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Conserved domains on  [gi|333956796|gb|EGL74432|]
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hypothetical protein CSE899_00440 [Cronobacter sakazakii E899]

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 ...
 2-382 2.44e-171

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: 495.50  E-value: 2.44e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796   2 QKLVRAFPATLLTSTVQGYEGTGRGFLLKFCAGID----GLRYRTLSTPVRWAQDDPLERLVSQALLFEDDDFART---- 73
Cdd:COG1444  295 EKLLAAFPRVVFTTTVHGYEGTGRGFLLRFCARLDestpGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLQlvda 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  74 PAGDVRFYSVSQKDWQTRPERAAALYRLLAGAHYRTSPLDLRRMMDAPGQSFIAAEAGGETVGALWLVTEGGLDAALSQA 153
Cdd:COG1444  375 PPGEVEYERLDQDELLADEELLRQLFGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEA 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 154 VWAGYRRPRGNLVAQSLSAHGGDPLAATLGGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVSFGYTPALWR 232
Cdd:COG1444  455 VWAGRRRPRGNLVPQSLAAHLGLPEAATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAKEeGLDWLGVSFGATPELLR 534

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 233 FWQRCGFTLLRFGSHREASSGCYNAMALVALSAAGARLVREEHQRLARDAT--------LLQRWVDETLP--LTPAPQAT 302
Cdd:COG1444  535 FWQRNGFVPVHLGTTRNASSGEYSAMVLKPLSEAGEALVDRAARRFARDLPnllsdplrDLDPDVARALLraLPADADPE 614

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 303 LNSDDWLALAGFAFAHRPLETSLGPLYRLLEA---------SPQTLQALRGRLALQMPVDVLCRKLGLSGRKALLAALRQ 373
Cdd:COG1444  615 LSDEDWRELAGFAFGHRPYEASLDALRRLLLAylldpradlSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRD 694


                 ....*....
gi 333956796 374 ETALALDAL 382
Cdd:COG1444  695 AVAQLLDAY 703
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-382 2.44e-171

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: 495.50  E-value: 2.44e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796   2 QKLVRAFPATLLTSTVQGYEGTGRGFLLKFCAGID----GLRYRTLSTPVRWAQDDPLERLVSQALLFEDDDFART---- 73
Cdd:COG1444  295 EKLLAAFPRVVFTTTVHGYEGTGRGFLLRFCARLDestpGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLQlvda 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  74 PAGDVRFYSVSQKDWQTRPERAAALYRLLAGAHYRTSPLDLRRMMDAPGQSFIAAEAGGETVGALWLVTEGGLDAALSQA 153
Cdd:COG1444  375 PPGEVEYERLDQDELLADEELLRQLFGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEA 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 154 VWAGYRRPRGNLVAQSLSAHGGDPLAATLGGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVSFGYTPALWR 232
Cdd:COG1444  455 VWAGRRRPRGNLVPQSLAAHLGLPEAATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAKEeGLDWLGVSFGATPELLR 534

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 233 FWQRCGFTLLRFGSHREASSGCYNAMALVALSAAGARLVREEHQRLARDAT--------LLQRWVDETLP--LTPAPQAT 302
Cdd:COG1444  535 FWQRNGFVPVHLGTTRNASSGEYSAMVLKPLSEAGEALVDRAARRFARDLPnllsdplrDLDPDVARALLraLPADADPE 614

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 303 LNSDDWLALAGFAFAHRPLETSLGPLYRLLEA---------SPQTLQALRGRLALQMPVDVLCRKLGLSGRKALLAALRQ 373
Cdd:COG1444  615 LSDEDWRELAGFAFGHRPYEASLDALRRLLLAylldpradlSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRD 694


                 ....*....
gi 333956796 374 ETALALDAL 382
Cdd:COG1444  695 AVAQLLDAY 703
tRNA_bind_3 pfam17176
tRNA-binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
 267-385 1.44e-38

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: 134.76  E-value: 1.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  267 GARLVREEHQRLARDATLLQRWVDETLPLTPAPQATLNSDDWLALAGFAFAHRPLETSLGPLYRLLEASPQTLQALRGRL 346
Cdd:pfam17176   1 GEALAQQAHQRLARDWRWLRQWIGLALPLPPPADQTLNDEDWRELAGFAFAHRPLEASLGALQRLLLRSSLPLPALRARL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 333956796  347 ALQMPVDVLCRKLGLSGRKALLAALRQETALALDALDAP 385
Cdd:pfam17176  81 QQQQSDAEIAALLGLSGRKALLARWREEAAQALAALDAA 119
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 183-223 7.56e-04

