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Conserved domains on  [gi|506405465|ref|WP_015925184|]
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stalk domain-containing protein [Ruminiclostridium cellulolyticum]

Protein Classification

Cu_amine_oxidN1 domain-containing protein( domain architecture ID 10277759)

Cu_amine_oxidN1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 62-153 2.78e-20

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


:

Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 85.73  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506405465   62 VQGKTFVPVKVITDALGASFTPDLKKKTAVIKYNDVEIKITDKKKEAVIAGKKTKMDAAPYIKNSSFMASVTFLADVFGA 141
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALGA 80

                          90
                  ....*....|..
gi 506405465  142 DLKNSGGKVTFT 153
Cdd:pfam07833  81 KVDWDEATRTVY 92
Cu_amine_oxidN1 super family cl06736
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 29-92 1.96e-06

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


The actual alignment was detected with superfamily member pfam07833:

Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 46.44  E-value: 1.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506405465   29 DENTSTII------TVSFKAGTTSYTVNGKAVKAEASA-VVQGKTFVPVKVITDALGASFTPDLKKKTAVI 92
Cdd:pfam07833  23 DGKTKTVTitkggtTIKLTIGSNTATVNGQEITLDVPPvLINGRTYVPLRFVAEALGAKVDWDEATRTVYI 93
 
Name Accession Description Interval E-value
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 62-153 2.78e-20

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 85.73  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506405465   62 VQGKTFVPVKVITDALGASFTPDLKKKTAVIKYNDVEIKITDKKKEAVIAGKKTKMDAAPYIKNSSFMASVTFLADVFGA 141
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALGA 80

                          90
                  ....*....|..
gi 506405465  142 DLKNSGGKVTFT 153
Cdd:pfam07833  81 KVDWDEATRTVY 92
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 29-92 1.96e-06

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 46.44  E-value: 1.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506405465   29 DENTSTII------TVSFKAGTTSYTVNGKAVKAEASA-VVQGKTFVPVKVITDALGASFTPDLKKKTAVI 92
Cdd:pfam07833  23 DGKTKTVTitkggtTIKLTIGSNTATVNGQEITLDVPPvLINGRTYVPLRFVAEALGAKVDWDEATRTVYI 93
 
Name Accession Description Interval E-value
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 62-153 2.78e-20

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 85.73  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506405465   62 VQGKTFVPVKVITDALGASFTPDLKKKTAVIKYNDVEIKITDKKKEAVIAGKKTKMDAAPYIKNSSFMASVTFLADVFGA 141
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALGA 80

                          90
                  ....*....|..
gi 506405465  142 DLKNSGGKVTFT 153
Cdd:pfam07833  81 KVDWDEATRTVY 92
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 29-92 1.96e-06

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 46.44  E-value: 1.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506405465   29 DENTSTII------TVSFKAGTTSYTVNGKAVKAEASA-VVQGKTFVPVKVITDALGASFTPDLKKKTAVI 92
Cdd:pfam07833  23 DGKTKTVTitkggtTIKLTIGSNTATVNGQEITLDVPPvLINGRTYVPLRFVAEALGAKVDWDEATRTVYI 93
 
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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