NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|339902462|gb|AEK23541|]
View 

Conserved hypothetical protein [Capnocytophaga canimorsus Cc5]

Protein Classification

acyltransferase family protein( domain architecture ID 229463)

acyltransferase family protein similar to Curvularia lunata acyltransferase clz18, part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS)

EC:  2.3.1.-
Gene Ontology:  GO:0016747

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WecH super family cl42266
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
166-333 2.36e-03

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3274:

Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 39.59  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462 166 LPLANYLTRANGTIFSIFpWFGYVSFgASLGYFFYKYRNTTNLYRNTIILLTVGIAILWFksdiFKYIYLTTDSNLFKEL 245
Cdd:COG3274  172 LPYLNTLLGIDLFFTLTL-FLGYLGY-FLLGYYLARYKARLKKRRLIALLLFLVGLALTF----LGTYLLSLQTGKFNEL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462 246 FHSEFLFLRLKNVLLVFLFF--IVTRNLITSKILRKIGQNTLSIYVIHCILLYgsitgigLIRFFKYSLNPYVTVIGALL 323
Cdd:COG3274  246 FYSYLSPNVVLMSVALFLLLknLSFRSSKLSRLLSRLSKYSFGIYLIHPLVLD-------LLTKLGLNLLNINPLLGIPL 318
                        170
                 ....*....|
gi 339902462 324 FILLNVWLSF 333
Cdd:COG3274  319 VALLTFVLSL 328
Acyl_transf_3 super family cl21495
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
7-205 7.25e-03

Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain is found in a wide range of acyltransferase enzymes, including, mainly, bacterial proteins which catalyze the transfer of acyl groups, other than amino-acyl, from one compound to another, such as Glucans biosynthesis protein C (OPGC) or protein OatA from Listeria monocytogenes serovar 1/2a and Staphylococcus aureus, an integral membrane protein which is responsible for O-acetylation at the C6-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic acid of the peptidoglycan, a modification that determines lysozyme resistance. This domain is also present in eukaryotic proteins, namely O-acyltransferase like protein (OACYL) from mouse and RHY1 (Regulator of hypoxia-inducible factor 1) and NRF6 (Nose resistant to fluoxetine protein 6) from Caenorhabditis elegans.


The actual alignment was detected with superfamily member pfam07786:

Pssm-ID: 473885  Cd Length: 222  Bit Score: 37.58  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462    7 RLYFIDIIRAFAICMMLQGHFVGSLmgEAFYD-DSNILFSVWRYCTGFTAPVFFAVSGFIFMFlmikeSDTKAVGWhnpr 85
Cdd:pfam07786   1 RYWEIDALRGIALILMIIFHFLWDL--EFFGYlDVDLTSGFWVYFARLIASLFLFIAGISLVL-----AHGRGLRW---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462   86 vKKGFHRALLLIGI--------GYLLRLSFEYVDILHCIGISLLLLIGLYLFtynkktyvlPTLLILITLSLFTFEPLYK 157
Cdd:pfam07786  70 -RKFLKRGLKIFAAallitaatYIAFPDSFIYFGILHFIGLASLLGLLFLRL---------PKWLLLLGALLFLALGLFL 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 339902462  158 SFKFDFLPLPLANYLTRAN---GTIFSIFPWFGYVSFGASLGYFFYKYRNT 205
Cdd:pfam07786 140 RSPTFDTPLLLWLGLSPLPfrtLDYFPLFPWFGVVLLGIALGRLLYPRGKR 190
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
166-333 2.36e-03

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 39.59  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462 166 LPLANYLTRANGTIFSIFpWFGYVSFgASLGYFFYKYRNTTNLYRNTIILLTVGIAILWFksdiFKYIYLTTDSNLFKEL 245
Cdd:COG3274  172 LPYLNTLLGIDLFFTLTL-FLGYLGY-FLLGYYLARYKARLKKRRLIALLLFLVGLALTF----LGTYLLSLQTGKFNEL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462 246 FHSEFLFLRLKNVLLVFLFF--IVTRNLITSKILRKIGQNTLSIYVIHCILLYgsitgigLIRFFKYSLNPYVTVIGALL 323
Cdd:COG3274  246 FYSYLSPNVVLMSVALFLLLknLSFRSSKLSRLLSRLSKYSFGIYLIHPLVLD-------LLTKLGLNLLNINPLLGIPL 318
                        170
                 ....*....|
gi 339902462 324 FILLNVWLSF 333
Cdd:COG3274  319 VALLTFVLSL 328
HGSNAT_cat pfam07786
Heparan-alpha-glucosaminide N-acetyltransferase, catalytic; This entry includes the catalytic ...
7-205 7.25e-03

Heparan-alpha-glucosaminide N-acetyltransferase, catalytic; This entry includes the catalytic domain of HGSNAT (Heparan-alpha-glucosaminide N-acetyltransferase). It contains the conserved histidine in the active site (His269), thought to hold the acetyl group during the transfer across the membrane and required for its enzymatic activity. HGSNAT transfers an acetyl group from cytoplasmically derived acetyl-CoA to terminal N-glucosamine residues of heparan sulfate within the lysosomes.


