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Conserved domains on  [gi|229597567|pdb|2KCW|A]
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Chain A, Uncharacterized acetyltransferase yjaB

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10013546)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate, similar to Escherichia coli putative N-acetyltransferase YjaB

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-146 1.71e-106

putative acetyltransferase; Provisional


:

Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 299.61  E-value: 1.71e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         2 VISIRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGFMLLSGQHMDALFIDPD 81
Cdd:PRK10514   1 MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
2KCW_A        82 VRGCGVGRVLVEHALSMAPELTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGKPYPLLNLAYVG 146
Cdd:PRK10514  81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHLAYVG 145
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-146 1.71e-106

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 299.61  E-value: 1.71e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         2 VISIRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGFMLLSGQHMDALFIDPD 81
Cdd:PRK10514   1 MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
2KCW_A        82 VRGCGVGRVLVEHALSMAPELTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGKPYPLLNLAYVG 146
Cdd:PRK10514  81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHLAYVG 145
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-127 1.73e-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: 1.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A        3 ISIRRSRHEEGEELVAIWCRSVDATHDflSAEYRTELEDLVRSFL-----PEAPLWVAVNErDQPVGFMLLS-------- 69
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEAIAEGTA--TFETEPPSEEEREAWFaailaPGRPVLVAEED-GEVVGFASLGpfrprpay 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
2KCW_A       70 -GQHMDALFIDPDVRGCGVGRVLVEHALSMAPE-----LTTNVNEQNEQAVGFYKKVGFKVTGR 127
Cdd:COG1247  79 rGTAEESIYVDPDARGRGIGRALLEALIERARArgyrrLVAVVLADNEASIALYEKLGFEEVGT 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 17-132 1.21e-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: 63.44  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         17 VAIWCRSVDAT--HDFLSAEyrtELEDLVRSflPEAPLWVAVNErDQPVGFMLLS-GQHMDALFIDPDVRGCGVGRVLVE 93
Cdd:pfam13673   1 EAPDYSEEGIEtfYEFISPE---ALRERIDQ--GEYFFFVAFEG-GQIVGVIALRdRGHISLLFVDPDYQGQGIGKALLE 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
2KCW_A         94 HALSMA-------PELTtnVNEQNeQAVGFYKKVGFKVTGRSEVDD 132
Cdd:pfam13673  75 AVEDYAekdgiklSELT--VNASP-YAVPFYEKLGFRATGPEQEFN 117
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-127 3.76e-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: 43.47  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         53 WVAVNERDQPVGF----MLLSGQHMDALFIDPDVRGCGVGRVLVEHALSMAP-----ELTTNVNEQNEQAVGFYKKVGFK 123
Cdd:TIGR01575  33 YLLARIGGKVVGYagvqIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKgrgvnEIFLEVRVSNIAAQALYKKLGFN 112


                  ....
2KCW_A        124 VTGR 127
Cdd:TIGR01575 113 EIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-102 1.18e-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: 40.72  E-value: 1.18e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2KCW_A       52 LWVAVNErDQPVGFMLLSGQ-------HMDALFIDPDVRGCGVGRVLVEHALSMAPEL 102
Cdd:cd04301   1 FLVAEDD-GEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-146 1.71e-106

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 299.61  E-value: 1.71e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         2 VISIRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGFMLLSGQHMDALFIDPD 81
Cdd:PRK10514   1 MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
2KCW_A        82 VRGCGVGRVLVEHALSMAPELTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGKPYPLLNLAYVG 146
Cdd:PRK10514  81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHLAYVG 145
PRK10562 PRK10562
putative acetyltransferase; Provisional
 5-136 9.76e-23

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 87.43  E-value: 9.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         5 IRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVR-SFLPEAPLWVAvNERDQPVGFM-LLSGQHMDALFIDPDV 82
Cdd:PRK10562   2 IREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRdVYLPAAQTWVW-EEDGKLLGFVsVLEGRFVGALFVAPKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
2KCW_A        83 RGCGVGRVLVEHALSMAPELTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGKP 136
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHP 134
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-127 1.73e-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: 1.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A        3 ISIRRSRHEEGEELVAIWCRSVDATHDflSAEYRTELEDLVRSFL-----PEAPLWVAVNErDQPVGFMLLS-------- 69
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEAIAEGTA--TFETEPPSEEEREAWFaailaPGRPVLVAEED-GEVVGFASLGpfrprpay 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
2KCW_A       70 -GQHMDALFIDPDVRGCGVGRVLVEHALSMAPE-----LTTNVNEQNEQAVGFYKKVGFKVTGR 127
Cdd:COG1247  79 rGTAEESIYVDPDARGRGIGRALLEALIERARArgyrrLVAVVLADNEASIALYEKLGFEEVGT 142
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 3-135 5.58e-17

