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Conserved domains on  [gi|42571719|ref|NP_973950|]
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nuclear shuttle interacting [Arabidopsis thaliana]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
175-254 8.78e-17

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 74.74  E-value: 8.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719 175 KLIGMARATSDHAFN----ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFEADPEGI 250
Cdd:COG3153  49 EIVGHVALSPVDIDGegpaLLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELG 128


                ....
gi 42571719 251 KGMF 254
Cdd:COG3153 129 LTLG 132
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
175-254 8.78e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 74.74  E-value: 8.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719 175 KLIGMARATSDHAFN----ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFEADPEGI 250
Cdd:COG3153  49 EIVGHVALSPVDIDGegpaLLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELG 128


                ....
gi 42571719 251 KGMF 254
Cdd:COG3153 129 LTLG 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 172-244 3.01e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 66.32  E-value: 3.01e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571719   172 QEKKLIGMARAT-SDHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFE 244
Cdd:pfam13508  10 DDGKIVGFAALLpLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 172-228 2.50e-08

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 49.58  E-value: 2.50e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571719 172 QEKKLIGMARATSDHAFN--ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISL 228
Cdd:cd04301   6 DDGEIVGFASLSPDGSGGdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 190-246 8.08e-08

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 50.31  E-value: 8.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571719  190 ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDI---------GNISLFAdsqvvdFYQNLGF-EAD 246
Cdd:PRK09491  64 ATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVatlwlevraSNAAAIA------LYESLGFnEVT 124
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 188-244 4.74e-07

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: 47.71  E-value: 4.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719   188 FNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISL---FADSQVVDFYQNLGFE 244
Cdd:TIGR01575  53 DEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLevrVSNIAAQALYKKLGFN 112
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
175-254 8.78e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 74.74  E-value: 8.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719 175 KLIGMARATSDHAFN----ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFEADPEGI 250
Cdd:COG3153  49 EIVGHVALSPVDIDGegpaLLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELG 128


                ....
gi 42571719 251 KGMF 254
Cdd:COG3153 129 LTLG 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
175-244 5.94e-15

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 68.01  E-value: 5.94e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571719 175 KLIGMARATSDHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQ---VVDFYQNLGFE 244
Cdd:COG3393   1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADnpaARRLYERLGFR 73
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 172-244 3.01e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 66.32  E-value: 3.01e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571719   172 QEKKLIGMARAT-SDHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFE 244
Cdd:pfam13508  10 DDGKIVGFAALLpLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 172-252 7.69e-13

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: 63.83  E-value: 7.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719   172 QEKKLIGMARA-TSDHafnatIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQV--VDFYQNLGFEA-DP 247
Cdd:pfam13673  38 EGGQIVGVIALrDRGH-----ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPyaVPFYEKLGFRAtGP 112


                  ....*
gi 42571719   248 EGIKG 252
Cdd:pfam13673 113 EQEFN 117
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 173-243 1.25e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 62.92  E-value: 1.25e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571719   173 EKKLIGMARATS--DHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADS---QVVDFYQNLGF 243
Cdd:pfam00583  41 DGELVGFASLSIidDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAAdnlAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 175-244 2.00e-12

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: 2.00e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719 175 KLIGMARATSDHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFE 244
Cdd:COG1246  38 EIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFE 107
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
172-248 2.59e-12

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 62.51  E-value: 2.59e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571719 172 QEKKLIGMARATSDHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFEADPE 248
Cdd:COG2153  41 DDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGE 117
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 190-248 4.41e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.44  E-value: 4.41e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571719 190 ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADS---QVVDFYQNLGFEADPE 248
Cdd:COG0456  14 AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREdneAAIALYEKLGFEEVGE 75
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 173-245 1.18e-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: 1.18e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571719 173 EKKLIGMARAT---SDHAFnatIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLF---ADSQVVDFYQNLGFEA 245
Cdd:COG0454  42 KGEPIGFAGLRrldDKVLE---LKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDtldGNPAAIRFYERLGFKE 117
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
175-256 1.72e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.39  E-value: 1.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719 175 KLIGMARATSDHAFNATIW----DVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISL--FADSQV-VDFYQNLGFEADP 247
Cdd:COG1247  62 EVVGFASLGPFRPRPAYRGtaeeSIYVDPDARGRGIGRALLEALIERARARGYRRLVAvvLADNEAsIALYEKLGFEEVG 141

