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Conserved domains on  [gi|505190002|ref|WP_015377104|]
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MULTISPECIES: GNAT family N-acetyltransferase [Serratia]

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];
1-170 2.97e-17

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.26  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   1 MFTVRQALLEDLTLVRDI---GIRTYRAHFGELWRYPHELEAFLAEdfsvsaldqtLRQPDVCWLLAYEDDALVGYARVN 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneAIAEGTATFETEPPSEEEREAWFAA----------ILAPGRPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  78 FDSLLAPTEQIgAELQkIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQGLSMCGEtcYTSA 157
Cdd:COG1247   71 PFRPRPAYRGT-AEES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGT--LPEV 146

                        170
                 ....*....|....*..
gi 505190002 158 QGSIGIW----YMSKAL 170
Cdd:COG1247  147 GFKFGRWldlvLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-170 2.97e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.26  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   1 MFTVRQALLEDLTLVRDI---GIRTYRAHFGELWRYPHELEAFLAEdfsvsaldqtLRQPDVCWLLAYEDDALVGYARVN 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneAIAEGTATFETEPPSEEEREAWFAA----------ILAPGRPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  78 FDSLLAPTEQIgAELQkIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQGLSMCGEtcYTSA 157
Cdd:COG1247   71 PFRPRPAYRGT-AEES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGT--LPEV 146

                        170
                 ....*....|....*..
gi 505190002 158 QGSIGIW----YMSKAL 170
Cdd:COG1247  147 GFKFGRWldlvLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 43-145 1.08e-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: 66.39  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   43 EDFSVSALDQTLRQPDVCWLLAYEDDALVGYARVNFDsllaPTEQIGAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQ 122
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSII----DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92

                          90       100
                  ....*....|....*....|...
gi 505190002  123 QKTLWLEVLQRNTGAQRFYQRQG 145
Cdd:pfam00583  93 CERIFLEVAADNLAAIALYEKLG 115
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-145 1.81e-12

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: 60.81  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   54 LRQPDVCWLLAYEDDALVGYARVNFDsllaPTEqigAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQR 133
Cdd:TIGR01575  26 LANYHLCYLLARIGGKVVGYAGVQIV----LDE---AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVS 98

                          90
                  ....*....|..
gi 505190002  134 NTGAQRFYQRQG 145
Cdd:TIGR01575  99 NIAAQALYKKLG 110
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-129 6.36e-07

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 44.57  E-value: 6.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190002  61 WLLAYEDDALVGYARVNFDSLLAPTeqigAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLE 129
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDT----AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 90-145 7.79e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.08  E-value: 7.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505190002  90 AELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQG 145
Cdd:PRK09491  64 ATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLG 119
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-170 2.97e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.26  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   1 MFTVRQALLEDLTLVRDI---GIRTYRAHFGELWRYPHELEAFLAEdfsvsaldqtLRQPDVCWLLAYEDDALVGYARVN 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneAIAEGTATFETEPPSEEEREAWFAA----------ILAPGRPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  78 FDSLLAPTEQIgAELQkIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQGLSMCGEtcYTSA 157
Cdd:COG1247   71 PFRPRPAYRGT-AEES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGT--LPEV 146

                        170
                 ....*....|....*..
gi 505190002 158 QGSIGIW----YMSKAL 170
Cdd:COG1247  147 GFKFGRWldlvLMQKRL 163
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 49-145 1.01e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 69.70  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  49 ALDQTLRQPD-----VCWLLAYEDDALVGYARvnfdslLAPTEQIGAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQ 123
Cdd:COG0454   19 ALDAELKAMEgslagAEFIAVDDKGEPIGFAG------LRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGC 92

                         90       100
                 ....*....|....*....|..
gi 505190002 124 KTLWLEVLQRNTGAQRFYQRQG 145
Cdd:COG0454   93 TALELDTLDGNPAAIRFYERLG 114
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 43-145 1.08e-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: 66.39  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   43 EDFSVSALDQTLRQPDVCWLLAYEDDALVGYARVNFDsllaPTEQIGAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQ 122
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSII----DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92

                          90       100
                  ....*....|....*....|...
gi 505190002  123 QKTLWLEVLQRNTGAQRFYQRQG 145
Cdd:pfam00583  93 CERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 90-170 4.96e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.21  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  90 AELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQGLSMCGETCYTSAQGSIgiwYMSKA 169
Cdd:COG0456   14 AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDAL---VMEKE 90


                 .
gi 505190002 170 L 170
Cdd:COG0456   91 L 91
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-145 1.81e-12

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: 60.81  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   54 LRQPDVCWLLAYEDDALVGYARVNFDsllaPTEqigAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQR 133
Cdd:TIGR01575  26 LANYHLCYLLARIGGKVVGYAGVQIV----LDE---AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVS 98

