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Conserved domains on  [gi|128399|sp|P14743|]
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RecName: Full=Glycylpeptide N-tetradecanoyltransferase; AltName: Full=Cell division control protein 72; AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase; Short=NMT; AltName: Full=Peptide N-myristoyltransferase

Protein Classification

glycylpeptide N-tetradecanoyltransferase( domain architecture ID 11473800)

glycylpeptide N-tetradecanoyltransferase (NMT) adds a myristoyl group (tetradecanoyl group) to the N-terminal glycine residue of certain cellular proteins

EC:  2.3.1.97
Gene Ontology:  GO:0004379|GO:0018008

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
1-455 0e+00

N-myristoyl transferase [Lipid metabolism];


:

Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 759.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399     1 MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKAMKDHKFWRTQPVKDFDEKVVEEGPIDKPKTPEDISDKPLPLLSSFE 80
Cdd:COG5092   1 MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPKLPDGLLFEFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399    81 WCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRG 160
Cdd:COG5092  81 WCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   161 KQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVSTCRYTHRPLNWKKLYEVDFTGLPDG 240
Cdd:COG5092 161 KRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   241 HTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEESLPlDKQVIFSYVVEQPD 320
Cdd:COG5092 241 RTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYSRRFELYEEFRFEEIVHTFRPVKNVV-DKQVTYSYVVEEPN 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   321 GKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATDAdfQFKDrFDPKATKALKTRLCELIYDACILAKNANMDVFNALT 400
Cdd:COG5092 320 GKITDFFSFYSLPFTTIENKKYKDIQGGYLYYYAGDD--QFKD-FDPKATKALKTRVAEMVGDAMILAKVEGCDVFNALT 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 128399   401 SQDNTLFLDDLKFGPGDGFLNFYLFNYRAKPITGGLNPDNSNDIKRRSNVGVVML 455
Cdd:COG5092 397 MMDNSLFLADLKFGCGDGFLNYYLYNYKSEEIPGGLNPDNSNDIKRRSKVGFVMP 451
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
1-455 0e+00

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 759.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399     1 MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKAMKDHKFWRTQPVKDFDEKVVEEGPIDKPKTPEDISDKPLPLLSSFE 80
Cdd:COG5092   1 MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPKLPDGLLFEFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399    81 WCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRG 160
Cdd:COG5092  81 WCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   161 KQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVSTCRYTHRPLNWKKLYEVDFTGLPDG 240
Cdd:COG5092 161 KRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   241 HTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEESLPlDKQVIFSYVVEQPD 320
Cdd:COG5092 241 RTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYSRRFELYEEFRFEEIVHTFRPVKNVV-DKQVTYSYVVEEPN 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   321 GKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATDAdfQFKDrFDPKATKALKTRLCELIYDACILAKNANMDVFNALT 400
Cdd:COG5092 320 GKITDFFSFYSLPFTTIENKKYKDIQGGYLYYYAGDD--QFKD-FDPKATKALKTRVAEMVGDAMILAKVEGCDVFNALT 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 128399   401 SQDNTLFLDDLKFGPGDGFLNFYLFNYRAKPITGGLNPDNSNDIKRRSNVGVVML 455
Cdd:COG5092 397 MMDNSLFLADLKFGCGDGFLNYYLYNYKSEEIPGGLNPDNSNDIKRRSKVGFVMP 451
NMT pfam01233
Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains ...
58-215 1.85e-109

Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.


Pssm-ID: 460124  Cd Length: 158  Bit Score: 319.82  E-value: 1.85e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399      58 PIDKPKTPEDISDKPLPLLSSFEWCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGV 137
Cdd:pfam01233   1 PIDPPKTVEDVRKEPYPLPDGFEWVTLDLNDDKELKEVYELLNENYVEDDDAMFRFNYSKEFLKWALKPPGWKKDWHVGV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 128399     138 RVKETQKLVAFISAIPVTLGVRGKQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVS 215
Cdd:pfam01233  81 RVKSSKKLVAFISGIPVTLRVRDKVVKMVEINFLCVHKKLRSKRLAPVLIKEITRRVNLQGIWQAVYTAGVVLPTPVS 158
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
1-455 0e+00

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 759.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399     1 MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKAMKDHKFWRTQPVKDFDEKVVEEGPIDKPKTPEDISDKPLPLLSSFE 80
Cdd:COG5092   1 MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPKLPDGLLFEFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399    81 WCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRG 160
Cdd:COG5092  81 WCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   161 KQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVSTCRYTHRPLNWKKLYEVDFTGLPDG 240
Cdd:COG5092 161 KRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   241 HTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEESLPlDKQVIFSYVVEQPD 320
Cdd:COG5092 241 RTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYSRRFELYEEFRFEEIVHTFRPVKNVV-DKQVTYSYVVEEPN 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399   321 GKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATDAdfQFKDrFDPKATKALKTRLCELIYDACILAKNANMDVFNALT 400
Cdd:COG5092 320 GKITDFFSFYSLPFTTIENKKYKDIQGGYLYYYAGDD--QFKD-FDPKATKALKTRVAEMVGDAMILAKVEGCDVFNALT 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 128399   401 SQDNTLFLDDLKFGPGDGFLNFYLFNYRAKPITGGLNPDNSNDIKRRSNVGVVML 455
Cdd:COG5092 397 MMDNSLFLADLKFGCGDGFLNYYLYNYKSEEIPGGLNPDNSNDIKRRSKVGFVMP 451
NMT pfam01233
Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains ...
58-215 1.85e-109

Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.


Pssm-ID: 460124  Cd Length: 158  Bit Score: 319.82  E-value: 1.85e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399      58 PIDKPKTPEDISDKPLPLLSSFEWCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGV 137
Cdd:pfam01233   1 PIDPPKTVEDVRKEPYPLPDGFEWVTLDLNDDKELKEVYELLNENYVEDDDAMFRFNYSKEFLKWALKPPGWKKDWHVGV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 128399     138 RVKETQKLVAFISAIPVTLGVRGKQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVS 215
Cdd:pfam01233  81 RVKSSKKLVAFISGIPVTLRVRDKVVKMVEINFLCVHKKLRSKRLAPVLIKEITRRVNLQGIWQAVYTAGVVLPTPVS 158
NMT_C pfam02799
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains ...
231-453 5.47e-105

Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.


Pssm-ID: 460699  Cd Length: 194  Bit Score: 309.76  E-value: 5.47e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399     231 EVDFTGLPDGHTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEEslpldkQV 310
Cdd:pfam02799   1 EVGFSHLPRNMTMARMIKLYKLPDETKTPGLRPMEEKDVPQVTELLNRYLSRFDLAPVFSEEEVEHWFLPRE------QV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128399     311 IFSYVVEQPDGKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATdadfqfkdrfdpKATKALKTRLCELIYDACILAKN 390
Cdd:pfam02799  75 VWSYVVEDPEGKITDFFSFYSLPSTVINNPKHKTLKAAYLFYYAA------------TSTKEAKKRLNELMNDALILAKK 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 128399     391 ANMDVFNALTSQDNTLFLDDLKFGPGDGFLNFYLFNYRAKPitGGLNPDnsndikrrsNVGVV 453
Cdd:pfam02799 143 AGFDVFNALTLMDNKLFLEDLKFGPGDGQLNYYLYNYRCPP--GGIDPS---------KVGLV 194
 
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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