NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446391627|ref|WP_000469482|]
View 

GNAT family N-acetyltransferase [Vibrio cholerae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-174 9.73e-44

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: 142.83  E-value: 9.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   1 MFIESLKIRLRSLEVEDAESFYQWSGDREVTQFSLSAyayPQSRSDIAKWLSEIN---SSSKTISFGIECKESQKLIGYA 77
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGP---PYSLEEARAWLERLLadwADGGALPFAIEDKEDGELIGVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  78 GISGISSLNRSGEYFILIGdKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGY 157
Cdd:COG1670   78 GLYDIDRANRSAEIGYWLA-PAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156

                        170
                 ....*....|....*..
gi 446391627 158 RNGRFMDKVQMSVLSRE 174
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-174 9.73e-44

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: 142.83  E-value: 9.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   1 MFIESLKIRLRSLEVEDAESFYQWSGDREVTQFSLSAyayPQSRSDIAKWLSEIN---SSSKTISFGIECKESQKLIGYA 77
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGP---PYSLEEARAWLERLLadwADGGALPFAIEDKEDGELIGVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  78 GISGISSLNRSGEYFILIGdKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGY 157
Cdd:COG1670   78 GLYDIDRANRSAEIGYWLA-PAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156

                        170
                 ....*....|....*..
gi 446391627 158 RNGRFMDKVQMSVLSRE 174
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-147 1.48e-25

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 95.49  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627    8 IRLRSLEVEDAESFYQWSGDREVTQFSlsaYAYPQSRSDIAKWLSEI---NSSSKTISFGIECKESQkLIGYAGISGISS 84
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYG---VPWPLTLEEAREWLARIwaaDEAERGYGWAIELKDTG-FIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446391627   85 LNRSGEYFILIGdKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQ 147
Cdd:pfam13302  78 EPERAELGYWLG-PDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 4-177 4.21e-08

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 50.57  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   4 ESLKIRLRSLEVEDAESFYQWSGDREVTQFSLS-AYAYPQSRSDIakWLSEINSSSKTiSFGIECKESQklIGYAGISGI 82
Cdd:PRK15130   3 SAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEePYEAFVELSDL--YDKHIHDQSER-RFVVECDGEK--AGLVELVEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  83 SSLNRSGEYFILIgDKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGYRNGRF 162
Cdd:PRK15130  78 NHVHRRAEFQIII-SPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEY 156

                        170
                 ....*....|....*
gi 446391627 163 MDKVQMSVLSREWPA 177
Cdd:PRK15130 157 RNTIRMCIFQHQYLA 171
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 72-129 8.08e-03

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: 33.40  E-value: 8.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446391627  72 KLIGYAGISGISSLNRSGEYFILIGDKAFWGKGLGTEVTRLVTNYgFRELGLHRIELT 129
Cdd:cd04301    9 EIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE-ARERGAKRLRLE 65
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-174 9.73e-44

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: 142.83  E-value: 9.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   1 MFIESLKIRLRSLEVEDAESFYQWSGDREVTQFSLSAyayPQSRSDIAKWLSEIN---SSSKTISFGIECKESQKLIGYA 77
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGP---PYSLEEARAWLERLLadwADGGALPFAIEDKEDGELIGVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  78 GISGISSLNRSGEYFILIGdKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGY 157
Cdd:COG1670   78 GLYDIDRANRSAEIGYWLA-PAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156

                        170
                 ....*....|....*..
gi 446391627 158 RNGRFMDKVQMSVLSRE 174
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-147 1.48e-25

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 95.49  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627    8 IRLRSLEVEDAESFYQWSGDREVTQFSlsaYAYPQSRSDIAKWLSEI---NSSSKTISFGIECKESQkLIGYAGISGISS 84
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYG---VPWPLTLEEAREWLARIwaaDEAERGYGWAIELKDTG-FIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446391627   85 LNRSGEYFILIGdKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQ 147
Cdd:pfam13302  78 EPERAELGYWLG-PDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-168 4.66e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.48  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   8 IRLRSLEVEDAE---SFYqwsgdREVTQFSLSAYAY-PQSRSDIAKWLSEINSSSktiSFGIECKESQKLIGYAGISGIS 83
Cdd:COG1247    2 MTIRPATPEDAPaiaAIY-----NEAIAEGTATFETePPSEEEREAWFAAILAPG---RPVLVAEEDGEVVGFASLGPFR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  84 S---LNRSGEYFILIgDKAFWGKGLGTE-VTRLVTnyGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGYRN 159
Cdd:COG1247   74 PrpaYRGTAEESIYV-DPDARGRGIGRAlLEALIE--RARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKF 150


                 ....*....
gi 446391627 160 GRFMDKVQM 168
Cdd:COG1247  151 GRWLDLVLM 159
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
10-164 2.59e-09

