NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|10835073|ref|NP_066565|]
View 

glycylpeptide N-tetradecanoyltransferase 1 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
NMT1 super family cl34897
N-myristoyl transferase [Lipid metabolism];
86-484 1.51e-148

N-myristoyl transferase [Lipid metabolism];


The actual alignment was detected with superfamily member COG5092:

Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 432.48  E-value: 1.51e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073  86 AERIQEIQKAIELFSV-----GQGPAKTMEEaskrsYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQ--EPYTLPQGFTW 158
Cdd:COG5092   7 AKKLENLLKLLQLNNDdtskfTQEQKKMGKD-----HKFWSTQPVDRFDEEAMPEGPIDKHTISIEQpkLPDGLLFEFEW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 159 DALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDT 238
Cdd:COG5092  82 CVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRGK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 239 EKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNM 318
Cdd:COG5092 162 RSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 319 TMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIID-----TFVVENANGE 393
Cdd:COG5092 242 TEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYSRRFELYEEFRFEEIVHTFRPVKNVVDkqvtySYVVEEPNGK 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 394 VTDFLSFYTLPSTIMNHPTHKSLKAAYSFY--------------NVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENK 459
Cdd:COG5092 322 ITDFFSFYSLPFTTIENKKYKDIQGGYLYYyagddqfkdfdpkaTKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNS 401
                       410       420
                ....*....|....*....|....*
gi 10835073 460 TFLEKLKFGIGDGNLQYYLYNWKCP 484
Cdd:COG5092 402 LFLADLKFGCGDGFLNYYLYNYKSE 426
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
86-484 1.51e-148

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 432.48  E-value: 1.51e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073  86 AERIQEIQKAIELFSV-----GQGPAKTMEEaskrsYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQ--EPYTLPQGFTW 158
Cdd:COG5092   7 AKKLENLLKLLQLNNDdtskfTQEQKKMGKD-----HKFWSTQPVDRFDEEAMPEGPIDKHTISIEQpkLPDGLLFEFEW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 159 DALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDT 238
Cdd:COG5092  82 CVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRGK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 239 EKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNM 318
Cdd:COG5092 162 RSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 319 TMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIID-----TFVVENANGE 393
Cdd:COG5092 242 TEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYSRRFELYEEFRFEEIVHTFRPVKNVVDkqvtySYVVEEPNGK 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 394 VTDFLSFYTLPSTIMNHPTHKSLKAAYSFY--------------NVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENK 459
Cdd:COG5092 322 ITDFFSFYSLPFTTIENKKYKDIQGGYLYYyagddqfkdfdpkaTKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNS 401
                       410       420
                ....*....|....*....|....*
gi 10835073 460 TFLEKLKFGIGDGNLQYYLYNWKCP 484
Cdd:COG5092 402 LFLADLKFGCGDGFLNYYLYNYKSE 426
NMT_C pfam02799
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains ...
308-494 4.61e-125

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: 362.53  E-value: 4.61e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073   308 EVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVV 387
Cdd:pfam02799   1 EVGFSHLPRNMTMARMIKLYKLPDETKTPGLRPMEEKDVPQVTELLNRYLSRFDLAPVFSEEEVEHWFLPREQVVWSYVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073   388 ENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQT-----PLLDLMSDALVLAKMKGFDVFNALDLMENKTFL 462
Cdd:pfam02799  81 EDPEGKITDFFSFYSLPSTVINNPKHKTLKAAYLFYYAATSTkeakkRLNELMNDALILAKKAGFDVFNALTLMDNKLFL 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 10835073   463 EKLKFGIGDGNLQYYLYNWKCP--SMGAEKVGLV 494
Cdd:pfam02799 161 EDLKFGPGDGQLNYYLYNYRCPpgGIDPSKVGLV 194
 
Name Accession Description Interval E-value
NMT1 COG5092
N-myristoyl transferase [Lipid metabolism];
86-484 1.51e-148

N-myristoyl transferase [Lipid metabolism];


Pssm-ID: 227423 [Multi-domain]  Cd Length: 451  Bit Score: 432.48  E-value: 1.51e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073  86 AERIQEIQKAIELFSV-----GQGPAKTMEEaskrsYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQ--EPYTLPQGFTW 158
Cdd:COG5092   7 AKKLENLLKLLQLNNDdtskfTQEQKKMGKD-----HKFWSTQPVDRFDEEAMPEGPIDKHTISIEQpkLPDGLLFEFEW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 159 DALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDT 238
Cdd:COG5092  82 CVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVKGTQKLVAFISAKPHLVSVRGK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 239 EKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNM 318
Cdd:COG5092 162 RSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTELPSPVSQGRYYHRPLNWKKLYMCGFSGLPDGR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 319 TMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIID-----TFVVENANGE 393
Cdd:COG5092 242 TEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYSRRFELYEEFRFEEIVHTFRPVKNVVDkqvtySYVVEEPNGK 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073 394 VTDFLSFYTLPSTIMNHPTHKSLKAAYSFY--------------NVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENK 459
Cdd:COG5092 322 ITDFFSFYSLPFTTIENKKYKDIQGGYLYYyagddqfkdfdpkaTKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNS 401
                       410       420
                ....*....|....*....|....*
gi 10835073 460 TFLEKLKFGIGDGNLQYYLYNWKCP 484
Cdd:COG5092 402 LFLADLKFGCGDGFLNYYLYNYKSE 426
NMT_C pfam02799
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain; The N and C-terminal domains ...
308-494 4.61e-125

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: 362.53  E-value: 4.61e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073   308 EVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVV 387
Cdd:pfam02799   1 EVGFSHLPRNMTMARMIKLYKLPDETKTPGLRPMEEKDVPQVTELLNRYLSRFDLAPVFSEEEVEHWFLPREQVVWSYVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073   388 ENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQT-----PLLDLMSDALVLAKMKGFDVFNALDLMENKTFL 462
Cdd:pfam02799  81 EDPEGKITDFFSFYSLPSTVINNPKHKTLKAAYLFYYAATSTkeakkRLNELMNDALILAKKAGFDVFNALTLMDNKLFL 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 10835073   463 EKLKFGIGDGNLQYYLYNWKCP--SMGAEKVGLV 494
Cdd:pfam02799 161 EDLKFGPGDGQLNYYLYNYRCPpgGIDPSKVGLV 194
NMT pfam01233
Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain; The N and C-terminal domains ...
137-291 2.57e-112

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: 328.68  E-value: 2.57e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835073   137 PVEPDK--DNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGV 214
Cdd:pfam01233   1 PIDPPKtvEDVRKEPYPLPDGFEWVTLDLNDDKELKEVYELLNENYVEDDDAMFRFNYSKEFLKWALKPPGWKKDWHVGV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10835073   215 RVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPV 291
Cdd:pfam01233  81 RVKSSKKLVAFISGIPVTLRVRDKVVKMVEINFLCVHKKLRSKRLAPVLIKEITRRVNLQGIWQAVYTAGVVLPTPV 157
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH