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Conserved domains on  [gi|41055301|ref|NP_956938|]
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RNA cytidine acetyltransferase [Danio rerio]

Protein Classification

tRNA(Met) cytidine acetyltransferase TmcA family protein( domain architecture ID 1000356)

tRNA(Met) cytidine acetyltransferase TmcA family protein may catalyze the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and either ATP or GTP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GNAT_acetyltr_2 pfam13718
GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related ...
530-754 1.47e-136

GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related N-acetyltransferase (GNAT) fold.


:

Pssm-ID: 463966 [Multi-domain]  Cd Length: 227  Bit Score: 409.69  E-value: 1.47e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    530 RLMALYVASHYKNSPNDLQMLSDAPAHHLFCLLPPVPPTQNSLPEVLAVLQVCLEGEISRQSILSSLSRGKKASGDLIPW 609
Cdd:pfam13718    1 RLMALYVASHYKNSPNDLQLLSDAPAHHLFVLLGPVDESGNALPDILCVVQVALEGRISRESVKNSLSRGKRASGDLIPW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    610 TVSEQFQDSEFAGLSGGRIVRIAVNPDYQGMGYGTRALQLLQRYYEGQFPLWDEQEQTMTSAITSVSSEA--VSLLEEVV 687
Cdd:pfam13718   81 TVSQQFQDEDFASLSGARIVRIATHPEYQGMGYGSRALELLIQYYEGKITDLSEAEELEEEEADRIEDEEsaVSLLEEKI 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055301    688 SPRKDLPPLLLKLNERRAERLDYLGVSYGLTPQPLKFWKKAGFVPVYLRQTPNDLTGEHSCIMLKDL 754
Cdd:pfam13718  161 RPRKELPPLLLKLSERPPERLDYLGVSFGLTPDLLKFWKRAGFVPVYLRQTPNELTGEHSCIMLRPL 227
tRNA_bind_2 pfam13725
Possible tRNA binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
765-978 1.58e-109

Possible tRNA binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine acetyltransferase, may be involved in tRNA-binding.


:

Pssm-ID: 463969  Cd Length: 231  Bit Score: 339.11  E-value: 1.58e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    765 WLSAFWKDFRRRFLSLMSFQFSKFSSTLALNILQNKSA-----KDDSTAVLTSAELAATFTPYDLKRLEMYSRNMVDYHL 839
Cdd:pfam13725    1 WLGAFAKDFRRRFLSLLSYQFRKFPSVLALSILESANAgakldPSTEPKPLTKAELDALLSPFDLKRLESYANNMLDYHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    840 IMDMIPVIARMHFLKQFG-DISLSVAQSALLLGIGLQHKSVDELEKEIGLPSSQLMGLFNRIIRKVVQFFNTLQERAVEA 918
Cdd:pfam13725   81 ILDLLPTLARLYFTGRLPsDVKLSGVQSAILLAIGLQRKDIDDLEKELNLPSNQLLALFNKIMRKISKYFRSIQEKAIEA 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055301    919 EMVATKDI----------GLEPTVQTLNEDLNDAAKEFDEKHK-KDIEKIKDMNLSEYMIRGDDEEWDQVL 978
Cdd:pfam13725  161 TLPKLKDIsahddevkdeDLEPLEQSLDEELEEAAKEVEEKLKeKQRELIDSLDLDKYAIKGDEEDWEKAL 231
TmcA super family cl34266
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
12-906 2.95e-99

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


The actual alignment was detected with superfamily member COG1444:

Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 328.33  E-value: 2.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301   12 IRVQIENGVAEHHRSMFVIVGDRGrdqvvilhhmlskatvrarpsvlWCYKkelgfssnrkkRMRQLQKKIKTGTLNLNQ 91
Cdd:COG1444    4 LRALRAEARRAGHRRLLVLSGDDE-----------------------WCRA-----------QAEALLEALPGDWLWVGE 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301   92 DDPFELfvaatniRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGIVVILlrtMNSLKQLYTMTMDVHS 171
Cdd:COG1444   50 RPPLGV-------EHIPPSAARRLLGREFDHVVFDAHDGFDPNALGALSGTVRGGGLLVLL---TPPLDEWPQRPDPDSL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  172 RYRTEAHQDVIGRFNERFILSLSSCKSCVVID-DQLNILPisshatnikPIPPKKqddgLSPREqelkdlkeslqdtqpv 250
Cdd:COG1444  120 RLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDqDSPLIDP---------ELPAKA----RFPRP---------------- 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  251 gvLVDGCKTLDQAKAvLKFIEAISEKtlRSTVALTAARGRGKSAALGLAMAGAVAFGYSnIFVTSPSPDNLHTLFEFVFK 330
Cdd:COG1444  171 --AYEGCLTADQAAA-LAALERLAER--KRVLVLTADRGRGKSAAAGLAAARLAAEGGR-VLVTAPSKAAVEELFEFAGE 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  331 GFDALQYQEHLDYEIIQSlnpefnkavvrvnifkehrqtIQYIHPADAVKL-GQAELLVIDEAAAIPLPLVKKLLG--PY 407
Cdd:COG1444  245 LLEALGVKYRELTGAGGR---------------------VRFVAPDALLERpPDADLLLVDEAAAIPVPLLEKLLAafPR 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  408 LVFmASTINGYEGTGRSLSLKLIQQLRQQssesqqnlsaenrntstarlaaARSLHEVTLHESIRYGQGDHVERWLN--- 484
Cdd:COG1444  304 VVF-TTTVHGYEGTGRGFLLRFCARLDES----------------------TPGWRELTLDEPIRWAAGDPLERWLFral 360
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  485 ----DLLCLDCLSVPriisgcplPQTCDLYYVNRDTLFcyhkASEAFLQRLMALYVASHYKNSPNDLQMLSDAPAHHLFC 560
Cdd:COG1444  361 lldaEPAVLQLVDAP--------PGEVEYERLDQDELL----ADEELLRQLFGLLVLAHYRTSPDDLRRLLDAPNQHFRA 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  561 LlppvppTQNslPEVLAVLQVCLEGEIS---RQSILsslsRGK-KASGDLIPWTVSEQFQDSEFAGLSGGRIVRIAVNPD 636
Cdd:COG1444  429 L------RTG--GKVVGVAWLAEEGGLDaelAEAVW----AGRrRPRGNLVPQSLAAHLGLPEAATLRGWRIVRIAVHPA 496
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  637 YQGMGYGTRalqllqryyegqfplwdeqeqtmtsaitsvsseavsLLEEVVsprkdlpplllklNERRAERLDYLGVSYG 716
Cdd:COG1444  497 LQRRGLGSR------------------------------------LLAEIR-------------EEAKEEGLDWLGVSFG 527
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  717 LTPQPLKFWKKAGFVPVYLRQTPNDLTGEHSCIMLKDLNS--EDLTDQ-NQWlsafwkdFRRRFLSLMSFQFSKFSSTLA 793
Cdd:COG1444  528 ATPELLRFWQRNGFVPVHLGTTRNASSGEYSAMVLKPLSEagEALVDRaARR-------FARDLPNLLSDPLRDLDPDVA 600
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  794 LNILQNksakddstavlTSAELAATFTPYDLKRLEMYSRNMVDYHLIMDMIPVIARMHFLKqfGDISLSVAQSALLLGIG 873
Cdd:COG1444  601 RALLRA-----------LPADADPELSDEDWRELAGFAFGHRPYEASLDALRRLLLAYLLD--PRADLSPREERLLVAKV 667
                        890       900       910
                 ....*....|....*....|....*....|....
gi 41055301  874 LQHKSVDELEKEIGLPS-SQLMGLFNRIIRKVVQ 906
Cdd:COG1444  668 LQGRSWEEVAEELGLSGrKALLRALRDAVAQLLD 701
 
Name Accession Description Interval E-value
GNAT_acetyltr_2 pfam13718
GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related ...
530-754 1.47e-136

GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related N-acetyltransferase (GNAT) fold.


