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Conserved domains on  [gi|943463935|ref|NP_001303804|]
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Apextrin C-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

VMO-I domain-containing protein( domain architecture ID 10083057)

VMO-I domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 23-208 5.85e-70

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


:

Pssm-ID: 238135  Cd Length: 177  Bit Score: 218.03  E-value: 5.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935  23 KEIKSEEITRYGVWYGYVHCNEGEYAGGMQskfseihVHSFWSFfNFFDNTGLNAVRLYCQRIGASnsTNGSLNPIMSGE 102
Cdd:cd00220    1 TVIESPNGGNWGTWGQWERCPSGSFANGFQ-------LKYETPQ-GFSDDTGLNAIALFCNPPDGK--TSNSENEIISGE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935 103 GADGKWGEVKWCPNGTVITGFSLKSVPDRGpFKDDLGATSFRVYCGNPFEGRSTKLLLESDKNEWGTWTGDQFCDKGFAV 182
Cdd:cd00220   71 GPWGSWREIQWCPNGTVIVGFALRSEPEQG-KGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAV 149

                        170       180
                 ....*....|....*....|....*...
gi 943463935 183 CGIKSQVEA--RAKDTTALNNVNLHCCP 208
Cdd:cd00220  150 CGIQTRIEPpqGLGDDTALNNVNLKCCR 177
 
Name Accession Description Interval E-value
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 23-208 5.85e-70

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


Pssm-ID: 238135  Cd Length: 177  Bit Score: 218.03  E-value: 5.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935  23 KEIKSEEITRYGVWYGYVHCNEGEYAGGMQskfseihVHSFWSFfNFFDNTGLNAVRLYCQRIGASnsTNGSLNPIMSGE 102
Cdd:cd00220    1 TVIESPNGGNWGTWGQWERCPSGSFANGFQ-------LKYETPQ-GFSDDTGLNAIALFCNPPDGK--TSNSENEIISGE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935 103 GADGKWGEVKWCPNGTVITGFSLKSVPDRGpFKDDLGATSFRVYCGNPFEGRSTKLLLESDKNEWGTWTGDQFCDKGFAV 182
Cdd:cd00220   71 GPWGSWREIQWCPNGTVIVGFALRSEPEQG-KGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAV 149

                        170       180
                 ....*....|....*....|....*...
gi 943463935 183 CGIKSQVEA--RAKDTTALNNVNLHCCP 208
Cdd:cd00220  150 CGIQTRIEPpqGLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 25-207 1.09e-50

Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold.


Pssm-ID: 427492  Cd Length: 166  Bit Score: 167.84  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935   25 IKSEEITRYGVWYGYVHCNEGEYAGGMQSKFSEihvhsfWSFFnfFDNTGLNAVRLYCQRIGASNSTNgslnpIMSGEGA 104
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQ------PQGF--GDDTALNAIRLFCKPLDHDLNTN-----ITSGEGF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935  105 DGKWGEVKWCPNGTVITGFSLKSVPDRGpFKDDLGATSFRVYCGNPFEgrstkllLESDKN---EWGTWTGDQfCDKGFA 181
Cdd:pfam03762  68 WGDWSGIQYCPAGGYLTGFQLRVEPPQG-IGDDTAANNIRFRCSNGEE-------LEGDGNtwgDWGEWSTDQ-CPGGTA 138

                         170       180
                  ....*....|....*....|....*...
gi 943463935  182 VCGIKSQVEA--RAKDTTALNNVNLHCC 207
Cdd:pfam03762 139 ICGIQTRVEPyqGGLDDTALNDVRFFCC 166
 
Name Accession Description Interval E-value
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 23-208 5.85e-70

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


Pssm-ID: 238135  Cd Length: 177  Bit Score: 218.03  E-value: 5.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935  23 KEIKSEEITRYGVWYGYVHCNEGEYAGGMQskfseihVHSFWSFfNFFDNTGLNAVRLYCQRIGASnsTNGSLNPIMSGE 102
Cdd:cd00220    1 TVIESPNGGNWGTWGQWERCPSGSFANGFQ-------LKYETPQ-GFSDDTGLNAIALFCNPPDGK--TSNSENEIISGE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935 103 GADGKWGEVKWCPNGTVITGFSLKSVPDRGpFKDDLGATSFRVYCGNPFEGRSTKLLLESDKNEWGTWTGDQFCDKGFAV 182
Cdd:cd00220   71 GPWGSWREIQWCPNGTVIVGFALRSEPEQG-KGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAV 149

                        170       180
                 ....*....|....*....|....*...
gi 943463935 183 CGIKSQVEA--RAKDTTALNNVNLHCCP 208
Cdd:cd00220  150 CGIQTRIEPpqGLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 25-207 1.09e-50

Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold.


Pssm-ID: 427492  Cd Length: 166  Bit Score: 167.84  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935   25 IKSEEITRYGVWYGYVHCNEGEYAGGMQSKFSEihvhsfWSFFnfFDNTGLNAVRLYCQRIGASNSTNgslnpIMSGEGA 104
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQ------PQGF--GDDTALNAIRLFCKPLDHDLNTN-----ITSGEGF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943463935  105 DGKWGEVKWCPNGTVITGFSLKSVPDRGpFKDDLGATSFRVYCGNPFEgrstkllLESDKN---EWGTWTGDQfCDKGFA 181
Cdd:pfam03762  68 WGDWSGIQYCPAGGYLTGFQLRVEPPQG-IGDDTAANNIRFRCSNGEE-------LEGDGNtwgDWGEWSTDQ-CPGGTA 138

                         170       180
                  ....*....|....*....|....*...
gi 943463935  182 VCGIKSQVEA--RAKDTTALNNVNLHCC 207
Cdd:pfam03762 139 ICGIQTRVEPyqGGLDDTALNDVRFFCC 166
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 162-213 2.10e-06

Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold.


Pssm-ID: 427492  Cd Length: 166  Bit Score: 47.27  E-value: 2.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 943463935  162 SDKNEWGTWTGDQFCDKGFAVCGIKSQVEARAK--DTTALNNVNLHCCPVSEDV 213
Cdd:pfam03762   4 PNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGfgDDTALNAIRLFCKPLDHDL 57
 
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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