRGIGKALMQH-----VQQRYPHLSLEVYQKNQRAVNFY 115
 
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