NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16130399|ref|NP_416969|]
View 

tRNA(Met) cytidine acetyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

tRNA(Met) cytidine acetyltransferase TmcA( domain architecture ID 11444527)

tRNA(Met) cytidine acetyltransferase 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-652 0e+00

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: 865.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   4 LTALHTLTAQMKREGIRRLLVLSGEEGWCFEHTLKLRDALPGDWLWISPRPDAE-NHCSPSALQTLLGREFRHAVFDARH 82
Cdd:COG1444   1 LDLLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGvEHIPPSAARRLLGREFDHVVFDAHD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399  83 GFDAAAFAALSGTLKAGSWLVLLLPVWEEWENQPDADSLRWSDCPDPIATPHFVQHLKRVLTADNEAILWRQNQPFsLAH 162
Cdd:COG1444  81 GFDPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDQDSPL-IDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 163 FTPRTDWYP---ATGAPQPEQQQLLKQLMTM--PPGVAAVTAARGRGKSALAGQLISRIA---GRAIVTAPAKASTDVLA 234
Cdd:COG1444 160 ELPAKARFPrpaYEGCLTADQAAALAALERLaeRKRVLVLTADRGRGKSAAAGLAAARLAaegGRVLVTAPSKAAVEELF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 235 QFAGE-----------------KFRFIAPDALLASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRG 297
Cdd:COG1444 240 EFAGEllealgvkyreltgaggRVRFVAPDALLERPPDADLLLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTGRG 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 298 FLLKFCARF----PHLHRFELQQPIRWAQGCPLEKMVSEALVFDDENFTHT----PQGNIVISAFEQTLWQSDPETPLKV 369
Cdd:COG1444 320 FLLRFCARLdestPGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLQlvdaPPGEVEYERLDQDELLADEELLRQL 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 370 YQLLSGAHYRTSPLDLRRMMDAPGQHFLQAAGENEIAGALWLVDEGGLSQQLSQAVWAGFRRPRGNLVAQSLAAHGNNPL 449
Cdd:COG1444 400 FGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGLPE 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 450 AATLRGRRVSRIAVHPARQREGTGRQLIAGALQYT--QDLDYLSVSFGYTGELWRFWQRCGFVLVRMGNHREASSGCYTA 527
Cdd:COG1444 480 AATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAkeEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEYSA 559

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 528 MALLPMSDAGKQLAEREHYRLRRDA--------QALAQWNGETLP--VDPLNDAVLSDDDWLELAGFAFAHRPLLTSLGC 597
Cdd:COG1444 560 MVLKPLSEAGEALVDRAARRFARDLpnllsdplRDLDPDVARALLraLPADADPELSDEDWRELAGFAFGHRPYEASLDA 639

                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130399 598 LLRLLQT---------SELALPALRGRLQKNASDAQLCTTLKLSGRKMLLVRQREEAAQALFAL 652
Cdd:COG1444 640 LRRLLLAylldpradlSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLLDAY 703
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-652 0e+00

