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Conserved domains on  [gi|2794054871|ref|WP_372190946|]
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tRNA(Met) cytidine acetyltransferase TmcA domain-containing protein, partial [Vibrio sp. 10N.222.54.A1]

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
TmcA super family cl34266
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
9-412 5.68e-102

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: 317.54  E-value: 5.68e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871   9 LHTLSNIAQHNDHRYGVVFDGDFDWQNSAVFTFLQDSNTPSIFqVGGTPFEGVIHAPVKKGQQLLGRECQVLVCDFREQF 88
Cdd:COG1444     4 LRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLW-VGERPPLGVEHIPPSAARRLLGREFDHVVFDAHDGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871  89 DANGFSAAlgslvggglllvlppkVNA--------------SEDSE---SFGQRWL-----------KRHF-DKLVS--- 136
Cdd:COG1444    83 DPNALGAL----------------SGTvrgggllvlltpplDEWPQrpdPDSLRLAvppepivtprfIRRLqRKLREhpg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 137 ---VSQHNEAGDVVQATHALPQMQSAQNGLdkFEQQNTAVELVKKVVsgHRKRPLILTADRGRGKSSTLGIAAAQLLVEr 213
Cdd:COG1444   147 vaiWDQDSPLIDPELPAKARFPRPAYEGCL--TADQAAALAALERLA--ERKRVLVLTADRGRGKSAAAGLAAARLAAE- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 214 hGFNIIVTAPSVKAVEPVFSHAGQGLESCEVvNATHIRHQGGSLRFVAPDELLKSKPDCDLLFVDEAATIPIPMLKSMVD 293
Cdd:COG1444   222 -GGRVLVTAPSKAAVEELFEFAGELLEALGV-KYRELTGAGGRVRFVAPDALLERPPDADLLLVDEAAAIPVPLLEKLLA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 294 IYHRMVFSTTVHGYEGSGRGFGIKFESWLSEHRPGWKGFKLEQPIRWNSNDPLEAWLFDCFLLgnDAsvtESAVDEIEGF 373
Cdd:COG1444   300 AFPRVVFTTTVHGYEGTGRGFLLRFCARLDESTPGWRELTLDEPIRWAAGDPLERWLFRALLL--DA---EPAVLQLVDA 374
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2794054871 374 SADAINQLnlgELSKSECLANPEQLQQCFSLLVDAHYQT 412
Cdd:COG1444   375 PPGEVEYE---RLDQDELLADEELLRQLFGLLVLAHYRT 410
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
9-412 5.68e-102

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: 317.54  E-value: 5.68e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871   9 LHTLSNIAQHNDHRYGVVFDGDFDWQNSAVFTFLQDSNTPSIFqVGGTPFEGVIHAPVKKGQQLLGRECQVLVCDFREQF 88
Cdd:COG1444     4 LRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLW-VGERPPLGVEHIPPSAARRLLGREFDHVVFDAHDGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871  89 DANGFSAAlgslvggglllvlppkVNA--------------SEDSE---SFGQRWL-----------KRHF-DKLVS--- 136
Cdd:COG1444    83 DPNALGAL----------------SGTvrgggllvlltpplDEWPQrpdPDSLRLAvppepivtprfIRRLqRKLREhpg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 137 ---VSQHNEAGDVVQATHALPQMQSAQNGLdkFEQQNTAVELVKKVVsgHRKRPLILTADRGRGKSSTLGIAAAQLLVEr 213
Cdd:COG1444   147 vaiWDQDSPLIDPELPAKARFPRPAYEGCL--TADQAAALAALERLA--ERKRVLVLTADRGRGKSAAAGLAAARLAAE- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 214 hGFNIIVTAPSVKAVEPVFSHAGQGLESCEVvNATHIRHQGGSLRFVAPDELLKSKPDCDLLFVDEAATIPIPMLKSMVD 293
Cdd:COG1444   222 -GGRVLVTAPSKAAVEELFEFAGELLEALGV-KYRELTGAGGRVRFVAPDALLERPPDADLLLVDEAAAIPVPLLEKLLA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 294 IYHRMVFSTTVHGYEGSGRGFGIKFESWLSEHRPGWKGFKLEQPIRWNSNDPLEAWLFDCFLLgnDAsvtESAVDEIEGF 373
Cdd:COG1444   300 AFPRVVFTTTVHGYEGTGRGFLLRFCARLDESTPGWRELTLDEPIRWAAGDPLERWLFRALLL--DA---EPAVLQLVDA 374
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2794054871 374 SADAINQLnlgELSKSECLANPEQLQQCFSLLVDAHYQT 412
Cdd:COG1444   375 PPGEVEYE---RLDQDELLADEELLRQLFGLLVLAHYRT 410
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
189-356 1.38e-87

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: 263.24  E-value: 1.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 189 ILTADRGRGKSSTLGIAAAQLlVERHGFNIIVTAPSVKAVEPVFSHAGQGLE---SCEVVNATHIRHQGGSLRFVAPDEL 265
Cdd:pfam05127   1 VITADRGRGKSAALGLAAAAL-IAQGYSRIIVTAPSPANVQTLFEFAIKGLDalgLTPKFRDGIIRGNGQRIRFIAPDEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 266 LKSKPDCDLLFVDEAATIPIPMLKSMVDIYHRMVFSTTVHGYEGSGRGFGIKFESWLSEHRPGWKGFKLEQPIRWNSNDP 345
Cdd:pfam05127  80 LKLPGQADLLVVDEAAAIPLPLLKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQLKKQLPGLRELELTEPIRYAEGDP 159
                         170
                  ....*....|.
gi 2794054871 346 LEAWLFDCFLL 356
Cdd:pfam05127 160 LEKWLNDLLLL 170
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
168-294 2.64e-05

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 44.08  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 168 QQNTAVELVKkvvsghRKRPLILTADRGRGKSSTLgiAAAQLLVERHGFNIIVTAPSVKAVepvfshagQGLESCEVVNA 247
Cdd:cd17933     1 EQKAAVRLVL------RNRVSVLTGGAGTGKTTTL--KALLAALEAEGKRVVLAAPTGKAA--------KRLSESTGIEA 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2794054871 248 T--H--IRHQGGSLRFVAPDELLKskpDCDLLFVDEAatipipmlkSMVDI 294
Cdd:cd17933    65 StiHrlLGINPGGGGFYYNEENPL---DADLLIVDEA---------SMVDT 103
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
9-412 5.68e-102

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: 317.54  E-value: 5.68e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871   9 LHTLSNIAQHNDHRYGVVFDGDFDWQNSAVFTFLQDSNTPSIFqVGGTPFEGVIHAPVKKGQQLLGRECQVLVCDFREQF 88
Cdd:COG1444     4 LRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLW-VGERPPLGVEHIPPSAARRLLGREFDHVVFDAHDGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871  89 DANGFSAAlgslvggglllvlppkVNA--------------SEDSE---SFGQRWL-----------KRHF-DKLVS--- 136
Cdd:COG1444    83 DPNALGAL----------------SGTvrgggllvlltpplDEWPQrpdPDSLRLAvppepivtprfIRRLqRKLREhpg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 137 ---VSQHNEAGDVVQATHALPQMQSAQNGLdkFEQQNTAVELVKKVVsgHRKRPLILTADRGRGKSSTLGIAAAQLLVEr 213
Cdd:COG1444   147 vaiWDQDSPLIDPELPAKARFPRPAYEGCL--TADQAAALAALERLA--ERKRVLVLTADRGRGKSAAAGLAAARLAAE- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 214 hGFNIIVTAPSVKAVEPVFSHAGQGLESCEVvNATHIRHQGGSLRFVAPDELLKSKPDCDLLFVDEAATIPIPMLKSMVD 293
Cdd:COG1444   222 -GGRVLVTAPSKAAVEELFEFAGELLEALGV-KYRELTGAGGRVRFVAPDALLERPPDADLLLVDEAAAIPVPLLEKLLA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 294 IYHRMVFSTTVHGYEGSGRGFGIKFESWLSEHRPGWKGFKLEQPIRWNSNDPLEAWLFDCFLLgnDAsvtESAVDEIEGF 373
Cdd:COG1444   300 AFPRVVFTTTVHGYEGTGRGFLLRFCARLDESTPGWRELTLDEPIRWAAGDPLERWLFRALLL--DA---EPAVLQLVDA 374
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2794054871 374 SADAINQLnlgELSKSECLANPEQLQQCFSLLVDAHYQT 412
Cdd:COG1444   375 PPGEVEYE---RLDQDELLADEELLRQLFGLLVLAHYRT 410
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
189-356 1.38e-87

