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Conserved domains on  [gi|2104871121|ref|WP_224841306|]
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GNAT family N-acetyltransferase [Bacillus tianshenii]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-133 9.96e-24

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 89.76  E-value: 9.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121   3 IIELRDKDqlLDQAIQVFWQQWGSEenfkfYEDAILHSATTSSDIPRFYVAVEEGEIIGTYAILRNDLNSRQDlCPWLAC 82
Cdd:COG3153     1 IRPATPED--AEAIAALLRAAFGPG-----REAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGP-ALLLGP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2104871121  83 LYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIEN--YYEKYGWKNSG 133
Cdd:COG3153    73 LAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLlpFYERFGFRPAG 125
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-133 9.96e-24

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 89.76  E-value: 9.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121   3 IIELRDKDqlLDQAIQVFWQQWGSEenfkfYEDAILHSATTSSDIPRFYVAVEEGEIIGTYAILRNDLNSRQDlCPWLAC 82
Cdd:COG3153     1 IRPATPED--AEAIAALLRAAFGPG-----REAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGP-ALLLGP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2104871121  83 LYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIEN--YYEKYGWKNSG 133
Cdd:COG3153    73 LAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLlpFYERFGFRPAG 125
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-130 4.31e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 63.63  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  49 RFYVAVEEGEIIGTYAILRNDlnsrQDLCPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIE--NYYEK 126
Cdd:pfam13508   4 RFFVAEDDGKIVGFAALLPLD----DEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRaaAFYEK 79


                  ....
gi 2104871121 127 YGWK 130
Cdd:pfam13508  80 LGFE 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-117 2.67e-12

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: 58.06  E-value: 2.67e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2104871121  50 FYVAVEEGEIIGTYAILRNDLNSRqdlCPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLT 117
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK07757 PRK07757
N-acetyltransferase;
50-110 6.40e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 43.26  E-value: 6.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104871121  50 FYVAVEEGEIIGTYA--ILRNDLnsrqdlcpwlA---CLYVAEEHRGKGMGAKLLDHGLSVAAEKG 110
Cdd:PRK07757   43 FYVAEEEGEIVGCCAlhILWEDL----------AeirSLAVSEDYRGQGIGRMLVEACLEEARELG 98
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-133 9.96e-24

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 89.76  E-value: 9.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121   3 IIELRDKDqlLDQAIQVFWQQWGSEenfkfYEDAILHSATTSSDIPRFYVAVEEGEIIGTYAILRNDLNSRQDlCPWLAC 82
Cdd:COG3153     1 IRPATPED--AEAIAALLRAAFGPG-----REAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGP-ALLLGP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2104871121  83 LYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIEN--YYEKYGWKNSG 133
Cdd:COG3153    73 LAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLlpFYERFGFRPAG 125
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 36-130 1.86e-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: 78.50  E-value: 1.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  36 AILHSATTSSDIPRFYVAVEEGEIIGTYAILRNDlnsrqDLCPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLY 115
Cdd:COG1246    16 ELIRPYALEEEIGEFWVAEEDGEIVGCAALHPLD-----EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLF 90

                          90
                  ....*....|....*..
gi 2104871121 116 LTTDIE--NYYEKYGWK 130
Cdd:COG1246    91 LLTTSAaiHFYEKLGFE 107
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
32-140 4.37e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 68.10  E-value: 4.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  32 FYEDAILHSATTSSDIPR------------------FYVAVEEGEIIGtYAILRNdlNSRQDLCPWLA--CLYVAEEHRG 91
Cdd:COG1247    18 IYNEAIAEGTATFETEPPseeereawfaailapgrpVLVAEEDGEVVG-FASLGP--FRPRPAYRGTAeeSIYVDPDARG 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104871121  92 KGMGAKLLDHGLSVAAEKGYENLYLTTDIEN-----YYEKYGWKNSGIVYGAGG 140
Cdd:COG1247    95 RGIGRALLEALIERARARGYRRLVAVVLADNeasiaLYEKLGFEEVGTLPEVGF 148
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-130 4.31e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 63.63  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  49 RFYVAVEEGEIIGTYAILRNDlnsrQDLCPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIE--NYYEK 126
Cdd:pfam13508   4 RFFVAEDDGKIVGFAALLPLD----DEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRaaAFYEK 79


                  ....
gi 2104871121 127 YGWK 130
Cdd:pfam13508  80 LGFE 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-129 1.52e-13

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


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 62.92  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  13 LDQAIQVFWQQWGSEENFKFYEdaiLHSATTSSDIPRFYVAVEEGEIIGTYAILRNDlnsRQDLCPWLACLYVAEEHRGK 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLD---LLEDWDEDASEGFFVAEEDGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2104871121  93 GMGAKLLDHGLSVAAEKGYENLYLTTDIEN-----YYEKYGW 129
Cdd:pfam00583  75 GIGTALLQALLEWARERGCERIFLEVAADNlaaiaLYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 79-148 1.02e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.05  E-value: 1.02e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2104871121  79 WLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIEN-----YYEKYGWKNSGIVYGAGGGSIKLYEK 148
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNeaaiaLYEKLGFEEVGERPNYYGDDALVMEK 89
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-117 2.67e-12

