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Conserved domains on  [gi|730813|sp|P39624|]
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RecName: Full=Spore coat polysaccharide biosynthesis protein SpsD

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

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
141-272 1.20e-15

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 72.72  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   141 PPEPGDTEAICELARDSF--TKSRYFQDPHlsrdaANEIFQEWTRNNLNGRAAVnIVAKHNGEVIGYL-----QGLSRDD 213
Cdd:COG1247   6 PATPEDAPAIAAIYNEAIaeGTATFETEPP-----SEEEREAWFAAILAPGRPV-LVAEEDGEVVGFAslgpfRPRPAYR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 730813   214 ECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGFT 272
Cdd:COG1247  80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
141-272 1.20e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 72.72  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   141 PPEPGDTEAICELARDSF--TKSRYFQDPHlsrdaANEIFQEWTRNNLNGRAAVnIVAKHNGEVIGYL-----QGLSRDD 213
Cdd:COG1247   6 PATPEDAPAIAAIYNEAIaeGTATFETEPP-----SEEEREAWFAAILAPGRPV-LVAEEDGEVVGFAslgpfRPRPAYR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 730813   214 ECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGFT 272
Cdd:COG1247  80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 148-271 4.43e-15

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: 69.85  E-value: 4.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     148 EAICELARDSFTKSRyfqdphlsRDAANEIFQEWTRNNLNGRaavnIVAKHNGEVIGYLQGLSRDDE---CILDLMAVKP 224
Cdd:pfam00583   2 EALYELLSEEFPEPW--------PDEPLDLLEDWDEDASEGF----FVAEEDGELVGFASLSIIDDEppvGEIEGLAVAP 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 730813     225 GFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGF 271
Cdd:pfam00583  70 EYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 181-279 4.56e-09

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 53.87  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     181 WTR----NNLNGRAAVNIVAKHNGEVIGYLQGLSRDDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQ 256
Cdd:TIGR01575  17 WTEaqfaEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVR 96

                          90       100
                  ....*....|....*....|....*
gi 730813     257 LHNVRAIRLYERMGFT--AEQSYYY 279
Cdd:TIGR01575  97 VSNIAAQALYKKLGFNeiAIRRNYY 121
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
143-279 2.42e-06

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 47.23  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813    143 EPGDTEAICELARDSFTKSRyFQDPHLSRDAANEIFQEWTRNnlngraAVN-------IVAKH-NGEVIGY--LQGLSrD 212
Cdd:PRK10975  53 TETDIPALRQLAAQAFAQSR-FRAPWYAPDDSGRFYAQWIEN------AVRgtfdhqcLLLRDaSGQIQGFvtLRELN-D 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730813    213 DECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGFTAEQSYYY 279
Cdd:PRK10975 125 TDARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGANIESTAYW 191
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 194-252 6.07e-05

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: 40.34  E-value: 6.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730813   194 IVAKHNGEVIGYLQGL---SRDDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVT 252
Cdd:cd04301   2 LVAEDDGEIVGFASLSpdgSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
141-272 1.20e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 72.72  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   141 PPEPGDTEAICELARDSF--TKSRYFQDPHlsrdaANEIFQEWTRNNLNGRAAVnIVAKHNGEVIGYL-----QGLSRDD 213
Cdd:COG1247   6 PATPEDAPAIAAIYNEAIaeGTATFETEPP-----SEEEREAWFAAILAPGRPV-LVAEEDGEVVGFAslgpfRPRPAYR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 730813   214 ECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGFT 272
Cdd:COG1247  80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 148-271 4.43e-15

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: 69.85  E-value: 4.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     148 EAICELARDSFTKSRyfqdphlsRDAANEIFQEWTRNNLNGRaavnIVAKHNGEVIGYLQGLSRDDE---CILDLMAVKP 224
Cdd:pfam00583   2 EALYELLSEEFPEPW--------PDEPLDLLEDWDEDASEGF----FVAEEDGELVGFASLSIIDDEppvGEIEGLAVAP 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 730813     225 GFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGF 271
Cdd:pfam00583  70 EYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 141-274 9.94e-14

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: 67.72  E-value: 9.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   141 PPEPGDTEAICELARDSFTkSRYFQDPHLSRDAANEIFQEWTRNNLNGRAAV-NIVAKHNGEVIGYLqGLSRDDEC--IL 217
Cdd:COG1670  12 PLRPEDAEALAELLNDPEV-ARYLPGPPYSLEEARAWLERLLADWADGGALPfAIEDKEDGELIGVV-GLYDIDRAnrSA 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 730813   218 DL-MAVKPGFEGKRIAFHLLANLIEQ-PETQKHRTVTAGTQLHNVRAIRLYERMGFTAE 274
Cdd:COG1670  90 EIgYWLAPAYWGKGYATEALRALLDYaFEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 204-284 2.75e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 56.20  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   204 GYLQG--LSRDDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGFTAEQSYYYYH 281
Cdd:COG0456   1 GFALLglVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80


                ...
gi 730813   282 IWP 284
Cdd:COG0456  81 GDD 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 194-272 3.88e-10

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: 56.54  E-value: 3.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   194 IVAKHNGEVIGYLqGLSRDDE--CILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTqlhNVRAIRLYERMGF 271
Cdd:COG1246  31 WVAEEDGEIVGCA-ALHPLDEdlAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGF 106