Pssm-ID: 463966 [Multi-domain]  Cd Length: 227  Bit Score: 409.69  E-value: 1.47e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    530 RLMALYVASHYKNSPNDLQMLSDAPAHHLFCLLPPVPPTQNSLPEVLAVLQVCLEGEISRQSILSSLSRGKKASGDLIPW 609
Cdd:pfam13718    1 RLMALYVASHYKNSPNDLQLLSDAPAHHLFVLLGPVDESGNALPDILCVVQVALEGRISRESVKNSLSRGKRASGDLIPW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    610 TVSEQFQDSEFAGLSGGRIVRIAVNPDYQGMGYGTRALQLLQRYYEGQFPLWDEQEQTMTSAITSVSSEA--VSLLEEVV 687
Cdd:pfam13718   81 TVSQQFQDEDFASLSGARIVRIATHPEYQGMGYGSRALELLIQYYEGKITDLSEAEELEEEEADRIEDEEsaVSLLEEKI 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055301    688 SPRKDLPPLLLKLNERRAERLDYLGVSYGLTPQPLKFWKKAGFVPVYLRQTPNDLTGEHSCIMLKDL 754
Cdd:pfam13718  161 RPRKELPPLLLKLSERPPERLDYLGVSFGLTPDLLKFWKRAGFVPVYLRQTPNELTGEHSCIMLRPL 227
tRNA_bind_2 pfam13725
Possible tRNA binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
765-978 1.58e-109

Possible tRNA binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine acetyltransferase, may be involved in tRNA-binding.


Pssm-ID: 463969  Cd Length: 231  Bit Score: 339.11  E-value: 1.58e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    765 WLSAFWKDFRRRFLSLMSFQFSKFSSTLALNILQNKSA-----KDDSTAVLTSAELAATFTPYDLKRLEMYSRNMVDYHL 839
Cdd:pfam13725    1 WLGAFAKDFRRRFLSLLSYQFRKFPSVLALSILESANAgakldPSTEPKPLTKAELDALLSPFDLKRLESYANNMLDYHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    840 IMDMIPVIARMHFLKQFG-DISLSVAQSALLLGIGLQHKSVDELEKEIGLPSSQLMGLFNRIIRKVVQFFNTLQERAVEA 918
Cdd:pfam13725   81 ILDLLPTLARLYFTGRLPsDVKLSGVQSAILLAIGLQRKDIDDLEKELNLPSNQLLALFNKIMRKISKYFRSIQEKAIEA 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055301    919 EMVATKDI----------GLEPTVQTLNEDLNDAAKEFDEKHK-KDIEKIKDMNLSEYMIRGDDEEWDQVL 978
Cdd:pfam13725  161 TLPKLKDIsahddevkdeDLEPLEQSLDEELEEAAKEVEEKLKeKQRELIDSLDLDKYAIKGDEEDWEKAL 231
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
12-906 2.95e-99

