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Conserved domains on  [gi|727181529|ref|WP_033644001|]
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MULTISPECIES: tRNA(Met) cytidine acetyltransferase TmcA [Serratia]

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

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List of domain hits

 Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-654 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: 822.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529   1 MLQAAQQLMRRQGIRRLLVLSGEPEWCREQAQRLAATLPGDWPWVGENPPPGQAALASGAVRQLLGQERLHAVFDAGHSL 80
Cdd:COG1444    3 LLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGVEHIPPSAARRLLGREFDHVVFDAHDGF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  81 DVEALAALSGALRAGSWLLLLTPPWRQWAQLPDGDSLRWSDCPQPITTPHFIHHLQQHLTDDSEVTIWRQDEPLTLAALP 160
Cdd:COG1444   83 DPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDQDSPLIDPELP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 161 --VREGWQPPDGRPTEEQQAILTALLQA--ESGVWVLTAARGRGKSTLAGMLVAQSPL---TCWITGPSRAATAVAGEWA 233
Cdd:COG1444  163 akARFPRPAYEGCLTADQAAALAALERLaeRKRVLVLTADRGRGKSAAAGLAAARLAAeggRVLVTAPSKAAVEELFEFA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 234 -----------------QGRAQFWAPDALLAQCREGDvsavgWLLVDEAAAIPAPLLQQLIGYFPRVLLTTTVQGYEGTG 296
Cdd:COG1444  243 gellealgvkyreltgaGGRVRFVAPDALLERPPDAD-----LLLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 297 RGFLLKFCAGL----PAYQALSLHQPMRWAQGDALERITDNALLFNELPAWP----ADGQAIDYSQAEQGELCADPQRLA 368
Cdd:COG1444  318 RGFLLRFCARLdestPGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLqlvdAPPGEVEYERLDQDELLADEELLR 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 369 RFYALLSSAHYRTSPLDLRRLMDAPGMHFGLAQAGLEVVGAVWLVEEGGLSAELAHDVWAGRRRPRGNLVAQSLAAHGGQ 448
Cdd:COG1444  398 QLFGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGL 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 449 WWAPTLRSRRITRIATLPALRRRGIARQLIERQRRQA--QGLDFLSVSFGYTEPLWRFWQSCGFELVRIGSKPEASSGCY 526
Cdd:COG1444  478 PEAATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAkeEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEY 557

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 527 TAMAILPLSEQGEALRHAAHKHLARDWP--------WLRQRIELTL--AIPGDDgDTSLGEEDWRELAGFAFAHRPLEAS 596
Cdd:COG1444  558 SAMVLKPLSEAGEALVDRAARRFARDLPnllsdplrDLDPDVARALlrALPADA-DPELSDEDWRELAGFAFGHRPYEAS 636

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181529 597 LGALQRLLLASSLPLPAL---------RGHLQRRHSPAECAERAGVSGQKALLRHWRHETAQALEQL 654
Cdd:COG1444  637 LDALRRLLLAYLLDPRADlspreerllVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLLDAY 703
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-654 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: 822.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529   1 MLQAAQQLMRRQGIRRLLVLSGEPEWCREQAQRLAATLPGDWPWVGENPPPGQAALASGAVRQLLGQERLHAVFDAGHSL 80
Cdd:COG1444    3 LLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGVEHIPPSAARRLLGREFDHVVFDAHDGF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  81 DVEALAALSGALRAGSWLLLLTPPWRQWAQLPDGDSLRWSDCPQPITTPHFIHHLQQHLTDDSEVTIWRQDEPLTLAALP 160
Cdd:COG1444   83 DPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDQDSPLIDPELP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 161 --VREGWQPPDGRPTEEQQAILTALLQA--ESGVWVLTAARGRGKSTLAGMLVAQSPL---TCWITGPSRAATAVAGEWA 233
Cdd:COG1444  163 akARFPRPAYEGCLTADQAAALAALERLaeRKRVLVLTADRGRGKSAAAGLAAARLAAeggRVLVTAPSKAAVEELFEFA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 234 -----------------QGRAQFWAPDALLAQCREGDvsavgWLLVDEAAAIPAPLLQQLIGYFPRVLLTTTVQGYEGTG 296
Cdd:COG1444  243 gellealgvkyreltgaGGRVRFVAPDALLERPPDAD-----LLLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 297 RGFLLKFCAGL----PAYQALSLHQPMRWAQGDALERITDNALLFNELPAWP----ADGQAIDYSQAEQGELCADPQRLA 368
Cdd:COG1444  318 RGFLLRFCARLdestPGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLqlvdAPPGEVEYERLDQDELLADEELLR 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 369 RFYALLSSAHYRTSPLDLRRLMDAPGMHFGLAQAGLEVVGAVWLVEEGGLSAELAHDVWAGRRRPRGNLVAQSLAAHGGQ 448
Cdd:COG1444  398 QLFGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGL 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 449 WWAPTLRSRRITRIATLPALRRRGIARQLIERQRRQA--QGLDFLSVSFGYTEPLWRFWQSCGFELVRIGSKPEASSGCY 526
Cdd:COG1444  478 PEAATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAkeEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEY 557

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 527 TAMAILPLSEQGEALRHAAHKHLARDWP--------WLRQRIELTL--AIPGDDgDTSLGEEDWRELAGFAFAHRPLEAS 596
Cdd:COG1444  558 SAMVLKPLSEAGEALVDRAARRFARDLPnllsdplrDLDPDVARALlrALPADA-DPELSDEDWRELAGFAFGHRPYEAS 636

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181529 597 LGALQRLLLASSLPLPAL---------RGHLQRRHSPAECAERAGVSGQKALLRHWRHETAQALEQL 654
Cdd:COG1444  637 LDALRRLLLAYLLDPRADlspreerllVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLLDAY 703
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
 192-338 2.31e-55

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: 186.20  E-value: 2.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  192 VLTAARGRGKSTLAGM----LVAQSPLTCWITGPSRAATAVAGEWAQ---------------------GRAQFWAPDALL 246
Cdd:pfam05127   1 VITADRGRGKSAALGLaaaaLIAQGYSRIIVTAPSPANVQTLFEFAIkgldalgltpkfrdgiirgngQRIRFIAPDELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  247 AQCREGDvsavgWLLVDEAAAIPAPLLQQLIGYFPRVLLTTTVQGYEGTGRGFLLKFCAGL----PAYQALSLHQPMRWA 322
Cdd:pfam05127  81 KLPGQAD-----LLVVDEAAAIPLPLLKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQLkkqlPGLRELELTEPIRYA 155

                         170
                  ....*....|....*.
gi 727181529  323 QGDALERITDNALLFN 338
Cdd:pfam05127 156 EGDPLEKWLNDLLLLD 171
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-654 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: 822.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529   1 MLQAAQQLMRRQGIRRLLVLSGEPEWCREQAQRLAATLPGDWPWVGENPPPGQAALASGAVRQLLGQERLHAVFDAGHSL 80
Cdd:COG1444    3 LLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGVEHIPPSAARRLLGREFDHVVFDAHDGF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  81 DVEALAALSGALRAGSWLLLLTPPWRQWAQLPDGDSLRWSDCPQPITTPHFIHHLQQHLTDDSEVTIWRQDEPLTLAALP 160
Cdd:COG1444   83 DPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRKLREHPGVAIWDQDSPLIDPELP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 161 --VREGWQPPDGRPTEEQQAILTALLQA--ESGVWVLTAARGRGKSTLAGMLVAQSPL---TCWITGPSRAATAVAGEWA 233
Cdd:COG1444  163 akARFPRPAYEGCLTADQAAALAALERLaeRKRVLVLTADRGRGKSAAAGLAAARLAAeggRVLVTAPSKAAVEELFEFA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 234 -----------------QGRAQFWAPDALLAQCREGDvsavgWLLVDEAAAIPAPLLQQLIGYFPRVLLTTTVQGYEGTG 296
Cdd:COG1444  243 gellealgvkyreltgaGGRVRFVAPDALLERPPDAD-----LLLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 297 RGFLLKFCAGL----PAYQALSLHQPMRWAQGDALERITDNALLFNELPAWP----ADGQAIDYSQAEQGELCADPQRLA 368
Cdd:COG1444  318 RGFLLRFCARLdestPGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLqlvdAPPGEVEYERLDQDELLADEELLR 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 369 RFYALLSSAHYRTSPLDLRRLMDAPGMHFGLAQAGLEVVGAVWLVEEGGLSAELAHDVWAGRRRPRGNLVAQSLAAHGGQ 448
Cdd:COG1444  398 QLFGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGL 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 449 WWAPTLRSRRITRIATLPALRRRGIARQLIERQRRQA--QGLDFLSVSFGYTEPLWRFWQSCGFELVRIGSKPEASSGCY 526
Cdd:COG1444  478 PEAATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAkeEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEY 557

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 527 TAMAILPLSEQGEALRHAAHKHLARDWP--------WLRQRIELTL--AIPGDDgDTSLGEEDWRELAGFAFAHRPLEAS 596
Cdd:COG1444  558 SAMVLKPLSEAGEALVDRAARRFARDLPnllsdplrDLDPDVARALlrALPADA-DPELSDEDWRELAGFAFGHRPYEAS 636

