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Conserved domains on  [gi|1907152318|ref|XP_036019250|]
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UPF0462 protein C4orf33 homolog isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOMON_like super family cl14783
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ...
 49-171 3.12e-07

Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


The actual alignment was detected with superfamily member cd09620:

Pssm-ID: 472705  Cd Length: 200  Bit Score: 48.53  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152318  49 PGKPFSELWNYEVVEAFF-LNDTTKQYLEVELCPHGQHLVLLL-----AGRRNVWKKE----------LPLSFKASRGGT 112
Cdd:cd09620    58 YTERDDPVWEDDVVEVFIdPDGDGPNYYEFEVNPLGTVLDAFIrrprdGGGDRDNRQPdsaglesavsIDGTLNDSDGDK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152318 113 NWEGEAYIPWSYF---------PPNVTKFNSFAIHGSND-RRVYEALYPVpqhelqQGQKPDFHRLEYF 171
Cdd:cd09620   138 GWTVELAIPFAALakaaggpplPGDVWRANFYRCGDPTEtPPHYLSWSPT------GVPDPHFHEPFGF 200
 
Name Accession Description Interval E-value
CBM9_like_3 cd09620
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ...
 49-171 3.12e-07

DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.


Pssm-ID: 187678  Cd Length: 200  Bit Score: 48.53  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152318  49 PGKPFSELWNYEVVEAFF-LNDTTKQYLEVELCPHGQHLVLLL-----AGRRNVWKKE----------LPLSFKASRGGT 112
Cdd:cd09620    58 YTERDDPVWEDDVVEVFIdPDGDGPNYYEFEVNPLGTVLDAFIrrprdGGGDRDNRQPdsaglesavsIDGTLNDSDGDK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152318 113 NWEGEAYIPWSYF---------PPNVTKFNSFAIHGSND-RRVYEALYPVpqhelqQGQKPDFHRLEYF 171
Cdd:cd09620   138 GWTVELAIPFAALakaaggpplPGDVWRANFYRCGDPTEtPPHYLSWSPT------GVPDPHFHEPFGF 200
 
Name Accession Description Interval E-value
CBM9_like_3 cd09620
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ...
 49-171 3.12e-07

DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.


Pssm-ID: 187678  Cd Length: 200  Bit Score: 48.53  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152318  49 PGKPFSELWNYEVVEAFF-LNDTTKQYLEVELCPHGQHLVLLL-----AGRRNVWKKE----------LPLSFKASRGGT 112
Cdd:cd09620    58 YTERDDPVWEDDVVEVFIdPDGDGPNYYEFEVNPLGTVLDAFIrrprdGGGDRDNRQPdsaglesavsIDGTLNDSDGDK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152318 113 NWEGEAYIPWSYF---------PPNVTKFNSFAIHGSND-RRVYEALYPVpqhelqQGQKPDFHRLEYF 171
Cdd:cd09620   138 GWTVELAIPFAALakaaggpplPGDVWRANFYRCGDPTEtPPHYLSWSPT------GVPDPHFHEPFGF 200
DOMON_murB_like cd09627
Domon-like domain of UDP-N-acetylenolpyruvoylglucosamine reductase; ...
 35-171 2.76e-04

Domon-like domain of UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylenolpyruvoylglucosamine reductase (murB) catalyzes an essential step in peptidoglycan biosynthesis, the reduction of UDP-N-acetylglucosamine-enolpyruvate to UDP-N-acetylmuramate. A subset of these FAD-dependent enzymes contains a C-terminal DOMON-like domain. DOMON domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes; initially DOMON domains were suspected to confer protein-protein interactions. The DOMON-like domain in murB may bind a heme.


Pssm-ID: 187685  Cd Length: 179  Bit Score: 40.00  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152318  35 SAPLFNDPPSPlgEPGKPFSELWNYEVVEAFFLNDTTKQYLEVELCPHGQHLVLLLAGRRN----VWKKELPLSFKASRG 110
Cdd:cd09627    42 PAALLIPLPAA--PAGGRRDGLWEHTCFELFLGAPGQPGYWEFNLSPSGHWNAYRFEGYRQrlegELSAEPPRIGLTRQP 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152318 111 GTNWEGeAYIPWSYFPPNVTKFNSFAIHGSNDRRVYEALYPVPQHelqQGQKPDFHRLEYF 171
Cdd:cd09627   120 DDLRLG-LRLDLALLPPFVRGTLELGLTAVIEDGDGLLSYWALAH---PGAQPDFHDRDRF 176
 
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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