NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1052869945|emb|SCJ12421|]
View 

Spermidine N(1)-acetyltransferase [uncultured Flavonifractor sp.]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 2-163 1.37e-37

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK10140:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 162  Bit Score: 126.63  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   2 EYSIRPIGPQDAEGFNALRRMPGVFENTLGLPSERVKRNQDGIASlGPDDHNFVAVTpDGTVIGVVGLKVRPQLRMRHTA 81
Cdd:PRK10140    3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD-RPGIKQLVACI-DGDVVGHLTIDVQQRPRRSHVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  82 DVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVDEYVMAR 161
Cdd:PRK10140   81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                  ..
gi 1052869945 162 LR 163
Cdd:PRK10140  161 VK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
2-163 1.37e-37

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 126.63  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   2 EYSIRPIGPQDAEGFNALRRMPGVFENTLGLPSERVKRNQDGIASlGPDDHNFVAVTpDGTVIGVVGLKVRPQLRMRHTA 81
Cdd:PRK10140    3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD-RPGIKQLVACI-DGDVVGHLTIDVQQRPRRSHVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  82 DVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVDEYVMAR 161
Cdd:PRK10140   81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                  ..
gi 1052869945 162 LR 163
Cdd:PRK10140  161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-164 6.28e-37

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: 125.11  E-value: 6.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   5 IRPIGPQDAEGFNALRRMPGVFENTLGLPS------ERVKRNQDGIASlgPDDHNFVAV-TPDGTVIGVVGLKVRPqlRM 77
Cdd:COG1670    10 LRPLRPEDAEALAELLNDPEVARYLPGPPYsleearAWLERLLADWAD--GGALPFAIEdKEDGELIGVVGLYDID--RA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  78 RHTADVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVDEY 157
Cdd:COG1670    86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                  ....*..
gi 1052869945 158 VMARLRP 164
Cdd:COG1670   166 LYSLLRE 172
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 49-137 7.95e-20

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: 79.87  E-value: 7.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  49 PDDHNFVAVTpDGTVIGVVGLKVRPQLRmRHTADVGIFVHTDWQGKGVGTALMQTVLDLADNWLmLVRVELEVFTDNVKA 128
Cdd:pfam00583  31 ASEGFFVAEE-DGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAA 107


                  ....*....
gi 1052869945 129 IHLYEKLGF 137
Cdd:pfam00583 108 IALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 60-144 3.24e-11

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: 57.72  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  60 DGTVIGVVGLKVrpqlrMRHTADV-GIFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDNVKAIHLYEKLGFE 138
Cdd:TIGR01575  39 GGKVVGYAGVQI-----VLDEAHIlNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKKLGFN 112


                  ....*.
gi 1052869945 139 KEGCKR 144
Cdd:TIGR01575 113 EIAIRR 118
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-111 8.55e-07

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 44.19  E-value: 8.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052869945  54 FVAVTPDGTVIGVVGLKVRPQlrMRHTADVG-IFVHTDWQGKGVGTALMQTVLDLADNW 111
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGS--GGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
2-163 1.37e-37

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 126.63  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   2 EYSIRPIGPQDAEGFNALRRMPGVFENTLGLPSERVKRNQDGIASlGPDDHNFVAVTpDGTVIGVVGLKVRPQLRMRHTA 81
Cdd:PRK10140    3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD-RPGIKQLVACI-DGDVVGHLTIDVQQRPRRSHVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  82 DVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVDEYVMAR 161
Cdd:PRK10140   81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                  ..
gi 1052869945 162 LR 163
Cdd:PRK10140  161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-164 6.28e-37

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: 125.11  E-value: 6.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   5 IRPIGPQDAEGFNALRRMPGVFENTLGLPS------ERVKRNQDGIASlgPDDHNFVAV-TPDGTVIGVVGLKVRPqlRM 77
Cdd:COG1670    10 LRPLRPEDAEALAELLNDPEVARYLPGPPYsleearAWLERLLADWAD--GGALPFAIEdKEDGELIGVVGLYDID--RA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  78 RHTADVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVDEY 157
Cdd:COG1670    86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                  ....*..
gi 1052869945 158 VMARLRP 164
Cdd:COG1670   166 LYSLLRE 172
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-162 7.17e-26

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 96.60  E-value: 7.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   2 EYSIRPIGPQDAEGFNALRR-----MPGVFENTLGLPSERVKRnqdgIASLGPDDHNFVAVTPDGTVIGVVGL-KVRPQL 75
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNeaiaeGTATFETEPPSEEEREAW----FAAILAPGRPVLVAEEDGEVVGFASLgPFRPRP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  76 RMRHTADVGIFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVD 155
Cdd:COG1247    77 AYRGTAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLD 155


                  ....*..
gi 1052869945 156 EYVMARL 162
Cdd:COG1247   156 LVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 49-137 7.95e-20

