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Conserved domains on  [gi|695336955|ref|WP_032534545|]
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MULTISPECIES: hypothetical protein [Bacteroides]

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 ...
 30-135 1.58e-05

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 cd04793:

Pssm-ID: 471159  Cd Length: 377  Bit Score: 44.65  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695336955  30 GLFQGKMGISLFFFIYARYVSNHWYEEFAGELLEDVCNGL-DINIPITFVDGLCGIGWAIEFMVQSGyveGNTDEILINI 108
Cdd:cd04793    1 SLSSGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELnSAGLSLSLFSGLAGLAFALLALSRNG---GRYQNLLSEL 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 695336955 109 DSKVMERDLRRISDISFET-----------GLEGIVAY 135
Cdd:cd04793   78 NEYIDELAEDRLAEAIAREgispgeydvisGLSGIGRY 115
 
Name Accession Description Interval E-value
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
 30-135 1.58e-05

Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as precursor peptides 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. Also contains SpaC (the cyclase involved in the biosynthesis of subtilin), NisC, and homologs.


Pssm-ID: 271201  Cd Length: 377  Bit Score: 44.65  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695336955  30 GLFQGKMGISLFFFIYARYVSNHWYEEFAGELLEDVCNGL-DINIPITFVDGLCGIGWAIEFMVQSGyveGNTDEILINI 108
Cdd:cd04793    1 SLSSGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELnSAGLSLSLFSGLAGLAFALLALSRNG---GRYQNLLSEL 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 695336955 109 DSKVMERDLRRISDISFET-----------GLEGIVAY 135
Cdd:cd04793   78 NEYIDELAEDRLAEAIAREgispgeydvisGLSGIGRY 115
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
28-87 2.38e-03

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 38.18  E-value: 2.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695336955  28 DSGLFQGKMGISLFFFIYARYVSNHWYEEFAGELLEDVCNGLDINIP----ITFVDGLCGIGWA 87
Cdd:COG4403   60 AADLYDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREELAgamgPGLFTGLGGIAYA 123
 
Name Accession Description Interval E-value
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
 30-135 1.58e-05

Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as precursor peptides 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. Also contains SpaC (the cyclase involved in the biosynthesis of subtilin), NisC, and homologs.


Pssm-ID: 271201  Cd Length: 377  Bit Score: 44.65  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695336955  30 GLFQGKMGISLFFFIYARYVSNHWYEEFAGELLEDVCNGL-DINIPITFVDGLCGIGWAIEFMVQSGyveGNTDEILINI 108
Cdd:cd04793    1 SLSSGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELnSAGLSLSLFSGLAGLAFALLALSRNG---GRYQNLLSEL 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 695336955 109 DSKVMERDLRRISDISFET-----------GLEGIVAY 135
Cdd:cd04793   78 NEYIDELAEDRLAEAIAREgispgeydvisGLSGIGRY 115
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
28-87 2.38e-03

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 38.18  E-value: 2.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695336955  28 DSGLFQGKMGISLFFFIYARYVSNHWYEEFAGELLEDVCNGLDINIP----ITFVDGLCGIGWA 87
Cdd:COG4403   60 AADLYDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREELAgamgPGLFTGLGGIAYA 123
 
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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