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 328.33  E-value: 2.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301   12 IRVQIENGVAEHHRSMFVIVGDRGrdqvvilhhmlskatvrarpsvlWCYKkelgfssnrkkRMRQLQKKIKTGTLNLNQ 91
Cdd:COG1444    4 LRALRAEARRAGHRRLLVLSGDDE-----------------------WCRA-----------QAEALLEALPGDWLWVGE 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301   92 DDPFELfvaatniRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGIVVILlrtMNSLKQLYTMTMDVHS 171
Cdd:COG1444   50 RPPLGV-------EHIPPSAARRLLGREFDHVVFDAHDGFDPNALGALSGTVRGGGLLVLL---TPPLDEWPQRPDPDSL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  172 RYRTEAHQDVIGRFNERFILSLSSCKSCVVID-DQLNILPisshatnikPIPPKKqddgLSPREqelkdlkeslqdtqpv 250
Cdd:COG1444  120 RLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDqDSPLIDP---------ELPAKA----RFPRP---------------- 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  251 gvLVDGCKTLDQAKAvLKFIEAISEKtlRSTVALTAARGRGKSAALGLAMAGAVAFGYSnIFVTSPSPDNLHTLFEFVFK 330
Cdd:COG1444  171 --AYEGCLTADQAAA-LAALERLAER--KRVLVLTADRGRGKSAAAGLAAARLAAEGGR-VLVTAPSKAAVEELFEFAGE 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  331 GFDALQYQEHLDYEIIQSlnpefnkavvrvnifkehrqtIQYIHPADAVKL-GQAELLVIDEAAAIPLPLVKKLLG--PY 407
Cdd:COG1444  245 LLEALGVKYRELTGAGGR---------------------VRFVAPDALLERpPDADLLLVDEAAAIPVPLLEKLLAafPR 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  408 LVFmASTINGYEGTGRSLSLKLIQQLRQQssesqqnlsaenrntstarlaaARSLHEVTLHESIRYGQGDHVERWLN--- 484
Cdd:COG1444  304 VVF-TTTVHGYEGTGRGFLLRFCARLDES----------------------TPGWRELTLDEPIRWAAGDPLERWLFral 360
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  485 ----DLLCLDCLSVPriisgcplPQTCDLYYVNRDTLFcyhkASEAFLQRLMALYVASHYKNSPNDLQMLSDAPAHHLFC 560
Cdd:COG1444  361 lldaEPAVLQLVDAP--------PGEVEYERLDQDELL----ADEELLRQLFGLLVLAHYRTSPDDLRRLLDAPNQHFRA 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  561 LlppvppTQNslPEVLAVLQVCLEGEIS---RQSILsslsRGK-KASGDLIPWTVSEQFQDSEFAGLSGGRIVRIAVNPD 636
Cdd:COG1444  429 L------RTG--GKVVGVAWLAEEGGLDaelAEAVW----AGRrRPRGNLVPQSLAAHLGLPEAATLRGWRIVRIAVHPA 496
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  637 YQGMGYGTRalqllqryyegqfplwdeqeqtmtsaitsvsseavsLLEEVVsprkdlpplllklNERRAERLDYLGVSYG 716
Cdd:COG1444  497 LQRRGLGSR------------------------------------LLAEIR-------------EEAKEEGLDWLGVSFG 527
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  717 LTPQPLKFWKKAGFVPVYLRQTPNDLTGEHSCIMLKDLNS--EDLTDQ-NQWlsafwkdFRRRFLSLMSFQFSKFSSTLA 793
Cdd:COG1444  528 ATPELLRFWQRNGFVPVHLGTTRNASSGEYSAMVLKPLSEagEALVDRaARR-------FARDLPNLLSDPLRDLDPDVA 600
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  794 LNILQNksakddstavlTSAELAATFTPYDLKRLEMYSRNMVDYHLIMDMIPVIARMHFLKqfGDISLSVAQSALLLGIG 873
Cdd:COG1444  601 RALLRA-----------LPADADPELSDEDWRELAGFAFGHRPYEASLDALRRLLLAYLLD--PRADLSPREERLLVAKV 667
                        890       900       910
                 ....*....|....*....|....*....|....
gi 41055301  874 LQHKSVDELEKEIGLPS-SQLMGLFNRIIRKVVQ 906
Cdd:COG1444  668 LQGRSWEEVAEELGLSGrKALLRALRDAVAQLLD 701
TmcA_N pfam08351
tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is ...
11-203 7.36e-71

tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is often found at the N-terminus of the bacterial tRNA(Met) cytidine acetyltransferase TmcA. TmcA catalyzes the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met) by using acetyl-CoA as an acetyl donor and either ATP or GTP. This modification is thought to ensure precise recognition of the AUG codon by strengthening C-G base-pair interaction and also prevent misrecognition of the near cognate AUA codon. This domain is also found in mammalian N-acetyltransferase 10 (NAT10) and fungal protein Kre33. Kre33 and NAT10 are RNA cytosine acetyltransferases with specificity toward both 18S rRNA and tRNAs and contain additional putative nuclear and nucleolar localization signals (NLS and NoLS respectively).


Pssm-ID: 462441 [Multi-domain]  Cd Length: 178  Bit Score: 232.95  E-value: 7.36e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301     11 RIRVQIENGVAEHHRSMFVIVGDRG----RDQVVILHHMLSKATvRARPSVLWCYKKELgfsSNRKKRMRQLQKKIKTGT 86
Cdd:pfam08351    2 RLRKLLEDAVKANHRRLVVIVGDDPelhvKEQVPNYHRILSRLS-SSKPSVLYCYHPEF---FDAKKRKKEFKKLVKRGE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301     87 LNLNqddpfelfvaatnIRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGIVVILLRTMNSLKQLYTMt 166
Cdd:pfam08351   78 LDIE-------------IEYIDYKESEKVLGQTYDMLVLDLFEDLTPNDLGRLVETVRGGGLIILLLPPLDSWKQLYTI- 143
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 41055301    167 mdVHSRYRTEAHQDVIGRFNERFILSLSSCKSCVVID 203
Cdd:pfam08351  144 --FHKSLVTPPYEDVKGRFNRRFIRSLLEHEGILIVD 178
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
616-656 1.73e-04