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 53.14  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   10 LRSLEVEDAESFYQWSGDREVTQFSLSAYAYPqSRSDIAKWLSEInSSSKTISFGIEckESQKLIGYAGISGISSLNRSG 89
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHS-SIEEFETFLAAY-LSPGEIVFGVA--ESDRLIGYATLRQFDYVKTHK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446391627   90 ---EYFILIGDKafwgKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGYRNGRFMD 164
Cdd:pfam13420  77 aelSFYVVKNND----EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 67-146 3.10e-09

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: 52.13  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   67 CKESQKLIGYAGISGISSLNRSGEYFILIGDKAFWGKGLGTEVTRLVTNYGfRELGLHRIELTAYCDNVAAVKAYENAGY 146
Cdd:pfam00583  38 AEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWA-RERGCERIFLEVAADNLAAIALYEKLGF 116
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 4-177 4.21e-08

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 50.57  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   4 ESLKIRLRSLEVEDAESFYQWSGDREVTQFSLS-AYAYPQSRSDIakWLSEINSSSKTiSFGIECKESQklIGYAGISGI 82
Cdd:PRK15130   3 SAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEePYEAFVELSDL--YDKHIHDQSER-RFVVECDGEK--AGLVELVEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  83 SSLNRSGEYFILIgDKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGYRNGRF 162
Cdd:PRK15130  78 NHVHRRAEFQIII-SPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEY 156

                        170
                 ....*....|....*
gi 446391627 163 MDKVQMSVLSREWPA 177
Cdd:PRK15130 157 RNTIRMCIFQHQYLA 171
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 97-165 3.58e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 3.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446391627  97 DKAFWGKGLGTEVTRLVTNYgFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGYRNGRFMDK 165
Cdd:COG0456   22 DPEYRGRGIGRALLEAALER-ARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEK 89
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
72-150 7.17e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.28  E-value: 7.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  72 KLIGYAGISGisslnRSGEYFILIG---DKAFWGKGLGTEVTRLVTNYgFRELGLHRIELTAYCDNVAAVKAYENAGYQH 148
Cdd:COG3393    1 ELVAMAGVRA-----ESPGVAEISGvytHPEYRGRGLASALVAALARE-ALARGARTPFLYVDADNPAARRLYERLGFRP 74


                 ..
gi 446391627 149 EG 150
Cdd:COG3393   75 VG 76
PRK10140 PRK10140
N-acetyltransferase;
97-169 1.09e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 46.13  E-value: 1.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446391627  97 DKAFWGKGLGTEVTRLVTNYGFRELGLHRIELTAYCDNVAAVKAYENAGYQHEGIKRESGYRNGRFMDKVQMS 169
Cdd:PRK10140  87 DSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMA 159
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 93-150 1.10e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 43.28  E-value: 1.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   93 ILIGDKAFWGKGLGTEVTRLVTNYGFRELGLHRI--ELTAycDNVAAVKAYENAGYQHEG 150
Cdd:pfam13523  84 LLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVvvEPDV--RNERAIRLLERAGFRKVK 141
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 72-166 1.22e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 42.73  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  72 KLIGYAGISGISSlnRSGEYFILIGDKAFWGKGLGTEVTRLVTNYgFRELGLHRIELTAYCDNVAAVKAYENAGYQHegI 151
Cdd:COG0454   44 EPIGFAGLRRLDD--KVLELKRLYVLPEYRGKGIGKALLEALLEW-ARERGCTALELDTLDGNPAAIRFYERLGFKE--I 118

                         90
                 ....*....|....*
gi 446391627 152 KRESGYRNGRFMDKV 166
Cdd:COG0454  119 ERYVAYVGGEFEKEL 133
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
7-162 6.49e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 38.35  E-value: 6.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627   7 KIRLRSLEVEDAESFY----QWSGDREVTQFSLSAYAypqsrsDIAKWLSEINSSSKTIS-----------FGIEckESQ 71
Cdd:COG3981    1 MMELVRPTLEDEESYLeylaEFLKEHIDGSGYLVSFE------DFEAWLERLLDEEKGEElpegwvpattyWLVD--EDG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391627  72 KLIGyagisGIS---SLNRsgeyFIL-----IGD---KAFWGKGLGTEVTRLVTNYGfRELGLHRIELTAYCDNVAAVKA 140
Cdd:COG3981   73 RIVG-----AINlrhELNE----FLLrvgghIGYgvrPSERGKGYATEMLRLALEEA-RELGLDRVLITCDKDNIASRKV 142

                        170       180
                 ....*....|....*....|....
gi 446391627 141 YENAG--YQHEGIKRESGYRNGRF 162
Cdd:COG3981  143 IEANGgvLEDEVVDEEDGRPVRRY 166
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 72-129 8.08e-03

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: 33.40  E-value: 8.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446391627  72 KLIGYAGISGISSLNRSGEYFILIGDKAFWGKGLGTEVTRLVTNYgFRELGLHRIELT 129
Cdd:cd04301    9 EIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE-ARERGAKRLRLE 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH