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Conserved domains on  [gi|488243557|ref|WP_002314765|]
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MULTISPECIES: glycoside hydrolase family 88 protein [Enterococcus]

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 ...
52-302 5.95e-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: 50.83  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557   52 DWT-ASFWLGILFLTKELSNSKDFDRTIesqlASFKERLEKDI------ALDTHDIGFLYqlsaVADYRLNKNESSKQIA 124
Cdd:pfam07470  28 DWTnGVFLYGMLEAYEATGDKEYLDYLK----AWADSLIDEGGkiltpyNLDDINIGLTL----LDLYEHTGDERYIQAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557  125 IQAADRLMeRYSPKSQIIQAWGDLDDPKQrgrMIIDCL-MNLPLLYFATEATGDESYKTAAYNHAKQTQKYivrdnatty 203
Cdd:pfam07470 100 IELADWVL-ATPPRTSEGGFWHKDIYPHQ---MWLDGLfMAGPFLAKYGKLTNEPKYLDEAVYQFLLTRRH--------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557  204 htyYFDDVTGVPKYGRTQQGYSDES--CWARGQAWGIYGF--TLSYLYTGDGSFLETATQLADYFLQelpedLICYWDli 279
Cdd:pfam07470 167 ---LYDPETGLYYHGWDESGTEPWAdpFWARGNGWYAMALadVLELLPEKHPARQELINILRDLVKA-----LAKYQD-- 236
                         250       260
                  ....*....|....*....|....*....
gi 488243557  280 fKEGS------QEEKDSSAAAIAACGLLE 302
Cdd:pfam07470 237 -ESGLwhqsldDPDRDSYLETSASAGFVY 264
 
Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
52-302 5.95e-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: 50.83  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557   52 DWT-ASFWLGILFLTKELSNSKDFDRTIesqlASFKERLEKDI------ALDTHDIGFLYqlsaVADYRLNKNESSKQIA 124
Cdd:pfam07470  28 DWTnGVFLYGMLEAYEATGDKEYLDYLK----AWADSLIDEGGkiltpyNLDDINIGLTL----LDLYEHTGDERYIQAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557  125 IQAADRLMeRYSPKSQIIQAWGDLDDPKQrgrMIIDCL-MNLPLLYFATEATGDESYKTAAYNHAKQTQKYivrdnatty 203
Cdd:pfam07470 100 IELADWVL-ATPPRTSEGGFWHKDIYPHQ---MWLDGLfMAGPFLAKYGKLTNEPKYLDEAVYQFLLTRRH--------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557  204 htyYFDDVTGVPKYGRTQQGYSDES--CWARGQAWGIYGF--TLSYLYTGDGSFLETATQLADYFLQelpedLICYWDli 279
Cdd:pfam07470 167 ---LYDPETGLYYHGWDESGTEPWAdpFWARGNGWYAMALadVLELLPEKHPARQELINILRDLVKA-----LAKYQD-- 236
                         250       260
                  ....*....|....*....|....*....
gi 488243557  280 fKEGS------QEEKDSSAAAIAACGLLE 302
Cdd:pfam07470 237 -ESGLwhqsldDPDRDSYLETSASAGFVY 264
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
168-326 1.81e-03

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 40.22  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557 168 LYFATEATGDESYKTAAYNHAKQTQKYIVRDNATTYHTYYfDDVTGVPkygrtqqGYSDEscwargQAWGIYGFTLSYLY 247
Cdd:COG1331  422 LAEAGRVLGDPEYLEAAERAADFILDNLWDPDGRLLRSYR-DGEAGIP-------GFLED------YAFLIEALLALYEA 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557 248 TGDGSFLETATQLADYFLQEL--PEDLICYW------DLIFKEgsQEEKDS---SAAAIAACGLLELSKQLPvsdhrHFD 316
Cdd:COG1331  488 TGDPRWLERALELADEALEHFwdPEDGGFFFtaddaeDLIVRP--KEIYDGatpSGNSVAARNLLRLAALTG-----DER 560
                        170
                 ....*....|
gi 488243557 317 YEEMAVKILG 326
Cdd:COG1331  561 YRERAERALR 570
 
Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
52-302 5.95e-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: 50.83  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557   52 DWT-ASFWLGILFLTKELSNSKDFDRTIesqlASFKERLEKDI------ALDTHDIGFLYqlsaVADYRLNKNESSKQIA 124
Cdd:pfam07470  28 DWTnGVFLYGMLEAYEATGDKEYLDYLK----AWADSLIDEGGkiltpyNLDDINIGLTL----LDLYEHTGDERYIQAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557  125 IQAADRLMeRYSPKSQIIQAWGDLDDPKQrgrMIIDCL-MNLPLLYFATEATGDESYKTAAYNHAKQTQKYivrdnatty 203
Cdd:pfam07470 100 IELADWVL-ATPPRTSEGGFWHKDIYPHQ---MWLDGLfMAGPFLAKYGKLTNEPKYLDEAVYQFLLTRRH--------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557  204 htyYFDDVTGVPKYGRTQQGYSDES--CWARGQAWGIYGF--TLSYLYTGDGSFLETATQLADYFLQelpedLICYWDli 279
Cdd:pfam07470 167 ---LYDPETGLYYHGWDESGTEPWAdpFWARGNGWYAMALadVLELLPEKHPARQELINILRDLVKA-----LAKYQD-- 236
                         250       260
                  ....*....|....*....|....*....
gi 488243557  280 fKEGS------QEEKDSSAAAIAACGLLE 302
Cdd:pfam07470 237 -ESGLwhqsldDPDRDSYLETSASAGFVY 264
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
168-326 1.81e-03

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 40.22  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557 168 LYFATEATGDESYKTAAYNHAKQTQKYIVRDNATTYHTYYfDDVTGVPkygrtqqGYSDEscwargQAWGIYGFTLSYLY 247
Cdd:COG1331  422 LAEAGRVLGDPEYLEAAERAADFILDNLWDPDGRLLRSYR-DGEAGIP-------GFLED------YAFLIEALLALYEA 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488243557 248 TGDGSFLETATQLADYFLQEL--PEDLICYW------DLIFKEgsQEEKDS---SAAAIAACGLLELSKQLPvsdhrHFD 316
Cdd:COG1331  488 TGDPRWLERALELADEALEHFwdPEDGGFFFtaddaeDLIVRP--KEIYDGatpSGNSVAARNLLRLAALTG-----DER 560
                        170
                 ....*....|
gi 488243557 317 YEEMAVKILG 326
Cdd:COG1331  561 YRERAERALR 570
 
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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