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Conserved domains on  [gi|1863502745|gb|QLA69209|]
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glycoside hydrolase family 88 protein [Enterobacter cloacae]

Protein Classification

glycoside hydrolase family protein( domain architecture ID 721)

glycoside hydrolase (GH) family protein may catalyze the hydrolysis of glycosidic bonds in complex sugars; may be a member of glycosyl hydrolase families GH47, GH76, GH88, or GH127

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LanC_like super family cl04955
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
51-360 9.92e-07

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.


The actual alignment was detected with superfamily member pfam07470:

Pssm-ID: 471159  Cd Length: 345  Bit Score: 50.06  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745  51 ETCQQGFYPLTDNVEWTTS-FWTGQLwLAWEMSGDTRFREMAEKHVRSF---GLRIAGRNDTNTHDLGFLYTLscvaAWR 126
Cdd:pfam07470  14 PDGKVIDLPPDNRWDWTNGvFLYGML-EAYEATGDKEYLDYLKAWADSLideGGKILTPYNLDDINIGLTLLD----LYE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 127 LTGNREARGFSLLAAEALLERfHEKARIIQAWGDLSDPEQagrMIIDC-NMNLPLLYWATEQTGDPRFAAAAKAHVMQAA 205
Cdd:pfam07470  89 HTGDERYIQAAIELADWVLAT-PPRTSEGGFWHKDIYPHQ---MWLDGlFMAGPFLAKYGKLTNEPKYLDEAVYQFLLTR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 206 TYLirddastfhtyyMDVSTGAPRYGNTQQGYAD--DSCWSRGQAWGIYGFLlsyiytgdetmialskrlanYFLNRLPE 283
Cdd:pfam07470 165 RHL------------YDPETGLYYHGWDESGTEPwaDPFWARGNGWYAMALA--------------------DVLELLPE 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 284 DYVCHWDLALVgtdaLRDASSaAIAVCGLLELVKHLPVTDPDREHYLE----------WAKGI-MSSLTKHYLMGKEEKG 352
Cdd:pfam07470 213 KHPARQELINI----LRDLVK-ALAKYQDESGLWHQSLDDPDRDSYLEtsasagfvyaLAKGVnKGYLDKKYLPVAQKAW 287

                  ....*...
gi 1863502745 353 NGLLKHSV 360
Cdd:pfam07470 288 KALLKNFV 295
 
Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
51-360 9.92e-07

Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.


Pssm-ID: 429478  Cd Length: 345  Bit Score: 50.06  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745  51 ETCQQGFYPLTDNVEWTTS-FWTGQLwLAWEMSGDTRFREMAEKHVRSF---GLRIAGRNDTNTHDLGFLYTLscvaAWR 126
Cdd:pfam07470  14 PDGKVIDLPPDNRWDWTNGvFLYGML-EAYEATGDKEYLDYLKAWADSLideGGKILTPYNLDDINIGLTLLD----LYE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 127 LTGNREARGFSLLAAEALLERfHEKARIIQAWGDLSDPEQagrMIIDC-NMNLPLLYWATEQTGDPRFAAAAKAHVMQAA 205
Cdd:pfam07470  89 HTGDERYIQAAIELADWVLAT-PPRTSEGGFWHKDIYPHQ---MWLDGlFMAGPFLAKYGKLTNEPKYLDEAVYQFLLTR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 206 TYLirddastfhtyyMDVSTGAPRYGNTQQGYAD--DSCWSRGQAWGIYGFLlsyiytgdetmialskrlanYFLNRLPE 283
Cdd:pfam07470 165 RHL------------YDPETGLYYHGWDESGTEPwaDPFWARGNGWYAMALA--------------------DVLELLPE 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 284 DYVCHWDLALVgtdaLRDASSaAIAVCGLLELVKHLPVTDPDREHYLE----------WAKGI-MSSLTKHYLMGKEEKG 352
Cdd:pfam07470 213 KHPARQELINI----LRDLVK-ALAKYQDESGLWHQSLDDPDRDSYLEtsasagfvyaLAKGVnKGYLDKKYLPVAQKAW 287

                  ....*...
gi 1863502745 353 NGLLKHSV 360
Cdd:pfam07470 288 KALLKNFV 295
 
Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
51-360 9.92e-07

Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.


Pssm-ID: 429478  Cd Length: 345  Bit Score: 50.06  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745  51 ETCQQGFYPLTDNVEWTTS-FWTGQLwLAWEMSGDTRFREMAEKHVRSF---GLRIAGRNDTNTHDLGFLYTLscvaAWR 126
Cdd:pfam07470  14 PDGKVIDLPPDNRWDWTNGvFLYGML-EAYEATGDKEYLDYLKAWADSLideGGKILTPYNLDDINIGLTLLD----LYE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 127 LTGNREARGFSLLAAEALLERfHEKARIIQAWGDLSDPEQagrMIIDC-NMNLPLLYWATEQTGDPRFAAAAKAHVMQAA 205
Cdd:pfam07470  89 HTGDERYIQAAIELADWVLAT-PPRTSEGGFWHKDIYPHQ---MWLDGlFMAGPFLAKYGKLTNEPKYLDEAVYQFLLTR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 206 TYLirddastfhtyyMDVSTGAPRYGNTQQGYAD--DSCWSRGQAWGIYGFLlsyiytgdetmialskrlanYFLNRLPE 283
Cdd:pfam07470 165 RHL------------YDPETGLYYHGWDESGTEPwaDPFWARGNGWYAMALA--------------------DVLELLPE 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863502745 284 DYVCHWDLALVgtdaLRDASSaAIAVCGLLELVKHLPVTDPDREHYLE----------WAKGI-MSSLTKHYLMGKEEKG 352
Cdd:pfam07470 213 KHPARQELINI----LRDLVK-ALAKYQDESGLWHQSLDDPDRDSYLEtsasagfvyaLAKGVnKGYLDKKYLPVAQKAW 287

                  ....*...
gi 1863502745 353 NGLLKHSV 360
Cdd:pfam07470 288 KALLKNFV 295
 
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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