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: 37.64  E-value: 7.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 333956796 183 GGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVS 223
Cdd:cd04301   24 DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARErGAKRLRLE 65
PRK07757 PRK07757
N-acetyltransferase;
190-239 1.35e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.02  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 333956796 190 VAVHPGRQREGIGRQLIEQARAQAPEgcdyLSV----SFGYTPalwRFWQRCGF 239
Cdd:PRK07757  71 LAVSEDYRGQGIGRMLVEACLEEARE----LGVkrvfALTYQP---EFFEKLGF 117
 
Name Accession Description Interval E-value
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-382 2.44e-171

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: 495.50  E-value: 2.44e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796   2 QKLVRAFPATLLTSTVQGYEGTGRGFLLKFCAGID----GLRYRTLSTPVRWAQDDPLERLVSQALLFEDDDFART---- 73
Cdd:COG1444  295 EKLLAAFPRVVFTTTVHGYEGTGRGFLLRFCARLDestpGWRELTLDEPIRWAAGDPLERWLFRALLLDAEPAVLQlvda 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  74 PAGDVRFYSVSQKDWQTRPERAAALYRLLAGAHYRTSPLDLRRMMDAPGQSFIAAEAGGETVGALWLVTEGGLDAALSQA 153
Cdd:COG1444  375 PPGEVEYERLDQDELLADEELLRQLFGLLVLAHYRTSPDDLRRLLDAPNQHFRALRTGGKVVGVAWLAEEGGLDAELAEA 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 154 VWAGYRRPRGNLVAQSLSAHGGDPLAATLGGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVSFGYTPALWR 232
Cdd:COG1444  455 VWAGRRRPRGNLVPQSLAAHLGLPEAATLRGWRIVRIAVHPALQRRGLGSRLLAEIREEAKEeGLDWLGVSFGATPELLR 534

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 233 FWQRCGFTLLRFGSHREASSGCYNAMALVALSAAGARLVREEHQRLARDAT--------LLQRWVDETLP--LTPAPQAT 302
Cdd:COG1444  535 FWQRNGFVPVHLGTTRNASSGEYSAMVLKPLSEAGEALVDRAARRFARDLPnllsdplrDLDPDVARALLraLPADADPE 614

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 303 LNSDDWLALAGFAFAHRPLETSLGPLYRLLEA---------SPQTLQALRGRLALQMPVDVLCRKLGLSGRKALLAALRQ 373
Cdd:COG1444  615 LSDEDWRELAGFAFGHRPYEASLDALRRLLLAylldpradlSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRD 694


                 ....*....
gi 333956796 374 ETALALDAL 382
Cdd:COG1444  695 AVAQLLDAY 703
tRNA_bind_3 pfam17176
tRNA-binding domain; This domain, found at the C-terminus of tRNA(Met) cytidine ...
 267-385 1.44e-38

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: 134.76  E-value: 1.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  267 GARLVREEHQRLARDATLLQRWVDETLPLTPAPQATLNSDDWLALAGFAFAHRPLETSLGPLYRLLEASPQTLQALRGRL 346
Cdd:pfam17176   1 GEALAQQAHQRLARDWRWLRQWIGLALPLPPPADQTLNDEDWRELAGFAFAHRPLEASLGALQRLLLRSSLPLPALRARL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 333956796  347 ALQMPVDVLCRKLGLSGRKALLAALRQETALALDALDAP 385
Cdd:pfam17176  81 QQQQSDAEIAALLGLSGRKALLARWREEAAQALAALDAA 119
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
 1-66 1.15e-21

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: 91.05  E-value: 1.15e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796    1 MQKLVRAFPATLLTSTVQGYEGTGRGFLLKFCAGID----GLRYRTLSTPVRWAQDDPLERLVSQALLFE 66
Cdd:pfam05127 102 LKQLLRGFPRVVFATTVHGYEGTGRGFSLKFLAQLKkqlpGLRELELTEPIRYAEGDPLEKWLNDLLLLD 171
GNAT_acetyltr_2 pfam13718
GNAT acetyltransferase 2; This domain has N-acetyltransferase activity. It has a GCN5-related ...
 101-240 3.39e-16

