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Conserved domains on  [gi|749156737|ref|XP_011129997|]
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glycylpeptide N-tetradecanoyltransferase [Gregarina niphandrodes]

Protein Classification

glycylpeptide N-tetradecanoyltransferase( domain architecture ID 1003034)

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

EC:  2.3.1.97
Gene Ontology:  GO:0004379|GO:0018008
PubMed:  10718634

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NMT1 super family cl34897
N-myristoyl transferase [Lipid metabolism];
19-413 1.36e-109

N-myristoyl transferase [Lipid metabolism];


The actual alignment was detected with superfamily member COG5092:

Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 330.02  E-value: 1.36e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  19 PEEVGKPHRFWDSQPVPSVSEALPEDCGVIETKSIDEVRKTPVPLPDTFEWVEL---GEEDLQEIYELLSKHYVEDNASC 95
Cdd:COG5092   31 QKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPKLPDGLLFEFEWCVIdvaNKKQLEDVFVLLEENYVEDIYAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  96 FRFEYTMESLKWAIFPPDSKRSWTIGIKTmvktpaldtkataigerKAQRKLVAFISGIPVKINIFGNRIAGGEVNFLCV 175
Cdd:COG5092  111 HRFRYSVEFLQWALDGPGGKKRWHIGVRV-----------------KGTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 176 HKKLRSRRLAPILIKELTRRINLDGVWHALYTAGIFIPRPVTDCRYYHRSMNVAKLVSIGFSALRAGESIEEAKKKAQLP 255
Cdd:COG5092  174 HKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALP 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 256 DHFTVPGIRPMEEKDVASVTQLLNNgfVKDKIKLYTELNEDDVCHWL-----LTKQGAVYTY-VKETEGKVTDFFSFYEL 329
Cdd:COG5092  254 AKTKTEGLRLAEEKDMEDVARLYLE--YSRRFELYEEFRFEEIVHTFrpvknVVDKQVTYSYvVEEPNGKITDFFSFYSL 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 330 NSKVLRfNQEYDLLKAAYNYYCNGTTMSR--------------KQLLEQSIIAANILKYDVFNALDLNHNFECFQELQFG 395
Cdd:COG5092  332 PFTTIE-NKKYKDIQGGYLYYYAGDDQFKdfdpkatkalktrvAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFG 410
                        410
                 ....*....|....*...
gi 749156737 396 PGDGSLKYYLYNYKCPLI 413
Cdd:COG5092  411 CGDGFLNYYLYNYKSEEI 428
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
19-413 1.36e-109

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 330.02  E-value: 1.36e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  19 PEEVGKPHRFWDSQPVPSVSEALPEDCGVIETKSIDEVRKTPVPLPDTFEWVEL---GEEDLQEIYELLSKHYVEDNASC 95
Cdd:COG5092   31 QKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPKLPDGLLFEFEWCVIdvaNKKQLEDVFVLLEENYVEDIYAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  96 FRFEYTMESLKWAIFPPDSKRSWTIGIKTmvktpaldtkataigerKAQRKLVAFISGIPVKINIFGNRIAGGEVNFLCV 175
Cdd:COG5092  111 HRFRYSVEFLQWALDGPGGKKRWHIGVRV-----------------KGTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 176 HKKLRSRRLAPILIKELTRRINLDGVWHALYTAGIFIPRPVTDCRYYHRSMNVAKLVSIGFSALRAGESIEEAKKKAQLP 255
Cdd:COG5092  174 HKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALP 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 256 DHFTVPGIRPMEEKDVASVTQLLNNgfVKDKIKLYTELNEDDVCHWL-----LTKQGAVYTY-VKETEGKVTDFFSFYEL 329
Cdd:COG5092  254 AKTKTEGLRLAEEKDMEDVARLYLE--YSRRFELYEEFRFEEIVHTFrpvknVVDKQVTYSYvVEEPNGKITDFFSFYSL 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 330 NSKVLRfNQEYDLLKAAYNYYCNGTTMSR--------------KQLLEQSIIAANILKYDVFNALDLNHNFECFQELQFG 395
Cdd:COG5092  332 PFTTIE-NKKYKDIQGGYLYYYAGDDQFKdfdpkatkalktrvAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFG 410
                        410
                 ....*....|....*...
gi 749156737 396 PGDGSLKYYLYNYKCPLI 413
Cdd:COG5092  411 CGDGFLNYYLYNYKSEEI 428
NMT pfam01233
Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains ...
49-217 3.99e-75

