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Conserved domains on  [gi|148236398|ref|NP_001087217|]
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diamine acetyltransferase 1b [Danio rerio]

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];
3-145 4.42e-21

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 84.28  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   3 NFNLRKAEPKDVPDILRLIKE-----LAKYEEMEDQVlitekDLLEDGFGEH--PFYHCVVADVSAEhqkvegysVIGFA 75
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAIlaPGRPVLVAEEDGE--------VVGFA 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236398  76 mYYFTYDPWIG-KLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRGA 145
Cdd:COG1247   68 -SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-145 4.42e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 84.28  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   3 NFNLRKAEPKDVPDILRLIKE-----LAKYEEMEDQVlitekDLLEDGFGEH--PFYHCVVADVSAEhqkvegysVIGFA 75
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAIlaPGRPVLVAEEDGE--------VVGFA 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236398  76 mYYFTYDPWIG-KLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRGA 145
Cdd:COG1247   68 -SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-144 1.88e-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: 66.00  E-value: 1.88e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148236398   71 VIGFAMYYFTYDPWigKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-126 2.89e-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: 48.04  E-value: 2.89e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148236398  71 VIGFAMYYFtyDPWIGKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMH 126
Cdd:cd04301   10 IVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 65-144 1.10e-06

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: 45.40  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   65 KVEGYSVIGFAMYYFTYDPwiGKLLyleDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:TIGR01575  36 ARIGGKVVGYAGVQIVLDE--AHIL---NIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLG 110
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
1-161 6.42e-04

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 37.97  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   1 MANFNLRKAEPKDVPDILRLIKELAKYEemedqvliTEKDLLEDGFG---EHPFYHCVVADVSAEhqkVEGysVIGFAM- 76
Cdd:PRK10146   1 MPACELRPATQYDTDAVYALICELKQAE--------FDHQAFRVGFNanlRDPNMRYHLALLDGE---VVG--MIGLHLq 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398  77 YYFTYDPWIGKllyLEDFYVMKEYRGFGIGSEILKHLSDTAVKnrcssmhfIVAESNKTSIDFyKRRGASDLSLQEGWRL 156
Cdd:PRK10146  68 FHLHHVNWIGE---IQELVVMPQARGLNVGSKLLAWAEEEARQ--------AGAEMTELSTNV-KRHDAHRFYLREGYEQ 135


                 ....*..
gi 148236398 157 --FRIDK 161
Cdd:PRK10146 136 shFRFTK 142
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-145 4.42e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 84.28  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   3 NFNLRKAEPKDVPDILRLIKE-----LAKYEEMEDQVlitekDLLEDGFGEH--PFYHCVVADVSAEhqkvegysVIGFA 75
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAIlaPGRPVLVAEEDGE--------VVGFA 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236398  76 mYYFTYDPWIG-KLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRGA 145
Cdd:COG1247   68 -SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-144 1.88e-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: 66.00  E-value: 1.88e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148236398   71 VIGFAMYYFTYDPWigKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 73-144 1.07e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.14  E-value: 1.07e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148236398  73 GFAMYYFTYDPWIGkllYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:COG0456    1 GFALLGLVDGGDEA---EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-144 2.29e-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: 63.47  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   4 FNLRKAEPKDVPDILRLIKELAkYEEMEDQVLITEKDlledgfGEhpfyhcvvadvsaehqkvegysVIGFAMYYftydP 83
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYA-LEEEIGEFWVAEED------GE----------------------IVGCAALH----P 47

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236398  84 WIGKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSmhfIVAESNKTSIDFYKRRG 144
Cdd:COG1246   48 LDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKR---LFLLTTSAAIHFYEKLG 105
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-144 6.67e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.41  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   6 LRKAEPKDVPDILRLIKElAKYEEMEDQVLiteKDLLEDGfgehPFYHCVVAdvsaehqkVEGYSVIGFAMYYFTYDPWI 85
Cdd:COG3153    1 IRPATPEDAEAIAALLRA-AFGPGREAELV---DRLREDP----AAGLSLVA--------EDDGEIVGHVALSPVDIDGE 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148236398  86 GKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSsmhFIVAESNKTSIDFYKRRG 144
Cdd:COG3153   65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGAR---AVVLLGDPSLLPFYERFG 120
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 6-144 1.22e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 58.91  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   6 LRKAEPKDvpdilrlIKELAKYEEMEDQVLITEKDLLEdgfgehpfYHCVVADVSAEhqkvegysVIGFAMYyFTYDPWI 85
Cdd:COG0454    3 IRKATPED-------INFILLIEALDAELKAMEGSLAG--------AEFIAVDDKGE--------PIGFAGL-RRLDDKV 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148236398  86 GkllYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:COG0454   59 L---ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLG 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-126 2.89e-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: 48.04  E-value: 2.89e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148236398  71 VIGFAMYYFtyDPWIGKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMH 126
Cdd:cd04301   10 IVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-144 7.02e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.83  E-value: 7.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   50 PFYHCVVADVSAEhqkvegysVIGFAMYYFTYDPWIGKLLYLedfYVMKEYRGFGIGSEILKHLSDTAVKNRCssmHFIV 129
Cdd:pfam13508   1 PGGRFFVAEDDGK--------IVGFAALLPLDDEGALAELRL---AVHPEYRGQGIGRALLEAAEAAAKEGGI---KLLE 66