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 72.01  E-value: 5.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A        3 ISIRRSRHEEGEELVAIwcrsvdathDFLSAEYRTELEDLVRSFlpeaplWVAVNERDQPVGFMLLS-----GQHMDALF 77
Cdd:COG0454   1 MSIRKATPEDINFILLI---------EALDAELKAMEGSLAGAE------FIAVDDKGEPIGFAGLRrlddkVLELKRLY 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
2KCW_A       78 IDPDVRGCGVGRVLVEHALSMAPE-----LTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGK 135
Cdd:COG0454  66 VLPEYRGKGIGKALLEALLEWARErgctaLELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-129 5.51e-14

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: 5.51e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
2KCW_A       72 HMDALFIDPDVRGCGVGRVLVEHALSMAPE-----LTTNVNEQNEQAVGFYKKVGFKVTGRSE 129
Cdd:COG0456  15 EIEDLAVDPEYRGRGIGRALLEAALERARErgarrLRLEVREDNEAAIALYEKLGFEEVGERP 77
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 17-132 1.21e-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: 63.44  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         17 VAIWCRSVDAT--HDFLSAEyrtELEDLVRSflPEAPLWVAVNErDQPVGFMLLS-GQHMDALFIDPDVRGCGVGRVLVE 93
Cdd:pfam13673   1 EAPDYSEEGIEtfYEFISPE---ALRERIDQ--GEYFFFVAFEG-GQIVGVIALRdRGHISLLFVDPDYQGQGIGKALLE 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
2KCW_A         94 HALSMA-------PELTtnVNEQNeQAVGFYKKVGFKVTGRSEVDD 132
Cdd:pfam13673  75 AVEDYAekdgiklSELT--VNASP-YAVPFYEKLGFRATGPEQEFN 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-124 6.11e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.15  E-value: 6.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         48 PEAPLWVAVNErDQPVGFMLLSGQHMDA------LFIDPDVRGCGVGRVLVEHALSMA--PELTTNVNEQNEQAVGFYKK 119
Cdd:pfam13508   1 PGGRFFVAEDD-GKIVGFAALLPLDDEGalaelrLAVHPEYRGQGIGRALLEAAEAAAkeGGIKLLELETTNRAAAFYEK 79


                  ....*
2KCW_A        120 VGFKV 124
Cdd:pfam13508  80 LGFEE 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 29-122 1.28e-10

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: 55.22  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         29 DFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGFMLLSGQ-------HMDALFIDPDVRGCGVGRVLVEHALSMAPE 101
Cdd:pfam00583  11 EFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIddeppvgEIEGLAVAPEYRGKGIGTALLQALLEWARE 90

                          90       100
                  ....*....|....*....|....*.
2KCW_A        102 -----LTTNVNEQNEQAVGFYKKVGF 122
Cdd:pfam00583  91 rgcerIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-137 1.51e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.48  E-value: 1.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A        5 IRRSRHEEGEELVAIWCRSvdathdfLSAEYRTELEDLVRSFLPEAPLWVAVNErDQPVGFMLLSGQHMD---------A 75
Cdd:COG3153   1 IRPATPEDAEAIAALLRAA-------FGPGREAELVDRLREDPAAGLSLVAEDD-GEIVGHVALSPVDIDgegpalllgP 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2KCW_A       76 LFIDPDVRGCGVGRVLVEHALSMAPE-------LTTnvneqNEQAVGFYKKVGFKVTGRSEVDDLGKPY 137
Cdd:COG3153  73 LAVDPEYRGQGIGRALMRAALEAARErgaravvLLG-----DPSLLPFYERFGFRPAGELGLTLGPDEV 136
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 38-132 9.41e-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: 53.07  E-value: 9.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A       38 ELEDLVRSFLPEAP---LWVAVNErDQPVGFMLLSGQ-----HMDALFIDPDVRGCGVGRVLVEHALSMAPE-------L 102
Cdd:COG1246  13 AILELIRPYALEEEigeFWVAEED-GEIVGCAALHPLdedlaELRSLAVHPDYRGRGIGRRLLEALLAEARElglkrlfL 91