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: 77.26  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  101 LLAGAHYRTSPLDLRRMMDAPG-QSFIAAEAGGETVGAL-------WLVTEGGLDAALSQAVWAGYRRPRGNLVAQSLSA 172
Cdd:pfam13718   5 LYVASHYKNSPNDLQLLSDAPAhHLFVLLGPVDESGNALpdilcvvQVALEGRISRESVKNSLSRGKRASGDLIPWTVSQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  173 HGGDPLAATLGGLRVSRVAVHPGRQREGIGRQLIEQARA----------------------------------------- 211
Cdd:pfam13718  85 QFQDEDFASLSGARIVRIATHPEYQGMGYGSRALELLIQyyegkitdlseaeeleeeeadriedeesavslleekirprk 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 333956796  212 -----------QAPEGCDYLSVSFGYTPALWRFWQRCGFT 240
Cdd:pfam13718 165 elpplllklseRPPERLDYLGVSFGLTPDLLKFWKRAGFV 204
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 183-240 3.46e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.73  E-value: 3.46e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333956796 183 GGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCD--YLSVSFGYTPALwRFWQRCGFT 240
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARErGARrlRLEVREDNEAAI-ALYEKLGFE 71
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
91-240 4.75e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  91 RPERAAALYRLLA---GAHYRTSPLDLRRMMDAPGQSFIAaEAGGETVGALWLvteggldaalsqavwagyrrprgnlva 167
Cdd:COG3153    5 TPEDAEAIAALLRaafGPGREAELVDRLREDPAAGLSLVA-EDDGEIVGHVAL--------------------------- 56

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333956796 168 qSLSAHGGDPLAATLGglrvsRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVSFgyTPALWRFWQRCGFT 240
Cdd:COG3153   57 -SPVDIDGEGPALLLG-----PLAVDPEYRGQGIGRALMRAALEAARErGARAVVLLG--DPSLLPFYERFGFR 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 189-240 1.32e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 45.91  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333956796  189 RVAVHPGRQREGIGRQLIEQARAQAPEGCDYLSVSFGYTPALwRFWQRCGFT 240
Cdd:pfam13508  33 RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAA-AFYEKLGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 183-243 1.83e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 44.27  E-value: 1.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333956796 183 GGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCD--YLSVSFGYTPALwRFWQRCGFTLLR 243
Cdd:COG0454   57 KVLELKRLYVLPEYRGKGIGKALLEALLEWARErGCTalELDTLDGNPAAI-RFYERLGFKEIE 119
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 187-239 6.64e-05

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: 42.12  E-value: 6.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333956796  187 VSRVAVHPGRQREGIGRQLIEQARAQAPE-GCD--YLSVSFGYTPAlWRFWQRCGF 239
Cdd:pfam00583  62 IEGLAVAPEYRGKGIGTALLQALLEWARErGCEriFLEVAADNLAA-IALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 177-261 2.62e-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: 40.75  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796 177 PLAATLGGLRvsRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVsfGYTPALWRFWQRCGFTLLRFGSHREASSGCY 255
Cdd:COG1246   47 PLDEDLAELR--SLAVHPDYRGRGIGRRLLEALLAEARElGLKRLFL--LTTSAAIHFYEKLGFEEIDKEDLPYAKVWQR 122


                 ....*.
gi 333956796 256 NAMALV 261
Cdd:COG1246  123 DSVVME 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 183-223 7.56e-04

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: 37.64  E-value: 7.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 333956796 183 GGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCDYLSVS 223
Cdd:cd04301   24 DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARErGAKRLRLE 65
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
96-240 1.24e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 39.21  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956796  96 AALYR---LLAGAHYRTSPLDLRRM------MDAPGQSFIAAEAGGETVGALWLVTEGGLDAALSQAVWAgyrrprgnlv 166
Cdd:COG1247   16 AAIYNeaiAEGTATFETEPPSEEEReawfaaILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEES---------- 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333956796 167 aqslsahggdplaatlgglrvsrVAVHPGRQREGIGRQLIEQARAQAPE-GCD--YLSVSFGYTPALwRFWQRCGFT 240
Cdd:COG1247   86 -----------------------IYVDPDARGRGIGRALLEALIERARArGYRrlVAVVLADNEASI-ALYEKLGFE 138
PRK07757 PRK07757
N-acetyltransferase;
190-239 1.35e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.02  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 333956796 190 VAVHPGRQREGIGRQLIEQARAQAPEgcdyLSV----SFGYTPalwRFWQRCGF 239
Cdd:PRK07757  71 LAVSEDYRGQGIGRMLVEACLEEARE----LGVkrvfALTYQP---EFFEKLGF 117
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
178-240 2.03e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.24  E-value: 2.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333956796 178 LAATLGGLRVSRVAVHPGRQREGIGRQLIEQARAQAPE-GCD--YLSVSfgyTPALwRFWQRCGFT 240
Cdd:COG2153   52 LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARErGARriVLSAQ---AHAV-GFYEKLGFV 113
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
179-243 6.41e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 35.65  E-value: 6.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333956796 179 AATLGGLRVSRVAVHPGRQREGIGRQLIEQARAQA-PEGCD--YLSVSFGYTPALwRFWQRCGFTLLR 243
Cdd:COG3393   10 AESPGVAEISGVYTHPEYRGRGLASALVAALAREAlARGARtpFLYVDADNPAAR-RLYERLGFRPVG 76
 
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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