Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
892-946
2.06e-14
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
:
Pssm-ID: 271215 [Multi-domain] Cd Length: 57 Bit Score: 68.34 E-value: 2.06e-14
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
42-550
5.57e-148
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
Pssm-ID: 400342 [Multi-domain] Cd Length: 503 Bit Score: 448.30 E-value: 5.57e-148
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
892-946
2.06e-14
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
Pssm-ID: 271215 [Multi-domain] Cd Length: 57 Bit Score: 68.34 E-value: 2.06e-14
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
893-946
4.36e-13
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.
Pssm-ID: 459805 [Multi-domain] Cd Length: 56 Bit Score: 64.51 E-value: 4.36e-13
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
49-256
2.83e-06
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 51.16 E-value: 2.83e-06
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
42-550
5.57e-148
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
Pssm-ID: 400342 [Multi-domain] Cd Length: 503 Bit Score: 448.30 E-value: 5.57e-148
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
892-946
2.06e-14
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
Pssm-ID: 271215 [Multi-domain] Cd Length: 57 Bit Score: 68.34 E-value: 2.06e-14
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
893-946
4.36e-13
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.
Pssm-ID: 459805 [Multi-domain] Cd Length: 56 Bit Score: 64.51 E-value: 4.36e-13
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
49-256
2.83e-06
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 51.16 E-value: 2.83e-06
Dockerin repeat domain; Dockerins are modules in the cellulosome complex that often anchor ...
893-946
1.24e-05
Dockerin repeat domain; Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.
Pssm-ID: 271212 Cd Length: 56 Bit Score: 43.56 E-value: 1.24e-05
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
882-914
1.72e-05
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
Pssm-ID: 271215 [Multi-domain] Cd Length: 57 Bit Score: 42.91 E-value: 1.72e-05
Dockerin repeat domains and domains resembling dockerin repeats; Dockerins are modules in the ...
893-946
3.69e-05
Dockerin repeat domains and domains resembling dockerin repeats; Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.
Pssm-ID: 271211 Cd Length: 57 Bit Score: 42.29 E-value: 3.69e-05
Type II dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
893-946
1.46e-04
Type II dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall.
Pssm-ID: 271213 Cd Length: 54 Bit Score: 40.27 E-value: 1.46e-04
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
883-914
6.55e-04
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.
Pssm-ID: 459805 [Multi-domain] Cd Length: 56 Bit Score: 38.70 E-value: 6.55e-04
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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