                        90
                ....*....|...
gi 42571719 248 E----GIKGMFWY 256
Cdd:COG1247 142 TlpevGFKFGRWL 154
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 172-228 2.50e-08

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 49.58  E-value: 2.50e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571719 172 QEKKLIGMARATSDHAFN--ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISL 228
Cdd:cd04301   6 DDGEIVGFASLSPDGSGGdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 190-246 8.08e-08

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 50.31  E-value: 8.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571719  190 ATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDI---------GNISLFAdsqvvdFYQNLGF-EAD 246
Cdd:PRK09491  64 ATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVatlwlevraSNAAAIA------LYESLGFnEVT 124
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 188-244 4.74e-07

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: 47.71  E-value: 4.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719   188 FNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISL---FADSQVVDFYQNLGFE 244
Cdd:TIGR01575  53 DEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLevrVSNIAAQALYKKLGFN 112
PRK03624 PRK03624
putative acetyltransferase; Provisional
 197-247 1.89e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 1.89e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42571719  197 VDPEYQGQGLGKALVEKLVRALLQRDIGNISLF---ADSQVVDFYQNLGFEADP 247
Cdd:PRK03624  76 VHPDFRGRGIGRALVARLEKKLIARGCPKINLQvreDNDAVLGFYEALGYEEQD 129
PTZ00330 PTZ00330
acetyltransferase; Provisional
 192-245 3.50e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 45.60  E-value: 3.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42571719  192 IWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFEA 245
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFRA 138
PRK07757 PRK07757
N-acetyltransferase;
197-244 2.05e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 43.64  E-value: 2.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 42571719  197 VDPEYQGQGLGKALVEKLVRALlqRDIGNISLFADSQVVDFYQNLGFE 244
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEA--RELGVKRVFALTYQPEFFEKLGFR 118
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 175-250 1.79e-03

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: 38.06  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571719 175 KLIGMARATSDHAFNATI-WDVLVDPEYQGQGLGKALVEKLVR-ALLQRDIGNISLFAD-----SQVVdfYQNLGFEadP 247
Cdd:COG1670  72 ELIGVVGLYDIDRANRSAeIGYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDpdntaSIRV--LEKLGFR--L 147


                ...
gi 42571719 248 EGI 250
Cdd:COG1670 148 EGT 150
PRK10514 PRK10514
putative acetyltransferase; Provisional
 197-244 1.91e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 1.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 42571719  197 VDPEYQGQGLGKALVEK-LVRA-LLQRDIGNislfADSQVVDFYQNLGFE 244
Cdd:PRK10514  77 VDPDVRGCGVGRMLVEHaLSLHpELTTDVNE----QNEQAVGFYKKMGFK 122
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
197-215 2.85e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 35.90  E-value: 2.85e-03
                        10
                ....*....|....*....
gi 42571719 197 VDPEYQGQGLGKALVEKLV 215
Cdd:COG2388  40 VPPALRGQGIASALVEAAL 58
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 192-243 5.81e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 36.22  E-value: 5.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42571719  192 IWDVLVDPEYQGQGLGKALVEKLVRAllQRDIGNISLFADSQV--VDFYQNLGF 243
Cdd:PLN02706  88 IEDVVVDSAARGKGLGKKIIEALTEH--ARSAGCYKVILDCSEenKAFYEKCGY 139
Eis COG4552
Predicted acetyltransferase [General function prediction only];
192-244 8.27e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.19  E-value: 8.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571719 192 IWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGnIS-LFADSQvvDFYQNLGFE 244
Cdd:COG4552  75 ITGVAVAPEHRRRGVARALLREALAELRERGQP-LSaLYPFEP--GFYRRFGYE 125
 
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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