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: 42.32  E-value: 1.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41055301    616 QDSEFAGLSGGRIVR-------IAVNPDYQGMGYGTRALQLLQRYYEG 656
Cdd:TIGR01575   38 IGGKVVGYAGVQIVLdeahilnIAVKPEYQGQGIGRALLRELIDEAKG 85
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
626-653 4.25e-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: 36.48  E-value: 4.25e-03
                         10        20
                 ....*....|....*....|....*...
gi 41055301  626 GRIVRIAVNPDYQGMGYGTRALQLLQRY 653
Cdd:cd04301   26 AYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
GNAT_acetyltr_2 pfam13718
GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related ...
530-754 1.47e-136

GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related N-acetyltransferase (GNAT) fold.


Pssm-ID: 463966 [Multi-domain]  Cd Length: 227  Bit Score: 409.69  E-value: 1.47e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    530 RLMALYVASHYKNSPNDLQMLSDAPAHHLFCLLPPVPPTQNSLPEVLAVLQVCLEGEISRQSILSSLSRGKKASGDLIPW 609
Cdd:pfam13718    1 RLMALYVASHYKNSPNDLQLLSDAPAHHLFVLLGPVDESGNALPDILCVVQVALEGRISRESVKNSLSRGKRASGDLIPW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    610 TVSEQFQDSEFAGLSGGRIVRIAVNPDYQGMGYGTRALQLLQRYYEGQFPLWDEQEQTMTSAITSVSSEA--VSLLEEVV 687
Cdd:pfam13718   81 TVSQQFQDEDFASLSGARIVRIATHPEYQGMGYGSRALELLIQYYEGKITDLSEAEELEEEEADRIEDEEsaVSLLEEKI 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055301    688 SPRKDLPPLLLKLNERRAERLDYLGVSYGLTPQPLKFWKKAGFVPVYLRQTPNDLTGEHSCIMLKDL 754
Cdd:pfam13718  161 RPRKELPPLLLKLSERPPERLDYLGVSFGLTPDLLKFWKRAGFVPVYLRQTPNELTGEHSCIMLRPL 227
tRNA_bind_2 pfam13725
Possible tRNA binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
765-978 1.58e-109

Possible tRNA binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine acetyltransferase, may be involved in tRNA-binding.


Pssm-ID: 463969  Cd Length: 231  Bit Score: 339.11  E-value: 1.58e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    765 WLSAFWKDFRRRFLSLMSFQFSKFSSTLALNILQNKSA-----KDDSTAVLTSAELAATFTPYDLKRLEMYSRNMVDYHL 839
Cdd:pfam13725    1 WLGAFAKDFRRRFLSLLSYQFRKFPSVLALSILESANAgakldPSTEPKPLTKAELDALLSPFDLKRLESYANNMLDYHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    840 IMDMIPVIARMHFLKQFG-DISLSVAQSALLLGIGLQHKSVDELEKEIGLPSSQLMGLFNRIIRKVVQFFNTLQERAVEA 918
Cdd:pfam13725   81 ILDLLPTLARLYFTGRLPsDVKLSGVQSAILLAIGLQRKDIDDLEKELNLPSNQLLALFNKIMRKISKYFRSIQEKAIEA 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055301    919 EMVATKDI----------GLEPTVQTLNEDLNDAAKEFDEKHK-KDIEKIKDMNLSEYMIRGDDEEWDQVL 978
Cdd:pfam13725  161 TLPKLKDIsahddevkdeDLEPLEQSLDEELEEAAKEVEEKLKeKQRELIDSLDLDKYAIKGDEEDWEKAL 231
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
12-906 2.95e-99

