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Conserved domains on  [gi|1916647|gb|AAC53189|]
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membrane amine oxidase, partial [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
 169-269 7.32e-37

Copper amine oxidase, N3 domain; This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


:

Pssm-ID: 426941 [Multi-domain]  Cd Length: 100  Bit Score: 127.44  E-value: 7.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916647    169 RPVLTREYQDIQEMIFhrELPQASGLLHHCCFYKRQGHNLLKMTTAPRGLQS-GDRATWFGIYYNLSGAGFYPHPIGLEL 247
Cdd:pfam02728   1 PPVTAEEYADIEEVIK--TDPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELEL 78

                          90       100
                  ....*....|....*....|..
gi 1916647    248 LVDHKALDPALWTIQKVFYQGR 269
Cdd:pfam02728  79 LVDHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
 66-152 8.70e-37

Copper amine oxidase, N2 domain; This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


:

Pssm-ID: 397027 [Multi-domain]  Cd Length: 87  Bit Score: 127.13  E-value: 8.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916647     66 EELTAVMSFLIKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGP 145
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80


                  ....*..
gi 1916647    146 LPHPSYM 152
Cdd:pfam02727  81 LPSPRYM 87
 
Name Accession Description Interval E-value
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
 169-269 7.32e-37

Copper amine oxidase, N3 domain; This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 426941 [Multi-domain]  Cd Length: 100  Bit Score: 127.44  E-value: 7.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916647    169 RPVLTREYQDIQEMIFhrELPQASGLLHHCCFYKRQGHNLLKMTTAPRGLQS-GDRATWFGIYYNLSGAGFYPHPIGLEL 247
Cdd:pfam02728   1 PPVTAEEYADIEEVIK--TDPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELEL 78

                          90       100
                  ....*....|....*....|..
gi 1916647    248 LVDHKALDPALWTIQKVFYQGR 269
Cdd:pfam02728  79 LVDHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
 66-152 8.70e-37

Copper amine oxidase, N2 domain; This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 397027 [Multi-domain]  Cd Length: 87  Bit Score: 127.13  E-value: 8.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916647     66 EELTAVMSFLIKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGP 145
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80


                  ....*..
gi 1916647    146 LPHPSYM 152
Cdd:pfam02727  81 LPSPRYM 87
 
Name Accession Description Interval E-value
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
 169-269 7.32e-37

Copper amine oxidase, N3 domain; This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 426941 [Multi-domain]  Cd Length: 100  Bit Score: 127.44  E-value: 7.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916647    169 RPVLTREYQDIQEMIFhrELPQASGLLHHCCFYKRQGHNLLKMTTAPRGLQS-GDRATWFGIYYNLSGAGFYPHPIGLEL 247
Cdd:pfam02728   1 PPVTAEEYADIEEVIK--TDPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELEL 78

                          90       100
                  ....*....|....*....|..
gi 1916647    248 LVDHKALDPALWTIQKVFYQGR 269
Cdd:pfam02728  79 LVDHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
 66-152 8.70e-37

Copper amine oxidase, N2 domain; This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 397027 [Multi-domain]  Cd Length: 87  Bit Score: 127.13  E-value: 8.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916647     66 EELTAVMSFLIKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGP 145
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80


                  ....*..
gi 1916647    146 LPHPSYM 152
Cdd:pfam02727  81 LPSPRYM 87
 
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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