NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1266074337|gb|PGZ72543|]
View 

N-acetyltransferase [Priestia megaterium]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10003213)

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
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
42-160 6.23e-19

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: 78.11  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  42 DLLHFNEHYVQAKGAAFFAAVTENQQVIGTIGLYAYDGRFhalkkryehktaAEIVKCYVDPAYRRLGIGQQLLKAVEQF 121
Cdd:COG1246    13 AILELIRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDL------------AELRSLAVHPDYRGRGIGRRLLEALLAE 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1266074337 122 AQNHFYDTLYLHTHpflPGAIPFWISQGFiERLAEQDEP 160
Cdd:COG1246    81 ARELGLKRLFLLTT---SAAIHFYEKLGF-EEIDKEDLP 115
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
42-160 6.23e-19

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: 78.11  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  42 DLLHFNEHYVQAKGAAFFAAVTENQQVIGTIGLYAYDGRFhalkkryehktaAEIVKCYVDPAYRRLGIGQQLLKAVEQF 121
Cdd:COG1246    13 AILELIRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDL------------AELRSLAVHPDYRGRGIGRRLLEALLAE 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1266074337 122 AQNHFYDTLYLHTHpflPGAIPFWISQGFiERLAEQDEP 160
Cdd:COG1246    81 ARELGLKRLFLLTT---SAAIHFYEKLGF-EEIDKEDLP 115
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
48-150 2.65e-14

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: 65.62  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  48 EHYVQAKGAAFFAAVtENQQVIGTIGLYaydgrfhalkKRYEHKTAAEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFY 127
Cdd:pfam00583  25 EDWDEDASEGFFVAE-EDGELVGFASLS----------IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93
                          90       100
                  ....*....|....*....|...
gi 1266074337 128 DTLYLHTHPFLPGAIPFWISQGF 150
Cdd:pfam00583  94 ERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
59-133 5.30e-11

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: 55.36  E-value: 5.30e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1266074337  59 FAAVTENQQVIGTIGLYAYDGRFHAlkkryehktaAEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLH 133
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDT----------AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
94-153 9.89e-04

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: 37.31  E-value: 9.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  94 AEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHTHPFLPGAIPFWISQGFIER 153
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
101-134 5.25e-03

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 36.06  E-value: 5.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1266074337 101 VDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHT 134
Cdd:PRK10975  134 VFPGAQGRGIGARLMQAALNWCQARGLTRLRVAT 167
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
42-160 6.23e-19

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: 78.11  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  42 DLLHFNEHYVQAKGAAFFAAVTENQQVIGTIGLYAYDGRFhalkkryehktaAEIVKCYVDPAYRRLGIGQQLLKAVEQF 121
Cdd:COG1246    13 AILELIRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDL------------AELRSLAVHPDYRGRGIGRRLLEALLAE 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1266074337 122 AQNHFYDTLYLHTHpflPGAIPFWISQGFiERLAEQDEP 160
Cdd:COG1246    81 ARELGLKRLFLLTT---SAAIHFYEKLGF-EEIDKEDLP 115
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
7-167 1.10e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 67.00  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337   7 YQIKEVKEKDAEVIQFVMNMRNELFPMleknqlsvdllhfnehyVQAKGAAFFAAVTENQQVIGTIGLyaydgrfhalkK 86
Cdd:COG0454     1 MSIRKATPEDINFILLIEALDAELKAM-----------------EGSLAGAEFIAVDDKGEPIGFAGL-----------R 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  87 RYEHKTAaEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHTHPFLPGAIPFWISQGFIERLAEQDEPWNTLHM 166
Cdd:COG0454    53 RLDDKVL-ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEK 131

                  .
gi 1266074337 167 D 167
Cdd:COG0454   132 E 132
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
48-150 2.65e-14