                        90       100       110
                ....*....|....*....|....*....|
2KCW_A      103 TTnvneqNEQAVGFYKKVGFKVTGRSEVDD 132
Cdd:COG1246  92 LT-----TSAAIHFYEKLGFEEIDKEDLPY 116
PRK09831 PRK09831
GNAT family N-acetyltransferase;
3-134 1.86e-08

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 49.96  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         3 ISIRRSRHEEGEELVAIWCRSVDAThdfLSAEYRTEL--------EDLVRSFLPEAPLWVAVNErDQPVGFMLLSGQHMD 74
Cdd:PRK09831   1 IQIRNYQPGDFQQLCAIFIRAVTMT---ASQHYSPQQiaawaqidESRWKEKLAKSQVRVAVIN-AQPVGFITCIEHYID 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A        75 ALFIDPDVRGCGVGRVLVEHALSMAPELTTNVneqNEQAVGFYKKVGFKVTGRSEVDDLG 134
Cdd:PRK09831  77 MLFVDPEYTRRGVASALLKPLIKSESELTVDA---SITAKPFFERYGFQTVKQQRVECRG 133
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
76-132 1.88e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.40  E-value: 1.88e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A       76 LFIDPDVRGCGVGRVLVEHALSMAPELTTN---VNEQnEQAVGFYKKVGFKVTGRSEVDD 132
Cdd:COG2153  64 VAVLPEYRGQGLGRALMEAAIEEARERGARrivLSAQ-AHAVGFYEKLGFVPVGEEFLEA 122
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-129 3.66e-06

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: 44.22  E-value: 3.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A        3 ISIRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVRSFLPE------APLWVAVNERDQPVGFMLLSGQHMD-- 74
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADwadggaLPFAIEDKEDGELIGVVGLYDIDRAnr 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2KCW_A       75 ----ALFIDPDVRGCGVGRVLVEHALSMA------PELTTNVNEQNEQAVGFYKKVGFKVTGRSE 129
Cdd:COG1670  88 saeiGYWLAPAYWGKGYATEALRALLDYAfeelglHRVEAEVDPDNTASIRVLEKLGFRLEGTLR 152
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-127 3.76e-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: 43.47  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         53 WVAVNERDQPVGF----MLLSGQHMDALFIDPDVRGCGVGRVLVEHALSMAP-----ELTTNVNEQNEQAVGFYKKVGFK 123
Cdd:TIGR01575  33 YLLARIGGKVVGYagvqIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKgrgvnEIFLEVRVSNIAAQALYKKLGFN 112


                  ....
2KCW_A        124 VTGR 127
Cdd:TIGR01575 113 EIAI 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
75-127 4.91e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.20  E-value: 4.91e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2KCW_A       75 ALFIDPDVRGCGVGRVLVEHALSMA-----PELTTNVNEQNEQAVGFYKKVGFKVTGR 127
Cdd:COG3393  20 GVYTHPEYRGRGLASALVAALAREAlargaRTPFLYVDADNPAARRLYERLGFRPVGE 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-102 1.18e-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: 40.72  E-value: 1.18e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2KCW_A       52 LWVAVNErDQPVGFMLLSGQ-------HMDALFIDPDVRGCGVGRVLVEHALSMAPEL 102
Cdd:cd04301   1 FLVAEDD-GEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-135 1.42e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KCW_A         1 MVISIRRSRHEEGEELVAIWCRSvdathdFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGfMLLSGQ-----HMDA 75
Cdd:PRK03624   1 DAMEIRVFRQADFEAVIALWERC------DLTRPWNDPEMDIERKLNHDPSLFLVAEVGGEVVG-TVMGGYdghrgWAYY 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
2KCW_A        76 LFIDPDVRGCGVGRVLVEHALSM-----APELTTNVNEQNEQAVGFYKKVGFKVtgrSEVDDLGK 135
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKliargCPKINLQVREDNDAVLGFYEALGYEE---QDRISLGK 135
PRK07757 PRK07757
N-acetyltransferase;
75-129 1.15e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.10  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2KCW_A        75 ALFIDPDVRGCGVGRVLVEHALSMAPELttNVNE------QneqaVGFYKKVGFKVTGRSE 129
Cdd:PRK07757  70 SLAVSEDYRGQGIGRMLVEACLEEAREL--GVKRvfaltyQ----PEFFEKLGFREVDKEA 124
 
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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