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Conserved domains on  [gi|2449442259|gb|WDS50277|]
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tailspike protein [Acinetobacter phage 3082-K84]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
phage_tailspike_middle super family cl40411
N-terminal and middle domains of tailspike protein in Acinetobacter bacteriophages; This model ...
 162-247 7.33e-06

N-terminal and middle domains of tailspike protein in Acinetobacter bacteriophages; This model describes the middle beta-helical domain of Acinetobacter bacteriophage tailspike proteins, as well as a separate N-terminal domain that does not appear to be part of the beta-helical substructure. The N-terminal domain may be involved in virion binding, and the molecules form a homo-trimeric arrangement. A C-terminal domain that may be involved in receptor binding is omitted from the model.


The actual alignment was detected with superfamily member cd20481:

Pssm-ID: 380473 [Multi-domain]  Cd Length: 419  Bit Score: 48.94  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449442259 162 SIADLFAI-PNPKSGSLVYVKSYHTGLNKGGGFRIYDE--TKGSQNNGFTVING----WVLTTDRYSVEQAGARGDGETD 234
Cdd:cd20481     7 TMADLRALkRTEDNGQVIYVQQYTPKYGGGGGLFYYDTtdTTTADNGGTIVVTAggkrWKRIDNGVDPTWFGADGNGVAD 86

                          90
                  ....*....|...
gi 2449442259 235 DSSAIQNALTVLY 247
Cdd:cd20481    87 SSPAIERAFDILY 99
GH55-like super family cl49631
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes ...
 221-284 3.80e-05

glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes glycoside hydrolase family 55 (GH55) domains, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching, found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Also included in this family is SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E, a secreted protein encoded by SACTE_4363. Structural studies reveal an extended substrate-binding cleft with six or more subsites for sugar binding formed at the interface of two right handed beta-helical domains. Mutation studies support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base. Trichoderma harzianum and T. viride LamA1 have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A, Chaetomium thermophilum CtLam55, as well as SacteLam55A, are exo-acting enzymes.


The actual alignment was detected with superfamily member cd23668:

Pssm-ID: 483971 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 3.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449442259 221 SVEQAGARGDGETDDSSAIQNALTVLypeISNRIqdfgpaLWFDSKRYKVSNTVLLPPYANIMG 284
Cdd:cd23668   305 NVKDYGAKGDGVTDDTAALQAILNTA---AGGKI------VYFPAGTYIVTDTLFIPPGSRIVG 359
 
Name Accession Description Interval E-value
phage_tailspike_middle cd20481
N-terminal and middle domains of tailspike protein in Acinetobacter bacteriophages; This model ...
 162-247 7.33e-06

N-terminal and middle domains of tailspike protein in Acinetobacter bacteriophages; This model describes the middle beta-helical domain of Acinetobacter bacteriophage tailspike proteins, as well as a separate N-terminal domain that does not appear to be part of the beta-helical substructure. The N-terminal domain may be involved in virion binding, and the molecules form a homo-trimeric arrangement. A C-terminal domain that may be involved in receptor binding is omitted from the model.


Pssm-ID: 380473 [Multi-domain]  Cd Length: 419  Bit Score: 48.94  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449442259 162 SIADLFAI-PNPKSGSLVYVKSYHTGLNKGGGFRIYDE--TKGSQNNGFTVING----WVLTTDRYSVEQAGARGDGETD 234
Cdd:cd20481     7 TMADLRALkRTEDNGQVIYVQQYTPKYGGGGGLFYYDTtdTTTADNGGTIVVTAggkrWKRIDNGVDPTWFGADGNGVAD 86

                          90
                  ....*....|...
gi 2449442259 235 DSSAIQNALTVLY 247
Cdd:cd20481    87 SSPAIERAFDILY 99
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
 221-284 3.80e-05

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 3.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449442259 221 SVEQAGARGDGETDDSSAIQNALTVLypeISNRIqdfgpaLWFDSKRYKVSNTVLLPPYANIMG 284
Cdd:cd23668   305 NVKDYGAKGDGVTDDTAALQAILNTA---AGGKI------VYFPAGTYIVTDTLFIPPGSRIVG 359
 
Name Accession Description Interval E-value
phage_tailspike_middle cd20481
N-terminal and middle domains of tailspike protein in Acinetobacter bacteriophages; This model ...
 162-247 7.33e-06

N-terminal and middle domains of tailspike protein in Acinetobacter bacteriophages; This model describes the middle beta-helical domain of Acinetobacter bacteriophage tailspike proteins, as well as a separate N-terminal domain that does not appear to be part of the beta-helical substructure. The N-terminal domain may be involved in virion binding, and the molecules form a homo-trimeric arrangement. A C-terminal domain that may be involved in receptor binding is omitted from the model.


Pssm-ID: 380473 [Multi-domain]  Cd Length: 419  Bit Score: 48.94  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449442259 162 SIADLFAI-PNPKSGSLVYVKSYHTGLNKGGGFRIYDE--TKGSQNNGFTVING----WVLTTDRYSVEQAGARGDGETD 234
Cdd:cd20481     7 TMADLRALkRTEDNGQVIYVQQYTPKYGGGGGLFYYDTtdTTTADNGGTIVVTAggkrWKRIDNGVDPTWFGADGNGVAD 86

                          90
                  ....*....|...
gi 2449442259 235 DSSAIQNALTVLY 247
Cdd:cd20481    87 SSPAIERAFDILY 99
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
 221-284 3.80e-05

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 3.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449442259 221 SVEQAGARGDGETDDSSAIQNALTVLypeISNRIqdfgpaLWFDSKRYKVSNTVLLPPYANIMG 284
Cdd:cd23668   305 NVKDYGAKGDGVTDDTAALQAILNTA---AGGKI------VYFPAGTYIVTDTLFIPPGSRIVG 359
GH55-like cd23271
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes ...
 217-295 4.39e-04

glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes glycoside hydrolase family 55 (GH55) domains, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching, found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Also included in this family is SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E, a secreted protein encoded by SACTE_4363. Structural studies reveal an extended substrate-binding cleft with six or more subsites for sugar binding formed at the interface of two right handed beta-helical domains. Mutation studies support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base. Trichoderma harzianum and T. viride LamA1 have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A, Chaetomium thermophilum CtLam55, as well as SacteLam55A, are exo-acting enzymes.


Pssm-ID: 467839 [Multi-domain]  Cd Length: 564  Bit Score: 43.52  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449442259 217 TDRYSVEQAGARGDGETDDSSAIQNALTVLYPEIsnriqdfgpALWFDSKRYKVSNTVLLPPYANIMG-GRSLMIGDAKS 295
Cdd:cd23271   250 SQFVSVKPGGAKGDGHTDDTEAINAAFDQGAGCL---------ILLFDPGVYIVTQTIEIPRATVILGeGLATIIPDGGK 320
 
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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