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: 79.87  E-value: 7.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  49 PDDHNFVAVTpDGTVIGVVGLKVRPQLRmRHTADVGIFVHTDWQGKGVGTALMQTVLDLADNWLmLVRVELEVFTDNVKA 128
Cdd:pfam00583  31 ASEGFFVAEE-DGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAA 107


                  ....*....
gi 1052869945 129 IHLYEKLGF 137
Cdd:pfam00583 108 IALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 85-161 5.11e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.30  E-value: 5.11e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052869945  85 IFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDNVKAIHLYEKLGFEKEGckrmtTVRNGRYVDEYVMAR 161
Cdd:COG0456    19 LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVG-----ERPNYYGDDALVMEK 89
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 3-156 1.45e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 69.31  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   3 YSIRPIGPQDAEGFNALRRMpgvfentlglpSERVKRnqdgIASLGPDDHnFVAVTPDGTVIGVVGLKVRPQlrmrHTAD 82
Cdd:COG0454     1 MSIRKATPEDINFILLIEAL-----------DAELKA----MEGSLAGAE-FIAVDDKGEPIGFAGLRRLDD----KVLE 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052869945  83 VG-IFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDNVKAIHLYEKLGFEKEGckRMTTVRNGRYVDE 156
Cdd:COG0454    61 LKrLYVLPEYRGKGIGKALLEALLEWARE-RGCTALELDTLDGNPAAIRFYERLGFKEIE--RYVAYVGGEFEKE 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-139 8.71e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 65.55  E-value: 8.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  49 PDDHNFVAVTpDGTVIGVVGLkvRPQLRMRHTADVGIFVHTDWQGKGVGTALMQTVLDLADNWlmlvRVELEVFTDNVKA 128
Cdd:pfam13508   1 PGGRFFVAED-DGKIVGFAAL--LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEG----GIKLLELETTNRA 73

                          90
                  ....*....|.
gi 1052869945 129 IHLYEKLGFEK 139
Cdd:pfam13508  74 AAFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-161 1.22e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   5 IRPIGPQDAEGFNALRRmpgvfentLGLPSERVKRNQDGIASLGPDDHNFVAVTpDGTVIGVVGLKVRPQLRMRHTADVG 84
Cdd:COG3153     1 IRPATPEDAEAIAALLR--------AAFGPGREAELVDRLREDPAAGLSLVAED-DGEIVGHVALSPVDIDGEGPALLLG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052869945  85 -IFVHTDWQGKGVGTALMQTVLDLADNwlmLVRVELEVFTDNvKAIHLYEKLGFEkegckRMTTVRNGRYVDEYVMAR 161
Cdd:COG3153    72 pLAVDPEYRGQGIGRALMRAALEAARE---RGARAVVLLGDP-SLLPFYERFGFR-----PAGELGLTLGPDEVFLAK 140
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 5-138 2.02e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 66.22  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   5 IRPIGPQDAEGFNALRRMPGVFENTLGLPS--ERVKRNQDGIASLGPDDH--NFVAVTPDGTVIGVVGLkvRPQLRMRHT 80
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLtlEEAREWLARIWAADEAERgyGWAIELKDTGFIGSIGL--YDIDGEPER 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052869945  81 ADVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFE 138
Cdd:pfam13302  82 AELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 47-138 3.71e-13

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: 62.70  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  47 LGPDDHNFVAVTPDGTVIGVVGLKVRPQlrmrHTADVG-IFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDn 125
Cdd:COG1246    23 LEEEIGEFWVAEEDGEIVGCAALHPLDE----DLAELRsLAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLTTSA- 96

                          90
                  ....*....|...
gi 1052869945 126 vkAIHLYEKLGFE 138
Cdd:COG1246    97 --AIHFYEKLGFE 107
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 52-155 2.76e-11

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: 57.67  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  52 HNFVAVTpDGTVIGVVGLKVRPQLRMrhtadvgIFVHTDWQGKGVGTALMQTVLDLADNWLmLVRVELEVFTDNVkAIHL 131
Cdd:pfam13673  32 FFFVAFE-GGQIVGVIALRDRGHISL-------LFVDPDYQGQGIGKALLEAVEDYAEKDG-IKLSELTVNASPY-AVPF 101

                          90       100
                  ....*....|....*....|....
gi 1052869945 132 YEKLGFEKEGckRMTTVRNGRYVD 155
Cdd:pfam13673 102 YEKLGFRATG--PEQEFNGIRFVP 123
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 60-144 3.24e-11

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: 57.72  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  60 DGTVIGVVGLKVrpqlrMRHTADV-GIFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDNVKAIHLYEKLGFE 138
Cdd:TIGR01575  39 GGKVVGYAGVQI-----VLDEAHIlNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKKLGFN 112


                  ....*.
gi 1052869945 139 KEGCKR 144
Cdd:TIGR01575 113 EIAIRR 118
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
63-138 2.28e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.14  E-value: 2.28e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052869945  63 VIGVVGLKVRPQlrmRHTADVGIFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDNVKAIHLYEKLGFE 138
Cdd:COG3393     2 LVAMAGVRAESP---GVAEISGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFR 73
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 60-160 2.92e-10