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: 865.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   4 LTALHTLTAQMKREGIRRLLVLSGEEGWCFEHTLKLRDALPGDWLWISPRPDAE-NHCSPSALQTLLGREFRHAVFDARH 82
Cdd:COG1444   1 LDLLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGvEHIPPSAARRLLGREFDHVVFDAHD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399  83 GFDAAAFAALSGTLKAGSWLVLLLPVWEEWENQPDADSLRWSDCPDPIATPHFVQHLKRVLTADNEAILWRQNQPFsLAH 162
Cdd:COG1444  81 GFDPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDQDSPL-IDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 163 FTPRTDWYP---ATGAPQPEQQQLLKQLMTM--PPGVAAVTAARGRGKSALAGQLISRIA---GRAIVTAPAKASTDVLA 234
Cdd:COG1444 160 ELPAKARFPrpaYEGCLTADQAAALAALERLaeRKRVLVLTADRGRGKSAAAGLAAARLAaegGRVLVTAPSKAAVEELF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 235 QFAGE-----------------KFRFIAPDALLASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRG 297
Cdd:COG1444 240 EFAGEllealgvkyreltgaggRVRFVAPDALLERPPDADLLLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTGRG 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 298 FLLKFCARF----PHLHRFELQQPIRWAQGCPLEKMVSEALVFDDENFTHT----PQGNIVISAFEQTLWQSDPETPLKV 369
Cdd:COG1444 320 FLLRFCARLdestPGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLQlvdaPPGEVEYERLDQDELLADEELLRQL 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 370 YQLLSGAHYRTSPLDLRRMMDAPGQHFLQAAGENEIAGALWLVDEGGLSQQLSQAVWAGFRRPRGNLVAQSLAAHGNNPL 449
Cdd:COG1444 400 FGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGLPE 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 450 AATLRGRRVSRIAVHPARQREGTGRQLIAGALQYT--QDLDYLSVSFGYTGELWRFWQRCGFVLVRMGNHREASSGCYTA 527
Cdd:COG1444 480 AATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAkeEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEYSA 559

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 528 MALLPMSDAGKQLAEREHYRLRRDA--------QALAQWNGETLP--VDPLNDAVLSDDDWLELAGFAFAHRPLLTSLGC 597
Cdd:COG1444 560 MVLKPLSEAGEALVDRAARRFARDLpnllsdplRDLDPDVARALLraLPADADPELSDEDWRELAGFAFGHRPYEASLDA 639

                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130399 598 LLRLLQT---------SELALPALRGRLQKNASDAQLCTTLKLSGRKMLLVRQREEAAQALFAL 652
Cdd:COG1444 640 LRRLLLAylldpradlSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLLDAY 703
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
 196-337 6.68e-62

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: 203.53  E-value: 6.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   196 AVTAARGRGKSALAG----QLISRIAGRAIVTAPAKASTDVLAQFA---------------------GEKFRFIAPDALL 250
Cdd:pfam05127   1 VITADRGRGKSAALGlaaaALIAQGYSRIIVTAPSPANVQTLFEFAikgldalgltpkfrdgiirgnGQRIRFIAPDELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   251 ASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRGFLLKFCAR----FPHLHRFELQQPIRWAQGCPL 326
Cdd:pfam05127  81 KLPGQADLLVVDEAAAIPLPLLKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQlkkqLPGLRELELTEPIRYAEGDPL 160

                         170
                  ....*....|.
gi 16130399   327 EKMVSEALVFD 337
Cdd:pfam05127 161 EKWLNDLLLLD 171
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-652 0e+00

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: 865.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   4 LTALHTLTAQMKREGIRRLLVLSGEEGWCFEHTLKLRDALPGDWLWISPRPDAE-NHCSPSALQTLLGREFRHAVFDARH 82
Cdd:COG1444   1 LDLLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGvEHIPPSAARRLLGREFDHVVFDAHD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399  83 GFDAAAFAALSGTLKAGSWLVLLLPVWEEWENQPDADSLRWSDCPDPIATPHFVQHLKRVLTADNEAILWRQNQPFsLAH 162
Cdd:COG1444  81 GFDPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDQDSPL-IDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 163 FTPRTDWYP---ATGAPQPEQQQLLKQLMTM--PPGVAAVTAARGRGKSALAGQLISRIA---GRAIVTAPAKASTDVLA 234
Cdd:COG1444 160 ELPAKARFPrpaYEGCLTADQAAALAALERLaeRKRVLVLTADRGRGKSAAAGLAAARLAaegGRVLVTAPSKAAVEELF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 235 QFAGE-----------------KFRFIAPDALLASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRG 297
Cdd:COG1444 240 EFAGEllealgvkyreltgaggRVRFVAPDALLERPPDADLLLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTGRG 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 298 FLLKFCARF----PHLHRFELQQPIRWAQGCPLEKMVSEALVFDDENFTHT----PQGNIVISAFEQTLWQSDPETPLKV 369
Cdd:COG1444 320 FLLRFCARLdestPGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLQlvdaPPGEVEYERLDQDELLADEELLRQL 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 370 YQLLSGAHYRTSPLDLRRMMDAPGQHFLQAAGENEIAGALWLVDEGGLSQQLSQAVWAGFRRPRGNLVAQSLAAHGNNPL 449
Cdd:COG1444 400 FGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGLPE 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 450 AATLRGRRVSRIAVHPARQREGTGRQLIAGALQYT--QDLDYLSVSFGYTGELWRFWQRCGFVLVRMGNHREASSGCYTA 527
Cdd:COG1444 480 AATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAkeEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEYSA 559