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 328.33  E-value: 2.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301   12 IRVQIENGVAEHHRSMFVIVGDRGrdqvvilhhmlskatvrarpsvlWCYKkelgfssnrkkRMRQLQKKIKTGTLNLNQ 91
Cdd:COG1444    4 LRALRAEARRAGHRRLLVLSGDDE-----------------------WCRA-----------QAEALLEALPGDWLWVGE 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301   92 DDPFELfvaatniRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGIVVILlrtMNSLKQLYTMTMDVHS 171
Cdd:COG1444   50 RPPLGV-------EHIPPSAARRLLGREFDHVVFDAHDGFDPNALGALSGTVRGGGLLVLL---TPPLDEWPQRPDPDSL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  172 RYRTEAHQDVIGRFNERFILSLSSCKSCVVID-DQLNILPisshatnikPIPPKKqddgLSPREqelkdlkeslqdtqpv 250
Cdd:COG1444  120 RLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDqDSPLIDP---------ELPAKA----RFPRP---------------- 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  251 gvLVDGCKTLDQAKAvLKFIEAISEKtlRSTVALTAARGRGKSAALGLAMAGAVAFGYSnIFVTSPSPDNLHTLFEFVFK 330
Cdd:COG1444  171 --AYEGCLTADQAAA-LAALERLAER--KRVLVLTADRGRGKSAAAGLAAARLAAEGGR-VLVTAPSKAAVEELFEFAGE 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  331 GFDALQYQEHLDYEIIQSlnpefnkavvrvnifkehrqtIQYIHPADAVKL-GQAELLVIDEAAAIPLPLVKKLLG--PY 407
Cdd:COG1444  245 LLEALGVKYRELTGAGGR---------------------VRFVAPDALLERpPDADLLLVDEAAAIPVPLLEKLLAafPR 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  408 LVFmASTINGYEGTGRSLSLKLIQQLRQQssesqqnlsaenrntstarlaaARSLHEVTLHESIRYGQGDHVERWLN--- 484
Cdd:COG1444  304 VVF-TTTVHGYEGTGRGFLLRFCARLDES----------------------TPGWRELTLDEPIRWAAGDPLERWLFral 360
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  485 ----DLLCLDCLSVPriisgcplPQTCDLYYVNRDTLFcyhkASEAFLQRLMALYVASHYKNSPNDLQMLSDAPAHHLFC 560
Cdd:COG1444  361 lldaEPAVLQLVDAP--------PGEVEYERLDQDELL----ADEELLRQLFGLLVLAHYRTSPDDLRRLLDAPNQHFRA 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  561 LlppvppTQNslPEVLAVLQVCLEGEIS---RQSILsslsRGK-KASGDLIPWTVSEQFQDSEFAGLSGGRIVRIAVNPD 636
Cdd:COG1444  429 L------RTG--GKVVGVAWLAEEGGLDaelAEAVW----AGRrRPRGNLVPQSLAAHLGLPEAATLRGWRIVRIAVHPA 496
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  637 YQGMGYGTRalqllqryyegqfplwdeqeqtmtsaitsvsseavsLLEEVVsprkdlpplllklNERRAERLDYLGVSYG 716
Cdd:COG1444  497 LQRRGLGSR------------------------------------LLAEIR-------------EEAKEEGLDWLGVSFG 527
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  717 LTPQPLKFWKKAGFVPVYLRQTPNDLTGEHSCIMLKDLNS--EDLTDQ-NQWlsafwkdFRRRFLSLMSFQFSKFSSTLA 793
Cdd:COG1444  528 ATPELLRFWQRNGFVPVHLGTTRNASSGEYSAMVLKPLSEagEALVDRaARR-------FARDLPNLLSDPLRDLDPDVA 600
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301  794 LNILQNksakddstavlTSAELAATFTPYDLKRLEMYSRNMVDYHLIMDMIPVIARMHFLKqfGDISLSVAQSALLLGIG 873
Cdd:COG1444  601 RALLRA-----------LPADADPELSDEDWRELAGFAFGHRPYEASLDALRRLLLAYLLD--PRADLSPREERLLVAKV 667
                        890       900       910
                 ....*....|....*....|....*....|....
gi 41055301  874 LQHKSVDELEKEIGLPS-SQLMGLFNRIIRKVVQ 906
Cdd:COG1444  668 LQGRSWEEVAEELGLSGrKALLRALRDAVAQLLD 701
TmcA_N pfam08351
tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is ...
11-203 7.36e-71

tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is often found at the N-terminus of the bacterial tRNA(Met) cytidine acetyltransferase TmcA. TmcA catalyzes the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met) by using acetyl-CoA as an acetyl donor and either ATP or GTP. This modification is thought to ensure precise recognition of the AUG codon by strengthening C-G base-pair interaction and also prevent misrecognition of the near cognate AUA codon. This domain is also found in mammalian N-acetyltransferase 10 (NAT10) and fungal protein Kre33. Kre33 and NAT10 are RNA cytosine acetyltransferases with specificity toward both 18S rRNA and tRNAs and contain additional putative nuclear and nucleolar localization signals (NLS and NoLS respectively).