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: 263.24  E-value: 1.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 189 ILTADRGRGKSSTLGIAAAQLlVERHGFNIIVTAPSVKAVEPVFSHAGQGLE---SCEVVNATHIRHQGGSLRFVAPDEL 265
Cdd:pfam05127   1 VITADRGRGKSAALGLAAAAL-IAQGYSRIIVTAPSPANVQTLFEFAIKGLDalgLTPKFRDGIIRGNGQRIRFIAPDEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 266 LKSKPDCDLLFVDEAATIPIPMLKSMVDIYHRMVFSTTVHGYEGSGRGFGIKFESWLSEHRPGWKGFKLEQPIRWNSNDP 345
Cdd:pfam05127  80 LKLPGQADLLVVDEAAAIPLPLLKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQLKKQLPGLRELELTEPIRYAEGDP 159
                         170
                  ....*....|.
gi 2794054871 346 LEAWLFDCFLL 356
Cdd:pfam05127 160 LEKWLNDLLLL 170
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
168-294 2.64e-05

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 44.08  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 168 QQNTAVELVKkvvsghRKRPLILTADRGRGKSSTLgiAAAQLLVERHGFNIIVTAPSVKAVepvfshagQGLESCEVVNA 247
Cdd:cd17933     1 EQKAAVRLVL------RNRVSVLTGGAGTGKTTTL--KALLAALEAEGKRVVLAAPTGKAA--------KRLSESTGIEA 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2794054871 248 T--H--IRHQGGSLRFVAPDELLKskpDCDLLFVDEAatipipmlkSMVDI 294
Cdd:cd17933    65 StiHrlLGINPGGGGFYYNEENPL---DADLLIVDEA---------SMVDT 103
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
123-294 7.62e-05

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: 44.97  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 123 GQRWLKRHFDKLVSVSQ-----HNEAGDVVQATHALPQMQsAQNGLDKFEQQNTAVELVKKvvsghRKRPLILTADRGRG 197
Cdd:COG0507    79 GRRYLTRLLEAEQRLARrlrrlARPALDEADVEAALAALE-PRAGITLSDEQREAVALALT-----TRRVSVLTGGAGTG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 198 KSSTLGIAAAQLlvERHGFNIIVTAPSVKAVEpVFSHAGqGLESCEVvnatH--IRHQGGSLRFV-APDELLKskpDCDL 274
Cdd:COG0507   153 KTTTLRALLAAL--EALGLRVALAAPTGKAAK-RLSEST-GIEARTI----HrlLGLRPDSGRFRhNRDNPLT---PADL 221
                         170       180
                  ....*....|....*....|
gi 2794054871 275 LFVDEAatipipmlkSMVDI 294
Cdd:COG0507   222 LVVDEA---------SMVDT 232
DEXDc_ComFA cd17925
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ...
168-288 1.23e-03

DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350683 [Multi-domain]  Cd Length: 143  Bit Score: 38.82  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794054871 168 QQNTAVELVKKVvsgHRKRPLILTADRGRGKSSTLGIAAAQLLveRHGFNIIVTAPSVKAVEPVFSHAGQGLESCEVVna 247
Cdd:cd17925     2 QQKASNALVETI---DAKEDLLVWAVTGAGKTEMLFPAIAQAL--RQGGRVAIASPRIDVCLELAPRLKAAFPGAAIV-- 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2794054871 248 thIRHQGGSLRFVAPD-------ELLKSKPDCDLLFVDEAATIPI---PML 288
Cdd:cd17925    75 --LLHGGSEDQYQRSPlviatthQLLRFYRAFDLLIIDEVDAFPYagdPML 123
 
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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