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: 65.62  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  48 EHYVQAKGAAFFAAVtENQQVIGTIGLYaydgrfhalkKRYEHKTAAEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFY 127
Cdd:pfam00583  25 EDWDEDASEGFFVAE-EDGELVGFASLS----------IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93
                          90       100
                  ....*....|....*....|...
gi 1266074337 128 DTLYLHTHPFLPGAIPFWISQGF 150
Cdd:pfam00583  94 ERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
81-170 4.20e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.29  E-value: 4.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  81 FHALKKRYEHKTAaEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHTHPFLPGAIPFWISQGF-IERLAEQDE 159
Cdd:COG0456     2 FALLGLVDGGDEA-EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFeEVGERPNYY 80
                          90
                  ....*....|.
gi 1266074337 160 PWNTLHMDRKI 170
Cdd:COG0456    81 GDDALVMEKEL 91
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
51-170 2.12e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 61.55  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  51 VQAKGAAFFAAVtENQQVIGTIGLYAYDGRfHALKKRYEHKTaaeivkcYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTL 130
Cdd:COG1247    47 ILAPGRPVLVAE-EDGEVVGFASLGPFRPR-PAYRGTAEESI-------YVDPDARGRGIGRALLEALIERARARGYRRL 117
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1266074337 131 YLHTHPFLPGAIPFWISQGF-----IERLAEQDEPW-NTLHMDRKI 170
Cdd:COG1247   118 VAVVLADNEASIALYEKLGFeevgtLPEVGFKFGRWlDLVLMQKRL 163
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
58-150 1.17e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.33  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  58 FFAAVtENQQVIGTIGLYAYDgrfhalkkRYEHKTAAEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHTHpf 137
Cdd:COG3153    41 SLVAE-DDGEIVGHVALSPVD--------IDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD-- 109
                          90
                  ....*....|...
gi 1266074337 138 lPGAIPFWISQGF 150
Cdd:COG3153   110 -PSLLPFYERFGF 121
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
67-169 2.21e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.84  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  67 QVIGTIGLYAYDGRFhalkkryehktaAEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHTHPFLPGAIPFWI 146
Cdd:COG3393     1 ELVAMAGVRAESPGV------------AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYE 68
                          90       100
                  ....*....|....*....|...
gi 1266074337 147 SQGFIERlaeqdEPWNTLHMDRK 169
Cdd:COG3393    69 RLGFRPV-----GEYATVLFRKP 86
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
54-152 2.75e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  54 KGAAFFAAVtENQQVIGTIGLYAYDGRFHALkkryehktaaeIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLH 133
Cdd:pfam13508   1 PGGRFFVAE-DDGKIVGFAALLPLDDEGALA-----------ELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE 68
                          90
                  ....*....|....*....
gi 1266074337 134 THpflPGAIPFWISQGFIE 152
Cdd:pfam13508  69 TT---NRAAAFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
59-133 5.30e-11

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: 55.36  E-value: 5.30e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1266074337  59 FAAVTENQQVIGTIGLYAYDGRFHAlkkryehktaAEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLH 133
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDT----------AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
5-137 1.75e-08

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: 51.15  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337   5 QMYQIKEVKEKDAEVIQFVMN----MRNELFPMLEKNQLSVDLLHFNEHYVQAKGAAFFAAVTENQQVIGTIGLYAYDGR 80
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNdpevARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYDIDRA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1266074337  81 FHalkkryehktAAEIvKCYVDPAYRRLGIGQQLLKAVEQFAQNHF-YDTLYLHTHPF 137
Cdd:COG1670    86 NR----------SAEI-GYWLAPAYWGKGYATEALRALLDYAFEELgLHRVEAEVDPD 132
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
101-152 8.33e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.95  E-value: 8.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1266074337 101 VDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLH--THpflpgAIPFWISQGFIE 152
Cdd:COG2153    66 VLPEYRGQGLGRALMEAAIEEARERGARRIVLSaqAH-----AVGFYEKLGFVP 114
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
54-152 1.99e-06

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: 44.95  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  54 KGAAFFAAVTENQQVIGTIGLyaydgrfhalkKRYEHktaaeIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYL- 132
Cdd:pfam13673  28 QGEYFFFVAFEGGQIVGVIAL-----------RDRGH-----ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELt 91
                          90       100
                  ....*....|....*....|.
gi 1266074337 133 -HTHPFlpgAIPFWISQGFIE 152
Cdd:pfam13673  92 vNASPY---AVPFYEKLGFRA 109
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
101-151 1.92e-04

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 40.97  E-value: 1.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1266074337 101 VDPAYRRLGIGQQLLKAVEQFAQNHFYDtlylhthpFL-------PGAIPFWISQGFI 151
Cdd:COG1444   493 VHPALQRRGLGSRLLAEIREEAKEEGLD--------WLgvsfgatPELLRFWQRNGFV 542
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
94-153 9.89e-04

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: 37.31  E-value: 9.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266074337  94 AEIVKCYVDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHTHPFLPGAIPFWISQGFIER 153
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
101-134 5.25e-03

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 36.06  E-value: 5.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1266074337 101 VDPAYRRLGIGQQLLKAVEQFAQNHFYDTLYLHT 134
Cdd:PRK10975  134 VFPGAQGRGIGARLMQAALNWCQARGLTRLRVAT 167
 
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