Pssm-ID: 462441 [Multi-domain]  Cd Length: 178  Bit Score: 232.95  E-value: 7.36e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301     11 RIRVQIENGVAEHHRSMFVIVGDRG----RDQVVILHHMLSKATvRARPSVLWCYKKELgfsSNRKKRMRQLQKKIKTGT 86
Cdd:pfam08351    2 RLRKLLEDAVKANHRRLVVIVGDDPelhvKEQVPNYHRILSRLS-SSKPSVLYCYHPEF---FDAKKRKKEFKKLVKRGE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301     87 LNLNqddpfelfvaatnIRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGIVVILLRTMNSLKQLYTMt 166
Cdd:pfam08351   78 LDIE-------------IEYIDYKESEKVLGQTYDMLVLDLFEDLTPNDLGRLVETVRGGGLIILLLPPLDSWKQLYTI- 143
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 41055301    167 mdVHSRYRTEAHQDVIGRFNERFILSLSSCKSCVVID 203
Cdd:pfam08351  144 --FHKSLVTPPYEDVKGRFNRRFIRSLLEHEGILIVD 178
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
283-482 1.39e-59

Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase activity, and a Walker B motif. In tRNA(Met) cytidine acetyltransferase (TmcA) it may function as an RNA helicase motor (driven by ATP hydrolysis) which delivers the wobble base to the active centre of the GCN5-related N-acetyltransferase (GNAT) domain. It is found in the bacterial exodeoxyribonuclease V alpha chain (RecD), which has 5'-3' helicase activity. It is structurally similar to the motor domain 1A in other SF1 helicases.


Pssm-ID: 461555 [Multi-domain]  Cd Length: 171  Bit Score: 201.22  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    283 ALTAARGRGKSAALGLAMAGAVAFGYSNIFVTSPSPDNLHTLFEFVFKGFDALQYQehldyeiiqslnPEFNKAVVRVNi 362
Cdd:pfam05127    1 VITADRGRGKSAALGLAAAALIAQGYSRIIVTAPSPANVQTLFEFAIKGLDALGLT------------PKFRDGIIRGN- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055301    363 fkehRQTIQYIHPADAVKL-GQAELLVIDEAAAIPLPLVKKLL-GPYLVFMASTINGYEGTGRSLSLKLIQQLRQQSses 440
Cdd:pfam05127   68 ----GQRIRFIAPDELLKLpGQADLLVVDEAAAIPLPLLKQLLrGFPRVVFATTVHGYEGTGRGFSLKFLAQLKKQL--- 140
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 41055301    441 qqnlsaenrntstarlaaaRSLHEVTLHESIRYGQGDHVERW 482
Cdd:pfam05127  141 -------------------PGLRELELTEPIRYAEGDPLEKW 163
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
616-656 1.73e-04

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: 42.32  E-value: 1.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41055301    616 QDSEFAGLSGGRIVR-------IAVNPDYQGMGYGTRALQLLQRYYEG 656
Cdd:TIGR01575   38 IGGKVVGYAGVQIVLdeahilnIAVKPEYQGQGIGRALLRELIDEAKG 85
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
626-657 1.22e-03

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: 39.81  E-value: 1.22e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 41055301    626 GRIVRIAVNPDYQGMGYGTRALQLLQRYYEGQ 657
Cdd:pfam00583   60 GEIEGLAVAPEYRGKGIGTALLQALLEWARER 91
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
626-653 4.25e-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: 36.48  E-value: 4.25e-03
                         10        20
                 ....*....|....*....|....*...
gi 41055301  626 GRIVRIAVNPDYQGMGYGTRALQLLQRY 653
Cdd:cd04301   26 AYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
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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