                          90
                  ....*....|....*
gi 148236398  130 AESNKTSIDFYKRRG 144
Cdd:pfam13508  67 LETTNRAAAFYEKLG 81
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 65-144 1.10e-06

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: 45.40  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   65 KVEGYSVIGFAMYYFTYDPwiGKLLyleDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:TIGR01575  36 ARIGGKVVGYAGVQIVLDE--AHIL---NIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLG 110
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-144 3.28e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.66  E-value: 3.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148236398  71 VIGFAMYYftydPWIGKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRG 144
Cdd:COG3393    2 LVAMAGVR----AESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 90-144 7.41e-05

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: 40.33  E-value: 7.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148236398   90 YLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVaESNKTSIDFYKRRG 144
Cdd:pfam13673  53 HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV-NASPYAVPFYEKLG 106
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
1-161 6.42e-04

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 37.97  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   1 MANFNLRKAEPKDVPDILRLIKELAKYEemedqvliTEKDLLEDGFG---EHPFYHCVVADVSAEhqkVEGysVIGFAM- 76
Cdd:PRK10146   1 MPACELRPATQYDTDAVYALICELKQAE--------FDHQAFRVGFNanlRDPNMRYHLALLDGE---VVG--MIGLHLq 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398  77 YYFTYDPWIGKllyLEDFYVMKEYRGFGIGSEILKHLSDTAVKnrcssmhfIVAESNKTSIDFyKRRGASDLSLQEGWRL 156
Cdd:PRK10146  68 FHLHHVNWIGE---IQELVVMPQARGLNVGSKLLAWAEEEARQ--------AGAEMTELSTNV-KRHDAHRFYLREGYEQ 135


                 ....*..
gi 148236398 157 --FRIDK 161
Cdd:PRK10146 136 shFRFTK 142
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-142 2.73e-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: 36.52  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   6 LRKAEPKDVPDILRLI--KELAKYEEMEDQVLITEKDLLE---DGFGEHPFYHCVVADVSAEHqkvegysVIGFAMYYft 80
Cdd:COG1670   10 LRPLRPEDAEALAELLndPEVARYLPGPPYSLEEARAWLErllADWADGGALPFAIEDKEDGE-------LIGVVGLY-- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148236398  81 YDPWIGKLLYLeDFYVMKEYRGFGIGSEILKHLSDTAVKN-RCSSMHFIVAESNKTSIDFYKR 142
Cdd:COG1670   81 DIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEK 142
COG5628 COG5628
Predicted acetyltransferase [General function prediction only];
2-113 3.21e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 444356  Cd Length: 163  Bit Score: 36.45  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236398   2 ANFNLRKAEPKDVPDILRL----IKELAKYeemedqvliTEKDLLEDGFGEHPFYHCVVAD--VSAEHQKVEGySVIGFA 75
Cdd:COG5628    1 MKVSIERVTAEDKPILENLyqlyLHDLSEF---------TGILPDADGLFEYEYLDTYWTDddRHPYLIYVDG-EPAGFA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 148236398  76 MyyftydpwIGKLLYLE------DFYVMKEYRGFGIGSEILKHL 113
Cdd:COG5628   71 L--------VRRLPFLEsdyeiaEFFVLRKYRRKGIGKRAAHEL 106
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
91-144 6.39e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.16  E-value: 6.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148236398  91 LEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSmhfIVAESNKTSIDFYKRRG 144
Cdd:COG2153   61 IGRVAVLPEYRGQGLGRALMEAAIEEARERGARR---IVLSAQAHAVGFYEKLG 111
 
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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