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 55.44  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  60 DGTVIGVVGLkVRPQLRMRHtADVGIFVHTDWQGkGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEK 139
Cdd:TIGR03585  59 ESRPIGVISF-TDINLVHKS-AFWGIYANPFCKP-GVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFER 135

                          90       100
                  ....*....|....*....|.
gi 1052869945 140 EGCKRmttvRNGRYVDEYVMA 160
Cdd:TIGR03585 136 EGVFR----QGGEYYDVLLMY 152
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 54-141 3.69e-08

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 50.57  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  54 FVaVTPDGTVIGVVGLKVRPQLRMRhtADVGIFVHTDWQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYE 133
Cdd:PRK15130   60 FV-VECDGEKAGLVELVEINHVHRR--AEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYR 136


                  ....*...
gi 1052869945 134 KLGFEKEG 141
Cdd:PRK15130  137 KLGFEVEG 144
PRK10562 PRK10562
putative acetyltransferase; Provisional
 85-142 1.24e-07

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 48.53  E-value: 1.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052869945  85 IFVHTDWQGKGVGTALMQTVLDLADnWLMLvrvelEVFTDNVKAIHLYEKLGFEKEGC 142
Cdd:PRK10562   74 LFVAPKAVRRGIGKALMQHVQQRYP-HLSL-----EVYQKNQRAVNFYHAQGFRIVDS 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-111 8.55e-07

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 44.19  E-value: 8.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052869945  54 FVAVTPDGTVIGVVGLKVRPQlrMRHTADVG-IFVHTDWQGKGVGTALMQTVLDLADNW 111
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGS--GGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER 57
PRK03624 PRK03624
putative acetyltransferase; Provisional
 87-140 3.37e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 44.15  E-value: 3.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1052869945  87 VHTDWQGKGVGTALMQTvldlADNWLM---LVRVELEVFTDNVKAIHLYEKLGFEKE 140
Cdd:PRK03624   76 VHPDFRGRGIGRALVAR----LEKKLIargCPKINLQVREDNDAVLGFYEALGYEEQ 128
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 85-137 9.83e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.99  E-value: 9.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052869945  85 IFVHTDWQGKGVGTALMQTVLD------LADNWLmlvrvelEVFTDNVKAIHLYEKLGF 137
Cdd:PRK09491   69 IAVDPDYQRQGLGRALLEHLIDelekrgVATLWL-------EVRASNAAAIALYESLGF 120
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
60-141 3.29e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 41.32  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  60 DGTVIGVvglkvrpqLRMRHTAD----VG-IFVHTDWQGKGVGTALMQTVLDLADNwLMLVRVELEVFTDnvkAIHLYEK 134
Cdd:COG2153    42 DGELVAT--------ARLLPPGDgeakIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSAQAH---AVGFYEK 109


                  ....*..
gi 1052869945 135 LGFEKEG 141
Cdd:COG2153   110 LGFVPVG 116
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
5-156 2.53e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 39.27  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945   5 IRPIGPQDAEGFNALRRMPGV--------FENTLglpsERVKRNQDGIASLGpddHNFVAVTPDGTVIGVVGLKVrPQLR 76
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVnpaftqeyAHSSI----EEFETFLAAYLSPG---EIVFGVAESDRLIGYATLRQ-FDYV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  77 MRHTADVGIFVHTDwQGKGVGTALMQTVLDLADNWLMLVRVELEVFTDNVKAIHLYEKLGFEKEGCKRMTTVRNGRYVDE 156
Cdd:pfam13420  73 KTHKAELSFYVVKN-NDEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDM 151
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
45-137 2.68e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 39.53  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  45 ASLGPDDHN-FVAVTPDGTVIGVVGLKVRPQlrmrHTADVGIF-VHTDWQGKGVGTALMQtvldLADNW-----LMLVRV 117
Cdd:PRK10975   94 AVRGTFDHQcLLLRDASGQIQGFVTLRELND----TDARIGLLaVFPGAQGRGIGARLMQ----AALNWcqargLTRLRV 165

                          90       100
                  ....*....|....*....|
gi 1052869945 118 ELEvfTDNVKAIHLYEKLGF 137
Cdd:PRK10975  166 ATQ--MGNLAALRLYIRSGA 183
PRK07757 PRK07757
N-acetyltransferase;
53-140 3.45e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.94  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869945  53 NFVAVTPDGTVIGVVGLKVrpqlrmrHTADV----GIFVHTDWQGKGVGTALMQTVLDLAdnwlmlvrVEL---EVFTDN 125
Cdd:PRK07757   42 DFYVAEEEGEIVGCCALHI-------LWEDLaeirSLAVSEDYRGQGIGRMLVEACLEEA--------RELgvkRVFALT 106

                          90
                  ....*....|....*...
gi 1052869945 126 VKAiHLYEKLGF---EKE 140
Cdd:PRK07757  107 YQP-EFFEKLGFrevDKE 123
 
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