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: 231.23  E-value: 3.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737   49 ETKSIDEVRKTPVPLPDTFEWVEL---GEEDLQEIYELLSKHYVEDNASCFRFEYTMESLKWAIFPPDSKRSWTIGIKtm 125
Cdd:pfam01233   4 PPKTVEDVRKEPYPLPDGFEWVTLdlnDDKELKEVYELLNENYVEDDDAMFRFNYSKEFLKWALKPPGWKKDWHVGVR-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  126 vktpaldtkataigeRKAQRKLVAFISGIPVKINIFGNRIAGGEVNFLCVHKKLRSRRLAPILIKELTRRINLDGVWHAL 205
Cdd:pfam01233  82 ---------------VKSSKKLVAFISGIPVTLRVRDKVVKMVEINFLCVHKKLRSKRLAPVLIKEITRRVNLQGIWQAV 146
                         170
                  ....*....|..
gi 749156737  206 YTAGIFIPRPVT 217
Cdd:pfam01233 147 YTAGVVLPTPVS 158
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
19-413 1.36e-109

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 330.02  E-value: 1.36e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  19 PEEVGKPHRFWDSQPVPSVSEALPEDCGVIETKSIDEVRKTPVPLPDTFEWVEL---GEEDLQEIYELLSKHYVEDNASC 95
Cdd:COG5092   31 QKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPKLPDGLLFEFEWCVIdvaNKKQLEDVFVLLEENYVEDIYAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  96 FRFEYTMESLKWAIFPPDSKRSWTIGIKTmvktpaldtkataigerKAQRKLVAFISGIPVKINIFGNRIAGGEVNFLCV 175
Cdd:COG5092  111 HRFRYSVEFLQWALDGPGGKKRWHIGVRV-----------------KGTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 176 HKKLRSRRLAPILIKELTRRINLDGVWHALYTAGIFIPRPVTDCRYYHRSMNVAKLVSIGFSALRAGESIEEAKKKAQLP 255
Cdd:COG5092  174 HKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALP 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 256 DHFTVPGIRPMEEKDVASVTQLLNNgfVKDKIKLYTELNEDDVCHWL-----LTKQGAVYTY-VKETEGKVTDFFSFYEL 329
Cdd:COG5092  254 AKTKTEGLRLAEEKDMEDVARLYLE--YSRRFELYEEFRFEEIVHTFrpvknVVDKQVTYSYvVEEPNGKITDFFSFYSL 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737 330 NSKVLRfNQEYDLLKAAYNYYCNGTTMSR--------------KQLLEQSIIAANILKYDVFNALDLNHNFECFQELQFG 395
Cdd:COG5092  332 PFTTIE-NKKYKDIQGGYLYYYAGDDQFKdfdpkatkalktrvAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFG 410
                        410
                 ....*....|....*...
gi 749156737 396 PGDGSLKYYLYNYKCPLI 413
Cdd:COG5092  411 CGDGFLNYYLYNYKSEEI 428
NMT pfam01233
Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains ...
49-217 3.99e-75

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: 231.23  E-value: 3.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737   49 ETKSIDEVRKTPVPLPDTFEWVEL---GEEDLQEIYELLSKHYVEDNASCFRFEYTMESLKWAIFPPDSKRSWTIGIKtm 125
Cdd:pfam01233   4 PPKTVEDVRKEPYPLPDGFEWVTLdlnDDKELKEVYELLNENYVEDDDAMFRFNYSKEFLKWALKPPGWKKDWHVGVR-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  126 vktpaldtkataigeRKAQRKLVAFISGIPVKINIFGNRIAGGEVNFLCVHKKLRSRRLAPILIKELTRRINLDGVWHAL 205
Cdd:pfam01233  82 ---------------VKSSKKLVAFISGIPVTLRVRDKVVKMVEINFLCVHKKLRSKRLAPVLIKEITRRVNLQGIWQAV 146
                         170
                  ....*....|..
gi 749156737  206 YTAGIFIPRPVT 217
Cdd:pfam01233 147 YTAGVVLPTPVS 158
NMT_C pfam02799
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains ...
234-421 7.59e-65

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: 206.14  E-value: 7.59e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  234 IGFSALRAGESIEEAKKKAQLPDHFTVPGIRPMEEKDVASVTQLLNNgFVKdKIKLYTELNEDDVCHWLLTKQGAVYTYV 313
Cdd:pfam02799   2 VGFSHLPRNMTMARMIKLYKLPDETKTPGLRPMEEKDVPQVTELLNR-YLS-RFDLAPVFSEEEVEHWFLPREQVVWSYV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749156737  314 KE-TEGKVTDFFSFYELNSKVLRfNQEYDLLKAAYNYYCNGTTMSR-----KQLLEQSIIAANILKYDVFNALDLNHNFE 387
Cdd:pfam02799  80 VEdPEGKITDFFSFYSLPSTVIN-NPKHKTLKAAYLFYYAATSTKEakkrlNELMNDALILAKKAGFDVFNALTLMDNKL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 749156737  388 CFQELQFGPGDGSLKYYLYNYKCP--LINPNENGVI 421
Cdd:pfam02799 159 FLEDLKFGPGDGQLNYYLYNYRCPpgGIDPSKVGLV 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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