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Conserved domains on  [gi|1370540715|gb|AVQ18140|]
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N-acetyltransferase [Fusobacterium mortiferum ATCC 9817]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-197 3.72e-06

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: 44.43  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370540715  28 EAFPDYFLTIFGEELLYEFYNQYFLNNNIFVVAEENNKIIGFIlgnnsdiprkkffnenfyrislkmifellklnknlwn 107
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA------------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370540715 108 GIFQRVFFIKEAIIskfrknikseeriiqnkksyrlLSIAVNPKIKGKNIAVEMEKYFCEELLKVGIEEVGLSVKKENIR 187
Cdd:pfam00583  49 SLSIIDDEPPVGEI----------------------EGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                         170
                  ....*....|
gi 1370540715 188 AIKFYEKCEY 197
Cdd:pfam00583 107 AIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-197 3.72e-06

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: 44.43  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370540715  28 EAFPDYFLTIFGEELLYEFYNQYFLNNNIFVVAEENNKIIGFIlgnnsdiprkkffnenfyrislkmifellklnknlwn 107
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA------------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370540715 108 GIFQRVFFIKEAIIskfrknikseeriiqnkksyrlLSIAVNPKIKGKNIAVEMEKYFCEELLKVGIEEVGLSVKKENIR 187
Cdd:pfam00583  49 SLSIIDDEPPVGEI----------------------EGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                         170
                  ....*....|
gi 1370540715 188 AIKFYEKCEY 197
Cdd:pfam00583 107 AIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 133-195 7.95e-06

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 43.11  E-value: 7.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370540715 133 RIIQNKKSYRLLSIAVNPKIKGKNIAVEMEKYFCEELLKVGIEEVGLSVKKENIRAIKFYEKC 195
Cdd:COG0456     6 GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKL 68
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
 137-198 1.71e-03

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 466844 [Multi-domain]  Cd Length: 383  Bit Score: 38.75  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370540715 137 NKKSYRLLSIAVNPKIKGKNIAVEMEKYFCEELLKvgieEVGLSVkKENIRA-IKFYEKCEYL 198
Cdd:cd11738   215 NKGKLKVLATTFDPYLGGRNFDEVLVDYFCEEFKT----KYKLNV-KENIRAlLRLYQECEKL 272
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-197 3.72e-06

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: 44.43  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370540715  28 EAFPDYFLTIFGEELLYEFYNQYFLNNNIFVVAEENNKIIGFIlgnnsdiprkkffnenfyrislkmifellklnknlwn 107
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA------------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370540715 108 GIFQRVFFIKEAIIskfrknikseeriiqnkksyrlLSIAVNPKIKGKNIAVEMEKYFCEELLKVGIEEVGLSVKKENIR 187
Cdd:pfam00583  49 SLSIIDDEPPVGEI----------------------EGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                         170
                  ....*....|
gi 1370540715 188 AIKFYEKCEY 197
Cdd:pfam00583 107 AIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 133-195 7.95e-06

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 43.11  E-value: 7.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370540715 133 RIIQNKKSYRLLSIAVNPKIKGKNIAVEMEKYFCEELLKVGIEEVGLSVKKENIRAIKFYEKC 195
Cdd:COG0456     6 GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKL 68
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
9-78 3.39e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 42.67  E-value: 3.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370540715   9 IIYRKVKKEDLNQIAKIHKEAFPD----YFLTIFGEELLYEFYNQYFLNNNIFVVAEENNKIIGFI-LGNNSDIP 78
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAEgtatFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFAsLGPFRPRP 76
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
11-78 8.71e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 41.22  E-value: 8.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370540715  11 YRKVKKEDLNQIAKIHKEAFPDYFLtifgEELLYEFYNQyfLNNNIFVVAEENNKIIGFILGNNSDIP 78
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGRE----AELVDRLRED--PAAGLSLVAEDDGEIVGHVALSPVDID 62
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
 137-198 1.71e-03

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 466844 [Multi-domain]  Cd Length: 383  Bit Score: 38.75  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370540715 137 NKKSYRLLSIAVNPKIKGKNIAVEMEKYFCEELLKvgieEVGLSVkKENIRA-IKFYEKCEYL 198
Cdd:cd11738   215 NKGKLKVLATTFDPYLGGRNFDEVLVDYFCEEFKT----KYKLNV-KENIRAlLRLYQECEKL 272
ASKHA_NBD_HSP70_HSPA4 cd11737
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ...
 137-198 4.64e-03

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 466843 [Multi-domain]  Cd Length: 381  Bit Score: 37.23  E-value: 4.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370540715 137 NKKSYRLLSIAVNPKIKGKNIAVEMEKYFCEELLKvgieEVGLSVKKEnIRA-IKFYEKCEYL 198
Cdd:cd11737   215 NKGKLKVLATAFDPTLGGRKFDEVLVNHFCEEFGK----KYKLDIKSK-IRAlLRLFQECEKL 272
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-68 5.42e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 35.62  E-value: 5.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370540715  11 YRKVKKEDLNQIAKIHKEAFPDyfltifGEELLYEFYNQYFLNNNIFVVAEENNKIIG 68
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYAFQD------EDSPELREYFRPLLEEGRVLGAFDDGELVS 52
 
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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