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Conserved domains on  [gi|15608138|ref|NP_215513|]
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acetyltransferase [Mycobacterium tuberculosis H37Rv]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11504055)

GNAT family N-acetyltransferase which catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate and which binds cAMP; similar to Mycolicibacterium smegmatis acetyltransferase Pat which specifically acetylates the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase

EC:  2.3.1.-
PubMed:  10940244

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 20-132 9.03e-22

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 88.54  E-value: 9.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138  20 VFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPR 98
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELALLGNGPR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15608138  99 SATVTTIEPLTGWTGGRGAFATMVHI-PGVGERLL 132
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEyPELARRLL 115
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 152-290 4.98e-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: 57.70  E-value: 4.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138 152 DGTQLMLRPVLPGDRERtvhgHIQFSGETLYRRFMSARVPSPA-----LMHYLSEVDYVDHFVWVVTDGSD--PVADARF 224
Cdd:COG1670   4 ETERLRLRPLRPEDAEA----LAELLNDPEVARYLPGPPYSLEearawLERLLADWADGGALPFAIEDKEDgeLIGVVGL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608138 225 VRDETDPTVAEIAFTVADAYQGRGIGSFLIGAL-SVAARVDGVERFAARMLSDNVPMRTIMDRYGAV 290
Cdd:COG1670  80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALlDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFR 146
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 20-132 9.03e-22

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 88.54  E-value: 9.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138  20 VFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPR 98
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELALLGNGPR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15608138  99 SATVTTIEPLTGWTGGRGAFATMVHI-PGVGERLL 132
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEyPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 20-139 3.75e-18

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 78.98  E-value: 3.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138     20 VFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPR 98
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGeEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 15608138     99 SATVTTiEPLTGWTGGRGAFATMVHIPGVGERLLRTARQRL 139
Cdd:smart00100  81 AASAAA-VALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 21-139 2.25e-17

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 79.26  E-value: 2.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138  21 FQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDGV-AIIARALPGMIVGEIALLRDSPRS 99
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGReQILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15608138 100 ATVTTIEPLTGWTGGRGAFATMVH-IPGVGERLLRTARQRL 139
Cdd:COG0664  81 ATAEALEDSELLRIPREDLEELLErNPELARALLRLLARRL 121
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 38-107 6.87e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 66.48  E-value: 6.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608138    38 PLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPRSATVTTIEP 107
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGrEQILAVLGPGDFFGELALLGGEPRSATVVALTD 71
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 152-290 4.98e-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: 57.70  E-value: 4.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138 152 DGTQLMLRPVLPGDRERtvhgHIQFSGETLYRRFMSARVPSPA-----LMHYLSEVDYVDHFVWVVTDGSD--PVADARF 224
Cdd:COG1670   4 ETERLRLRPLRPEDAEA----LAELLNDPEVARYLPGPPYSLEearawLERLLADWADGGALPFAIEDKEDgeLIGVVGL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608138 225 VRDETDPTVAEIAFTVADAYQGRGIGSFLIGAL-SVAARVDGVERFAARMLSDNVPMRTIMDRYGAV 290
Cdd:COG1670  80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALlDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFR 146
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 156-290 7.53e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 56.59  E-value: 7.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138   156 LMLRPVLPGDRERTVhghiQFSGETLYRRFMSARVPSPA-----LMHYLSEVDYVDHFVWVVTD-GSDPVADARFVRDET 229
Cdd:pfam13302   2 LLLRPLTEEDAEALF----ELLSDPEVMRYGVPWPLTLEearewLARIWAADEAERGYGWAIELkDTGFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608138   230 DPTVAEIAFTVADAYQGRGIGS-FLIGALSVAARVDGVERFAARMLSDNVPMRTIMDRYGAV 290
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATeAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 209-269 2.64e-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: 38.80  E-value: 2.64e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608138 209 VWVVTDGSDPVADARFVRDETDPTVAEI-AFTVADAYQGRGIGSFLIGALSVAARVDGVERF 269
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGGDTAYIgDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 12-68 5.47e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 41.63  E-value: 5.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15608138   12 VEDLAGMDVFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVS 68
Cdd:PLN02868   7 VEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS 63
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 20-132 9.03e-22

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 88.54  E-value: 9.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138  20 VFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPR 98
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELALLGNGPR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15608138  99 SATVTTIEPLTGWTGGRGAFATMVHI-PGVGERLL 132
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEyPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 20-139 3.75e-18

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 78.98  E-value: 3.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138     20 VFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPR 98
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGeEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 15608138     99 SATVTTiEPLTGWTGGRGAFATMVHIPGVGERLLRTARQRL 139
Cdd:smart00100  81 AASAAA-VALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 21-139 2.25e-17

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 79.26  E-value: 2.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138  21 FQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDGV-AIIARALPGMIVGEIALLRDSPRS 99
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGReQILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15608138 100 ATVTTIEPLTGWTGGRGAFATMVH-IPGVGERLLRTARQRL 139
Cdd:COG0664  81 ATAEALEDSELLRIPREDLEELLErNPELARALLRLLARRL 121
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 38-107 6.87e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 66.48  E-value: 6.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608138    38 PLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDG-VAIIARALPGMIVGEIALLRDSPRSATVTTIEP 107
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGrEQILAVLGPGDFFGELALLGGEPRSATVVALTD 71
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 152-290 4.98e-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: 57.70  E-value: 4.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138 152 DGTQLMLRPVLPGDRERtvhgHIQFSGETLYRRFMSARVPSPA-----LMHYLSEVDYVDHFVWVVTDGSD--PVADARF 224
Cdd:COG1670   4 ETERLRLRPLRPEDAEA----LAELLNDPEVARYLPGPPYSLEearawLERLLADWADGGALPFAIEDKEDgeLIGVVGL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608138 225 VRDETDPTVAEIAFTVADAYQGRGIGSFLIGAL-SVAARVDGVERFAARMLSDNVPMRTIMDRYGAV 290
Cdd:COG1670  80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALlDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFR 146
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 156-290 7.53e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 56.59  E-value: 7.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138   156 LMLRPVLPGDRERTVhghiQFSGETLYRRFMSARVPSPA-----LMHYLSEVDYVDHFVWVVTD-GSDPVADARFVRDET 229
Cdd:pfam13302   2 LLLRPLTEEDAEALF----ELLSDPEVMRYGVPWPLTLEearewLARIWAADEAERGYGWAIELkDTGFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608138   230 DPTVAEIAFTVADAYQGRGIGS-FLIGALSVAARVDGVERFAARMLSDNVPMRTIMDRYGAV 290
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATeAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
156-290 8.06e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 56.93  E-value: 8.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138 156 LMLRPVLPGDRERtVHGHIQFSGETLYRRFMSARVPSPALMHYLSEVDYVDHFVWVVTDGSDPVADARFVRDETDP---T 232
Cdd:COG1247   2 MTIRPATPEDAPA-IAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPayrG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15608138 233 VAEIAFTVADAYQGRGIGSFLIGALSVAARVDGVERFAARMLSDNVPMRTIMDRYGAV 290
Cdd:COG1247  81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 206-269 3.06e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.45  E-value: 3.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608138   206 DHFVWVVTDGSDPVADARFVRDETDPTVAEIAFTVADAYQGRGIGSFLIGALSVAARVDGVERF 269
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLL 65
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 181-281 8.85e-06

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: 44.43  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138   181 LYRRFMSARVPSPALMHYLSEVDYVDHFVWVVTDGSDPVADARFVRDETDPTVAEI-AFTVADAYQGRGIGSFLIGALSV 259
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLE 86

                          90       100
                  ....*....|....*....|..
gi 15608138   260 AARVDGVERFAARMLSDNVPMR 281
Cdd:pfam00583  87 WARERGCERIFLEVAADNLAAI 108
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 209-269 2.64e-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: 38.80  E-value: 2.64e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608138 209 VWVVTDGSDPVADARFVRDETDPTVAEI-AFTVADAYQGRGIGSFLIGALSVAARVDGVERF 269
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGGDTAYIgDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 12-68 5.47e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 41.63  E-value: 5.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15608138   12 VEDLAGMDVFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVS 68
Cdd:PLN02868   7 VEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS 63
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 183-288 2.80e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.34  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608138 183 RRFMSARVPSPAlmhylsEVDYVDHFVWVVTDGSdPVADARFVRdeTDPTVAEIA-FTVADAYQGRGIGSFLIGALSVAA 261
Cdd:COG0454  17 IEALDAELKAME------GSLAGAEFIAVDDKGE-PIGFAGLRR--LDDKVLELKrLYVLPEYRGKGIGKALLEALLEWA 87

                        90       100
                ....*....|....*....|....*..
gi 15608138 262 RVDGVERFAARMLSDNVPMRTIMDRYG 288
Cdd:COG0454  88 RERGCTALELDTLDGNPAAIRFYERLG 114
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 206-268 3.18e-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: 37.28  E-value: 3.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608138 206 DHFVWVVTDGSDPVADARFVRDETDptVAEIA-FTVADAYQGRGIGSFLIGALSVAARVDGVER 268
Cdd:COG1246  27 IGEFWVAEEDGEIVGCAALHPLDED--LAELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKR 88
 
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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