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 528 MALLPMSDAGKQLAEREHYRLRRDA--------QALAQWNGETLP--VDPLNDAVLSDDDWLELAGFAFAHRPLLTSLGC 597
Cdd:COG1444 560 MVLKPLSEAGEALVDRAARRFARDLpnllsdplRDLDPDVARALLraLPADADPELSDEDWRELAGFAFGHRPYEASLDA 639

                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130399 598 LLRLLQT---------SELALPALRGRLQKNASDAQLCTTLKLSGRKMLLVRQREEAAQALFAL 652
Cdd:COG1444 640 LRRLLLAylldpradlSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLLDAY 703
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
 196-337 6.68e-62

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: 203.53  E-value: 6.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   196 AVTAARGRGKSALAG----QLISRIAGRAIVTAPAKASTDVLAQFA---------------------GEKFRFIAPDALL 250
Cdd:pfam05127   1 VITADRGRGKSAALGlaaaALIAQGYSRIIVTAPSPANVQTLFEFAikgldalgltpkfrdgiirgnGQRIRFIAPDELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   251 ASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRGFLLKFCAR----FPHLHRFELQQPIRWAQGCPL 326
Cdd:pfam05127  81 KLPGQADLLVVDEAAAIPLPLLKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQlkkqLPGLRELELTEPIRYAEGDPL 160

                         170
                  ....*....|.
gi 16130399   327 EKMVSEALVFD 337
Cdd:pfam05127 161 EKWLNDLLLLD 171
tRNA_bind_3 pfam17176
tRNA-binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
 537-655 1.91e-46

tRNA-binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine acyltransferase, may be involved in tRNA-binding. This family represents the tRNA-binding domain proteins not captured by pfam13725.


Pssm-ID: 465371  Cd Length: 119  Bit Score: 160.18  E-value: 1.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   537 GKQLAEREHYRLRRDAQALAQWNGETLPVDPLNDAVLSDDDWLELAGFAFAHRPLLTSLGCLLRLLQTSELALPALRGRL 616
Cdd:pfam17176   1 GEALAQQAHQRLARDWRWLRQWIGLALPLPPPADQTLNDEDWRELAGFAFAHRPLEASLGALQRLLLRSSLPLPALRARL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 16130399   617 QKNASDAQLCTTLKLSGRKMLLVRQREEAAQALFALNDV 655
Cdd:pfam17176  81 QQQQSDAEIAALLGLSGRKALLARWREEAAQALAALDAA 119
GNAT_acetyltr_2 pfam13718
GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related ...
 372-512 1.05e-15

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: 76.88  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   372 LLSGAHYRTSPLDLRRMMDAPGQHFLQAAGEN--------EIAGALWLVDEGGLSQQLSQAVWAGFRRPRGNLVAQSLAA 443
Cdd:pfam13718   5 LYVASHYKNSPNDLQLLSDAPAHHLFVLLGPVdesgnalpDILCVVQVALEGRISRESVKNSLSRGKRASGDLIPWTVSQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   444 HGNNPLAATLRGRRVSRIAVHPARQREGTGRQ------------------------------------------------ 475
Cdd:pfam13718  85 QFQDEDFASLSGARIVRIATHPEYQGMGYGSRalelliqyyegkitdlseaeeleeeeadriedeesavslleekirprk 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 16130399   476 -----LIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFVLV 512
Cdd:pfam13718 165 elpplLLKLSERPPERLDYLGVSFGLTPDLLKFWKRAGFVPV 206
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
458-530 1.76e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 45.08  E-value: 1.76e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130399 458 VSRIAVHPARQREGTGRQLIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFVLVRMGNHREASSGCYTAMAL 530
Cdd:COG3153  70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
TmcA_N pfam08351
tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is ...
 16-145 3.63e-05

