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Conserved domains on  [gi|594150381|ref|NP_001277298|]
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glycylpeptide N-tetradecanoyltransferase 2 isoform c [Mus musculus]

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];
106-473 2.21e-144

N-myristoyl transferase [Lipid metabolism];


The actual alignment was detected with superfamily member COG5092:

Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 421.31  E-value: 2.21e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 106 YQFWDTQPVPKLNEVITSHGAIEPDKDNIRQ--EPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSP 183
Cdd:COG5092   38 HKFWSTQPVDRFDEEAMPEGPIDKHTISIEQpkLPDGLLFEFEWCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 184 EFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLE 263
Cdd:COG5092  118 EFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 264 GIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKAVRELIN 343
Cdd:COG5092  198 GIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYL 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 344 IYLKQFHLAPVMDDAEVAHWFLPREHIID-----TFVVENPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFY------ 412
Cdd:COG5092  278 EYSRRFELYEEFRFEEIVHTFRPVKNVVDkqvtySYVVEEPNGKITDFFSFYSLPFTTIENKKYKDIQGGYLYYyagddq 357
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150381 413 --------NIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCP 473
Cdd:COG5092  358 fkdfdpkaTKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFGCGDGFLNYYLYNYKSE 426
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
106-473 2.21e-144

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 421.31  E-value: 2.21e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 106 YQFWDTQPVPKLNEVITSHGAIEPDKDNIRQ--EPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSP 183
Cdd:COG5092   38 HKFWSTQPVDRFDEEAMPEGPIDKHTISIEQpkLPDGLLFEFEWCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 184 EFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLE 263
Cdd:COG5092  118 EFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 264 GIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKAVRELIN 343
Cdd:COG5092  198 GIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYL 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 344 IYLKQFHLAPVMDDAEVAHWFLPREHIID-----TFVVENPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFY------ 412
Cdd:COG5092  278 EYSRRFELYEEFRFEEIVHTFRPVKNVVDkqvtySYVVEEPNGKITDFFSFYSLPFTTIENKKYKDIQGGYLYYyagddq 357
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150381 413 --------NIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCP 473
Cdd:COG5092  358 fkdfdpkaTKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFGCGDGFLNYYLYNYKSE 426
NMT_C pfam02799
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains ...
297-483 2.98e-126

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: 365.23  E-value: 2.98e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381  297 EVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKAVRELINIYLKQFHLAPVMDDAEVAHWFLPREHIIDTFVV 376
Cdd:pfam02799   1 EVGFSHLPRNMTMARMIKLYKLPDETKTPGLRPMEEKDVPQVTELLNRYLSRFDLAPVFSEEEVEHWFLPREQVVWSYVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381  377 ENPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTET-----PLLDLMNDALIIAKLKGFDVFNALDLMENKTFL 451
Cdd:pfam02799  81 EDPEGKITDFFSFYSLPSTVINNPKHKTLKAAYLFYYAATSTkeakkRLNELMNDALILAKKAGFDVFNALTLMDNKLFL 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 594150381  452 EKLKFGIGDGNLQYYLYNWRCP--GTDSEKVGLV 483
Cdd:pfam02799 161 EDLKFGPGDGQLNYYLYNYRCPpgGIDPSKVGLV 194
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
106-473 2.21e-144

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 421.31  E-value: 2.21e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 106 YQFWDTQPVPKLNEVITSHGAIEPDKDNIRQ--EPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSP 183
Cdd:COG5092   38 HKFWSTQPVDRFDEEAMPEGPIDKHTISIEQpkLPDGLLFEFEWCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 184 EFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLE 263
Cdd:COG5092  118 EFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 264 GIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKAVRELIN 343
Cdd:COG5092  198 GIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYL 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381 344 IYLKQFHLAPVMDDAEVAHWFLPREHIID-----TFVVENPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFY------ 412
Cdd:COG5092  278 EYSRRFELYEEFRFEEIVHTFRPVKNVVDkqvtySYVVEEPNGKITDFFSFYSLPFTTIENKKYKDIQGGYLYYyagddq 357
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150381 413 --------NIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCP 473
Cdd:COG5092  358 fkdfdpkaTKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFGCGDGFLNYYLYNYKSE 426
NMT_C pfam02799
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains ...
297-483 2.98e-126

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: 365.23  E-value: 2.98e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381  297 EVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKAVRELINIYLKQFHLAPVMDDAEVAHWFLPREHIIDTFVV 376
Cdd:pfam02799   1 EVGFSHLPRNMTMARMIKLYKLPDETKTPGLRPMEEKDVPQVTELLNRYLSRFDLAPVFSEEEVEHWFLPREQVVWSYVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381  377 ENPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTET-----PLLDLMNDALIIAKLKGFDVFNALDLMENKTFL 451
Cdd:pfam02799  81 EDPEGKITDFFSFYSLPSTVINNPKHKTLKAAYLFYYAATSTkeakkRLNELMNDALILAKKAGFDVFNALTLMDNKLFL 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 594150381  452 EKLKFGIGDGNLQYYLYNWRCP--GTDSEKVGLV 483
Cdd:pfam02799 161 EDLKFGPGDGQLNYYLYNYRCPpgGIDPSKVGLV 194
NMT pfam01233
Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains ...
127-281 5.17e-113

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: 330.22  E-value: 5.17e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150381  127 IEPDK--DNIRQEPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVR 204
Cdd:pfam01233   2 IDPPKtvEDVRKEPYPLPDGFEWVTLDLNDDKELKEVYELLNENYVEDDDAMFRFNYSKEFLKWALKPPGWKKDWHVGVR 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150381  205 VSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPVA 281
Cdd:pfam01233  82 VKSSKKLVAFISGIPVTLRVRDKVVKMVEINFLCVHKKLRSKRLAPVLIKEITRRVNLQGIWQAVYTAGVVLPTPVS 158
 
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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