                .
gi 730813   272 T 272
Cdd:COG1246 107 E 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 194-280 1.90e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.06  E-value: 1.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   194 IVAKHNGEVIGYLqGLSR--DDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGF 271
Cdd:COG0454  37 IAVDDKGEPIGFA-GLRRldDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGF 115


                ....*....
gi 730813   272 TAEQSYYYY 280
Cdd:COG0454 116 KEIERYVAY 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
143-287 3.96e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 54.32  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   143 EPGDTEAICELARDSFtksryfqdphlSRDAANEIFQEWTRNNLNGRAavnIVAKHNGEVIGYLQG-----LSRDDECIL 217
Cdd:COG3153   5 TPEDAEAIAALLRAAF-----------GPGREAELVDRLREDPAAGLS---LVAEDDGEIVGHVALspvdiDGEGPALLL 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730813   218 DLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTqlhNVRAIRLYERMGFTAEQSY----YYYHIWPGKE 287
Cdd:COG3153  71 GPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGELgltlGPDEVFLAKE 141
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 194-272 4.47e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 4.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     194 IVAKHNGEVIGYLQGLSRDDECIL--DLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTqlhNVRAIRLYERMGF 271
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLGF 82


                  .
gi 730813     272 T 272
Cdd:pfam13508  83 E 83
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 181-279 4.56e-09

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 53.87  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     181 WTR----NNLNGRAAVNIVAKHNGEVIGYLQGLSRDDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQ 256
Cdd:TIGR01575  17 WTEaqfaEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVR 96

                          90       100
                  ....*....|....*....|....*
gi 730813     257 LHNVRAIRLYERMGFT--AEQSYYY 279
Cdd:TIGR01575  97 VSNIAAQALYKKLGFNeiAIRRNYY 121
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
191-274 7.95e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.18  E-value: 7.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   191 AVNIVAKHNGEVIGYLqglsR-----DDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHnvrAIRL 265
Cdd:COG2153  34 ARHLLAYDDGELVATA----RllppgDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGF 106


                ....*....
gi 730813   266 YERMGFTAE 274
Cdd:COG2153 107 YEKLGFVPV 115
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 141-272 7.54e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 47.73  E-value: 7.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     141 PPEPGDTEAICELARDSfTKSRYFQDPHLSRDAANEIFQEWTRNNLNGRAAV-NIVAKHNGEV--IGYLQGLSRDDECIL 217
Cdd:pfam13302   6 PLTEEDAEALFELLSDP-EVMRYGVPWPLTLEEAREWLARIWAADEAERGYGwAIELKDTGFIgsIGLYDIDGEPERAEL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 730813     218 DLMaVKPGFEGKRIAFHLLANLIEQ--PETQKHRtVTAGTQLHNVRAIRLYERMGFT 272
Cdd:pfam13302  85 GYW-LGPDYWGKGYATEAVRALLEYafEELGLPR-LVARIDPENTASRRVLEKLGFK 139
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
143-279 2.42e-06

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 47.23  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813    143 EPGDTEAICELARDSFTKSRyFQDPHLSRDAANEIFQEWTRNnlngraAVN-------IVAKH-NGEVIGY--LQGLSrD 212
Cdd:PRK10975  53 TETDIPALRQLAAQAFAQSR-FRAPWYAPDDSGRFYAQWIEN------AVRgtfdhqcLLLRDaSGQIQGFvtLRELN-D 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730813    213 DECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGFTAEQSYYY 279
Cdd:PRK10975 125 TDARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGANIESTAYW 191
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
190-282 9.54e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 9.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813   190 AAVNIVAKHNGEVIGylqglsrddecildlMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERM 269
Cdd:COG3393   6 AGVRAESPGVAEISG---------------VYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERL 70

                        90
                ....*....|...
gi 730813   270 GFTAEQSYYYYHI 282
Cdd:COG3393  71 GFRPVGEYATVLF 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 194-252 6.07e-05

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: 40.34  E-value: 6.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730813   194 IVAKHNGEVIGYLQGL---SRDDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVT 252
Cdd:cd04301   2 LVAEDDGEIVGFASLSpdgSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 194-273 6.37e-04

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: 38.79  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813     194 IVAKHNGEVIGYLqglSRDDECILDLMAVKPGFEGKRIAFHLLANLIEQPETQ--KHRTVTAGTQLHnvrAIRLYERMGF 271
Cdd:pfam13673  34 FVAFEGGQIVGVI---ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDgiKLSELTVNASPY---AVPFYEKLGF 107


                  ..
gi 730813     272 TA 273
Cdd:pfam13673 108 RA 109
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 213-278 1.48e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 38.37  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730813    213 DECILDLMAVKPGFEGKRIAFHLLANLIEQPETQKHRTVTAGTQLHNVRAIRLYERMGF---TAEQSYY 278
Cdd:PRK09491  62 DEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFnevTIRRNYY 130
PRK10562 PRK10562
putative acetyltransferase; Provisional
 141-278 8.74e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.81  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730813    141 PPEPGDTEAICELARDSFTKSRYFQDPHLSRDAANEIfqewtRNNLNGrAAVNIVAKHNGEVIGYLQGLsrdDECILDLM 220
Cdd:PRK10562   4 EYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLV-----RDVYLP-AAQTWVWEEDGKLLGFVSVL---EGRFVGAL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 730813    221 AVKPGFEGKRIAFHLLANLieqpeTQKHRTVTAGTQLHNVRAIRLYERMGFTAEQSYY 278
Cdd:PRK10562  75 FVAPKAVRRGIGKALMQHV-----QQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAW 127
 
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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