                          90
                  ....*....|..
gi 505190002  134 NTGAQRFYQRQG 145
Cdd:TIGR01575  99 NIAAQALYKKLG 110
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 53-170 2.93e-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: 60.39  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  53 TLRQPDVCWLLAYEDDALVGYARvnfdslLAPTEQIGAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVlq 132
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAA------LHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT-- 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 505190002 133 rNTGAQRFYQRQGLSMCGETCYTSA-QGSIGIWYMSKAL 170
Cdd:COG1246   94 -TSAAIHFYEKLGFEEIDKEDLPYAkVWQRDSVVMEKDL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-145 9.49e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.15  E-value: 9.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   57 PDVCWLLAYEDDALVGYARVNFDSLLAPTEQIgaelqKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRntg 136
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAEL-----RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR--- 72


                  ....*....
gi 505190002  137 AQRFYQRQG 145
Cdd:pfam13508  73 AAAFYEKLG 81
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
62-145 1.08e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.95  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  62 LLAYEDDALVGYARvnfdslLAPTEQIGAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVlQrnTGAQRFY 141
Cdd:COG2153   37 LLAYDDGELVATAR------LLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA-Q--AHAVGFY 107


                 ....
gi 505190002 142 QRQG 145
Cdd:COG2153  108 EKLG 111
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
70-145 2.76e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 2.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190002  70 LVGYARVNfdsllAPTEQIgAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQG 145
Cdd:COG3393    2 LVAMAGVR-----AESPGV-AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-170 3.82e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 49.70  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   4 VRQALLEDLTLVRDIgirTYRAhfgelwrYPHELEAFLAEDFSVSALDQtlrqpdvCWLLAYEDDALVGYARVNFDSLLA 83
Cdd:COG3153    1 IRPATPEDAEAIAAL---LRAA-------FGPGREAELVDRLREDPAAG-------LSLVAEDDGEIVGHVALSPVDIDG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  84 PTEqiGAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVlqrNTGAQRFYQRQGLSMCGETCYTSAQGSIgi 163
Cdd:COG3153   64 EGP--ALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGELGLTLGPDEV-- 136


                 ....*..
gi 505190002 164 wYMSKAL 170
Cdd:COG3153  137 -FLAKEL 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-129 6.36e-07

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 44.57  E-value: 6.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190002  61 WLLAYEDDALVGYARVNFDSLLAPTeqigAELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLE 129
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDT----AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 90-145 7.79e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.08  E-value: 7.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505190002  90 AELQKIYFLPGHAGNGYGQRLFEQVQQRAIERQQKTLWLEVLQRNTGAQRFYQRQG 145
Cdd:PRK09491  64 ATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLG 119
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-145 1.10e-05

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: 43.45  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   1 MFTVRQALLEDLTLVRDIgirTYRAHFGELWRYPHELEAFLAEDFSVSALDQTLRQPDVCWLLAYEDDALVGYARVNFDS 80
Cdd:COG1670    7 RLRLRPLRPEDAEALAEL---LNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYDID 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190002  81 LLAPTEQIGaelqkIYFLPGHAGNGYGQRLFEQVQQRAIERQQ-KTLWLEVLQRNTGAQRFYQRQG 145
Cdd:COG1670   84 RANRSAEIG-----YWLAPAYWGKGYATEALRALLDYAFEELGlHRVEAEVDPDNTASIRVLEKLG 144
PRK10562 PRK10562
putative acetyltransferase; Provisional
 99-145 1.39e-05

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 42.75  E-value: 1.39e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 505190002  99 PGHAGNGYGQRLFEQVQQRaierqQKTLWLEVLQRNTGAQRFYQRQG 145
Cdd:PRK10562  78 PKAVRRGIGKALMQHVQQR-----YPHLSLEVYQKNQRAVNFYHAQG 119
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-170 1.52e-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: 42.26  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   36 ELEAFLaEDFSVSALDQTLRQPDVCWLLAYEDDALVGYARVnfdsllapteqigAELQKIYFL---PGHAGNGYGQRLFE 112
Cdd:pfam13673   9 GIETFY-EFISPEALRERIDQGEYFFFVAFEGGQIVGVIAL-------------RDRGHISLLfvdPDYQGQGIGKALLE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002  113 QVQQRAIERQQKTLWLEVLQRNTgAQRFYQRQGLSMCGETCYTSaqgsiGIWY--MSKAL 170
Cdd:pfam13673  75 AVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRATGPEQEFN-----GIRFvpMEKEL 128
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 31-146 4.34e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 35.78  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190002   31 WRYPHELEAFLAEDFSVSALDQTLRQPDVCWLLAYEDDALVGYARVNfdslLAPTEQIGAELqKIYFLPGHAGNGYGQRL 110
Cdd:pfam13302  27 YGVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTGFIGSIGLY----DIDGEPERAEL-GYWLGPDYWGKGYATEA 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 505190002  111 FEQVQQRAIERQQ-KTLWLEVLQRNTGAQRFYQRQGL 146
Cdd:pfam13302 102 VRALLEYAFEELGlPRLVARIDPENTASRRVLEKLGF 138
 
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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