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: 44.97  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399    16 REGIRRLLVLSGEEGWC--------FEHTLKLRDALPGDWLWIsPRPDAEN----------------------HCSPSAL 65
Cdd:pfam08351  12 KANHRRLVVIVGDDPELhvkeqvpnYHRILSRLSSSKPSVLYC-YHPEFFDakkrkkefkklvkrgeldieieYIDYKES 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399    66 QTLLGREFRHAVFDARHGFDAAAFAALSGTLKAGSWLVLLLPVWEEWENQPDADSLRWSDCPDPIATPHFVQHLKRVLTA 145
Cdd:pfam08351  91 EKVLGQTYDMLVLDLFEDLTPNDLGRLVETVRGGGLIILLLPPLDSWKQLYTIFHKSLVTPPYEDVKGRFNRRFIRSLLE 170
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 460-510 3.94e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.44  E-value: 3.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16130399   460 RIAVHPARQREGTGRQLIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFV 510
Cdd:pfam13508  33 RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 178-282 4.40e-05

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 44.86  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399   178 PEQQQLLKQLMTMPPGVAAVTAARGRGKS-ALAG--QLISRIAGRAIVTAPAKASTDVLAQFAGEKFRFIA----PDALL 250
Cdd:pfam13604   4 AEQAAAVRALLTSGDRVAVLVGPAGTGKTtALKAlrEAWEAAGYRVIGLAPTGRAAKVLGEELGIPADTIAkllhRLGGR 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 16130399   251 ASDEQADWLVVDEAAAIPAPLLHQLVSRFPRT 282
Cdd:pfam13604  84 AGLDPGTLLIVDEAGMVGTRQMARLLKLAEDA 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 458-513 1.43e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 41.18  E-value: 1.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 458 VSRIAVHPARQREGTGRQLIAGALQYTQDLD----YLSVSFGYTGeLWRFWQRCGFVLVR 513
Cdd:COG0456  16 IEDLAVDPEYRGRGIGRALLEAALERARERGarrlRLEVREDNEA-AIALYEKLGFEEVG 74
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 458-512 9.38e-04

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: 39.98  E-value: 9.38e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130399 458 VSRIAVHPARQREGTGRQLIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFVLV 512
Cdd:COG1246  55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEI 109
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 148-281 1.97e-03

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 41.12  E-value: 1.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130399 148 EAILWRQNQPFSLAHFTPRTDWYPATGAPQ--PEQQQLLKQLMTmPPGVAAVTAARGRGKSALAGQLIS---RIAGRAIV 222
Cdd:COG0507  95 RRLRRLARPALDEADVEAALAALEPRAGITlsDEQREAVALALT-TRRVSVLTGGAGTGKTTTLRALLAaleALGLRVAL 173

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130399 223 TAP-------------AKASTdvLAQF-----AGEKFRFIAPDALLAsdeqADWLVVDEAAAIPAPLLHQLVSRFPR 281
Cdd:COG0507 174 AAPtgkaakrlsestgIEART--IHRLlglrpDSGRFRHNRDNPLTP----ADLLVVDEASMVDTRLMAALLEALPR 244
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
441-512 2.48e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.63  E-value: 2.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130399 441 LAAHGNNPLAATLR-------GRRVSRIAVHPARQREGTGRQLIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFVLV 512
Cdd:COG2153  37 LLAYDDGELVATARllppgdgEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPV 115
 
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