Pssm-ID: 377915  Cd Length: 222  Bit Score: 37.58  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462    7 RLYFIDIIRAFAICMMLQGHFVGSLmgEAFYD-DSNILFSVWRYCTGFTAPVFFAVSGFIFMFlmikeSDTKAVGWhnpr 85
Cdd:pfam07786   1 RYWEIDALRGIALILMIIFHFLWDL--EFFGYlDVDLTSGFWVYFARLIASLFLFIAGISLVL-----AHGRGLRW---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462   86 vKKGFHRALLLIGI--------GYLLRLSFEYVDILHCIGISLLLLIGLYLFtynkktyvlPTLLILITLSLFTFEPLYK 157
Cdd:pfam07786  70 -RKFLKRGLKIFAAallitaatYIAFPDSFIYFGILHFIGLASLLGLLFLRL---------PKWLLLLGALLFLALGLFL 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 339902462  158 SFKFDFLPLPLANYLTRAN---GTIFSIFPWFGYVSFGASLGYFFYKYRNT 205
Cdd:pfam07786 140 RSPTFDTPLLLWLGLSPLPfrtLDYFPLFPWFGVVLLGIALGRLLYPRGKR 190
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
166-333 2.36e-03

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 39.59  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462 166 LPLANYLTRANGTIFSIFpWFGYVSFgASLGYFFYKYRNTTNLYRNTIILLTVGIAILWFksdiFKYIYLTTDSNLFKEL 245
Cdd:COG3274  172 LPYLNTLLGIDLFFTLTL-FLGYLGY-FLLGYYLARYKARLKKRRLIALLLFLVGLALTF----LGTYLLSLQTGKFNEL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462 246 FHSEFLFLRLKNVLLVFLFF--IVTRNLITSKILRKIGQNTLSIYVIHCILLYgsitgigLIRFFKYSLNPYVTVIGALL 323
Cdd:COG3274  246 FYSYLSPNVVLMSVALFLLLknLSFRSSKLSRLLSRLSKYSFGIYLIHPLVLD-------LLTKLGLNLLNINPLLGIPL 318
                        170
                 ....*....|
gi 339902462 324 FILLNVWLSF 333
Cdd:COG3274  319 VALLTFVLSL 328
HGSNAT_cat pfam07786
Heparan-alpha-glucosaminide N-acetyltransferase, catalytic; This entry includes the catalytic ...
7-205 7.25e-03

Heparan-alpha-glucosaminide N-acetyltransferase, catalytic; This entry includes the catalytic domain of HGSNAT (Heparan-alpha-glucosaminide N-acetyltransferase). It contains the conserved histidine in the active site (His269), thought to hold the acetyl group during the transfer across the membrane and required for its enzymatic activity. HGSNAT transfers an acetyl group from cytoplasmically derived acetyl-CoA to terminal N-glucosamine residues of heparan sulfate within the lysosomes.


Pssm-ID: 377915  Cd Length: 222  Bit Score: 37.58  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462    7 RLYFIDIIRAFAICMMLQGHFVGSLmgEAFYD-DSNILFSVWRYCTGFTAPVFFAVSGFIFMFlmikeSDTKAVGWhnpr 85
Cdd:pfam07786   1 RYWEIDALRGIALILMIIFHFLWDL--EFFGYlDVDLTSGFWVYFARLIASLFLFIAGISLVL-----AHGRGLRW---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339902462   86 vKKGFHRALLLIGI--------GYLLRLSFEYVDILHCIGISLLLLIGLYLFtynkktyvlPTLLILITLSLFTFEPLYK 157
Cdd:pfam07786  70 -RKFLKRGLKIFAAallitaatYIAFPDSFIYFGILHFIGLASLLGLLFLRL---------PKWLLLLGALLFLALGLFL 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 339902462  158 SFKFDFLPLPLANYLTRAN---GTIFSIFPWFGYVSFGASLGYFFYKYRNT 205
Cdd:pfam07786 140 RSPTFDTPLLLWLGLSPLPfrtLDYFPLFPWFGVVLLGIALGRLLYPRGKR 190
 
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