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Conserved domains on  [gi|504863220|ref|WP_015050322|]
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copper amine oxidase N-terminal domain-containing protein [Thermacetogenium phaeum]

Protein Classification

copper amine oxidase N-terminal domain-containing protein( domain architecture ID 10544882)

copper amine oxidase N-terminal domain-containing protein such as Brevibacillus choshinensis protease inhibitor, which inhibits serine proteases such as trypsin, chymotrypsin and subtilisin

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 ...
 171-267 1.05e-24

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: 94.21  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504863220  171 KNSRLYVSARFCARAFGipdANIMWDGTTGTARIIAGSRVIQMTIGSNVMSVNGASIVMDTVPEIVpPGRVMLPIGWLAQ 250
Cdd:pfam07833   1 KNGRTLVPLRAIAEALG---AKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLI-NGRTYVPLRFVAE 76

                          90
                  ....*....|....*..
gi 504863220  251 ALGAQATWDQTTQTATL 267
Cdd:pfam07833  77 ALGAKVDWDEATRTVYI 93
 
Name Accession Description Interval E-value
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 171-267 1.05e-24

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: 94.21  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504863220  171 KNSRLYVSARFCARAFGipdANIMWDGTTGTARIIAGSRVIQMTIGSNVMSVNGASIVMDTVPEIVpPGRVMLPIGWLAQ 250
Cdd:pfam07833   1 KNGRTLVPLRAIAEALG---AKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLI-NGRTYVPLRFVAE 76

                          90
                  ....*....|....*..
gi 504863220  251 ALGAQATWDQTTQTATL 267
Cdd:pfam07833  77 ALGAKVDWDEATRTVYI 93
 
Name Accession Description Interval E-value
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 171-267 1.05e-24

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: 94.21  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504863220  171 KNSRLYVSARFCARAFGipdANIMWDGTTGTARIIAGSRVIQMTIGSNVMSVNGASIVMDTVPEIVpPGRVMLPIGWLAQ 250
Cdd:pfam07833   1 KNGRTLVPLRAIAEALG---AKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLI-NGRTYVPLRFVAE 76

                          90
                  ....*....|....*..
gi 504863220  251 ALGAQATWDQTTQTATL 267
Cdd:pfam07833  77 ALGAKVDWDEATRTVYI 93
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 140-204 2.82e-10

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: 55.69  E-value: 2.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504863220  140 GGTTVmaVLRAGDPVMMVNGQGIVMDALPYLKNSRLYVSARFCARAFGipdANIMWDGTTGTARI 204
Cdd:pfam07833  34 GGTTI--KLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALG---AKVDWDEATRTVYI 93
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 239-268 1.15e-05

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: 42.98  E-value: 1.15e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 504863220  239 GRVMLPIGWLAQALGAQATWDQTTQTATLE 268
Cdd:pfam07833   3 GRTLVPLRAIAEALGAKVDWDGKTKTVTIT 32
 
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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