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181529 597 LGALQRLLLASSLPLPAL---------RGHLQRRHSPAECAERAGVSGQKALLRHWRHETAQALEQL 654
Cdd:COG1444  637 LDALRRLLLAYLLDPRADlspreerllVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLLDAY 703
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
 192-338 2.31e-55

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: 186.20  E-value: 2.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  192 VLTAARGRGKSTLAGM----LVAQSPLTCWITGPSRAATAVAGEWAQ---------------------GRAQFWAPDALL 246
Cdd:pfam05127   1 VITADRGRGKSAALGLaaaaLIAQGYSRIIVTAPSPANVQTLFEFAIkgldalgltpkfrdgiirgngQRIRFIAPDELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  247 AQCREGDvsavgWLLVDEAAAIPAPLLQQLIGYFPRVLLTTTVQGYEGTGRGFLLKFCAGL----PAYQALSLHQPMRWA 322
Cdd:pfam05127  81 KLPGQAD-----LLVVDEAAAIPLPLLKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQLkkqlPGLRELELTEPIRYA 155

                         170
                  ....*....|....*.
gi 727181529  323 QGDALERITDNALLFN 338
Cdd:pfam05127 156 EGDPLEKWLNDLLLLD 171
tRNA_bind_3 pfam17176
tRNA-binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
 538-657 2.14e-36

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: 132.45  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  538 GEALRHAAHKHLARDWPWLRQRIELTLAIPgDDGDTSLGEEDWRELAGFAFAHRPLEASLGALQRLLLASSLPLPALRGH 617
Cdd:pfam17176   1 GEALAQQAHQRLARDWRWLRQWIGLALPLP-PPADQTLNDEDWRELAGFAFAHRPLEASLGALQRLLLRSSLPLPALRAR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 727181529  618 LQRRHSPAECAERAGVSGQKALLRHWRHETAQALEQLNAQ 657
Cdd:pfam17176  80 LQQQQSDAEIAALLGLSGRKALLARWREEAAQALAALDAA 119
GNAT_acetyltr_2 pfam13718
GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related ...
 369-534 2.45e-14

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: 72.64  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  369 RFYALLSSAHYRTSPLDLRRLMDAPGMH-FGL-------AQAGLEVVGAVWLVEEGGLSAELAHDVWAGRRRPRGNLVAQ 440
Cdd:pfam13718   1 RLMALYVASHYKNSPNDLQLLSDAPAHHlFVLlgpvdesGNALPDILCVVQVALEGRISRESVKNSLSRGKRASGDLIPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529  441 SLAAHGGQWWAPTLRSRRITRIATLPALRRRGI---ARQLIERQR----------------------------------- 482
Cdd:pfam13718  81 TVSQQFQDEDFASLSGARIVRIATHPEYQGMGYgsrALELLIQYYegkitdlseaeeleeeeadriedeesavslleeki 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181529  483 ---------------RQAQGLDFLSVSFGYTEPLWRFWQSCGFELVRIGSKPEASSGCYTAMAILPL 534
Cdd:pfam13718 161 rprkelpplllklseRPPERLDYLGVSFGLTPDLLKFWKRAGFVPVYLRQTPNELTGEHSCIMLRPL 227
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 461-511 4.38e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.44  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 727181529  461 RIATLPALRRRGIARQLIERQRRQAQGLDFLSVSFGYTEPLWRFWQSCGFE 511
Cdd:pfam13508  33 RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 459-515 5.14e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 42.34  E-value: 5.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181529 459 ITRIATLPALRRRGIARQLIERQRRQAQGLDFLSVSFGYTE---PLWRFWQSCGFELVRI 515
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREdneAAIALYEKLGFEEVGE 75
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 459-521 2.16e-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: 41.52  E-value: 2.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181529 459 ITRIATLPALRRRGIARQLIERQRRQAQGLDFLSVSFGYTEPLWRFWQSCGFELVRIGSKPEA 521
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYA 117
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
459-514 1.07e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 39.68  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727181529 459 ITRIATLPALRRRGIARQLIERQRRQAQGLDFLSVSFGYTEPLWRFWQSCGFELVR 514
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAG 125
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
447-514 2.47e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 37.58  E-value: 2.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181529 447 GQWWAPTLRSRRITRIATLPALRRRGIARQLIERQRRQA--QGLD--FLSVsFGYTEPLWRFWQSCGFELVR 514
Cdd:COG3393    6 AGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREAlaRGARtpFLYV-DADNPAARRLYERLGFRPVG 76
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
458-513 2.75e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.63  E-value: 2.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727181529 458 RITRIATLPALRRRGIARQLIERQRRQAQGLDFLSVSFGYTEPLWRFWQSCGFELV 513
Cdd:COG2153   60 KIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPV 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.
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