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: 58.06  E-value: 2.67e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2104871121  50 FYVAVEEGEIIGTYAILRNDLNSRqdlCPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLT 117
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-130 7.48e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.22  E-value: 7.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  50 FYVAVEEGEIIGTYAILRNDLNSrqdlcPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIEN-----YY 124
Cdd:COG0454    36 FIAVDDKGEPIGFAGLRRLDDKV-----LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNpaairFY 110


                  ....*.
gi 2104871121 125 EKYGWK 130
Cdd:COG0454   111 ERLGFK 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
51-136 1.57e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 52.88  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  51 YVAVEEGEIIGTYAILRNDLN----SRqdlcpwlacLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLT--TDIENYY 124
Cdd:COG2153    37 LLAYDDGELVATARLLPPGDGeakiGR---------VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSaqAHAVGFY 107

                          90
                  ....*....|..
gi 2104871121 125 EKYGWKNSGIVY 136
Cdd:COG2153   108 EKLGFVPVGEEF 119
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 50-133 2.94e-09

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: 51.89  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  50 FYVAVEEGEIIGtYAILRNdlNSRqdlcpwLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIENY----YE 125
Cdd:pfam13673  33 FFVAFEGGQIVG-VIALRD--RGH------ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPYavpfYE 103


                  ....*...
gi 2104871121 126 KYGWKNSG 133
Cdd:pfam13673 104 KLGFRATG 111
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-129 1.57e-08

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 49.88  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121   8 DKDQLLDQAIQVFwqQWGSEENFKFYEDAILhsattssDIPRFYVAVEEGEIIGTYAILRNDLN--SRQDLCPWLACLYV 85
Cdd:pfam13527   8 EFDEVLRLLEYAF--QDEDSPELREYFRPLL-------EEGRVLGAFDDGELVSTLALYPFELNvpGKTLPAAGITGVAT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2104871121  86 AEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIENYYEKYGW 129
Cdd:pfam13527  79 YPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYPSSYPIYRRFGY 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-129 1.47e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 46.43  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121   1 MEIIELRDKDqlLDQAIQVFWQ--QWGSEENFKFYEDAILHSAttssdipRFYVAVEEGEIIGTYAILRNDLNSRQDLCP 78
Cdd:COG4552     1 MEIRPLTEDD--LDAFARLLAYafGPEPDDEELEAYRPLLEPG-------RVLGVFDDGELVGTLALYPFTLNVGGARVP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104871121  79 --WLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLT-TDIEnYYEKYGW 129
Cdd:COG4552    72 maGITGVAVAPEHRRRGVARALLREALAELRERGQPLSALYpFEPG-FYRRFGY 124
PRK07757 PRK07757
N-acetyltransferase;
50-110 6.40e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 43.26  E-value: 6.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104871121  50 FYVAVEEGEIIGTYA--ILRNDLnsrqdlcpwlA---CLYVAEEHRGKGMGAKLLDHGLSVAAEKG 110
Cdd:PRK07757   43 FYVAEEEGEIVGCCAlhILWEDL----------AeirSLAVSEDYRGQGIGRMLVEACLEEARELG 98
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-130 3.52e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.28  E-value: 3.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2104871121  83 LYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTTDIENY-----YEKYGWK 130
Cdd:COG3393    21 VYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPaarrlYERLGFR 73
PRK10514 PRK10514
putative acetyltransferase; Provisional
 83-133 4.40e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 41.14  E-value: 4.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104871121  83 LYVAEEHRGKGMGAKLLDHGLSVAAEkgyenlyLTTDI--EN-----YYEKYGWKNSG 133
Cdd:PRK10514   75 LFVDPDVRGCGVGRMLVEHALSLHPE-------LTTDVneQNeqavgFYKKMGFKVTG 125
PLN02825 PLN02825
amino-acid N-acetyltransferase
 47-118 1.56e-04

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 40.53  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2104871121  47 IPRFYVAVEEGEIIGTYAILRndlnSRQDLCPWLACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLYLTT 118
Cdd:PLN02825  406 LDSFVVVEREGSIIACAALFP----FFEEKCGEVAAIAVSPECRGQGQGDKLLDYIEKKAASLGLEKLFLLT 473
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 46-118 2.34e-04

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 40.13  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121  46 DIPRFYVAVEEGEIIGTYAilrndlnsrqdLCPW-------LACLYVAEEHRGKGMGAKLLDHGLSVAAEKGYENLY-LT 117
Cdd:PRK05279  332 EIDKFTVIERDGLIIGCAA-----------LYPFpeekmgeMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFvLT 400


                  .
gi 2104871121 118 T 118
Cdd:PRK05279  401 T 401
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-135 6.43e-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: 35.36  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104871121   4 IELRDKDQLL----DQAIQVFWQQWG-SEENFKFYEDAILHSATTSSDIPRFYVAVEEGEIIGTYAILRNDLNSRqdlCP 78
Cdd:COG1670    13 LRPEDAEALAellnDPEVARYLPGPPySLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYDIDRANR---SA 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104871121  79 WLAcLYVAEEHRGKGMG----AKLLDHGLsvaAEKGYENLYLTTDIENY-----YEKYGWKNSGIV 135
Cdd:COG1670    90 EIG-YWLAPAYWGKGYAtealRALLDYAF---EELGLHRVEAEVDPDNTasirvLEKLGFRLEGTL 151
 
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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