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Conserved domains on  [gi|134948567|ref|NP_647457|]
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DBH-like monooxygenase protein 2 precursor [Mus musculus]

Protein Classification

DOMON_DOH and Cu2_monooxygen domain-containing protein( domain architecture ID 10176538)

protein containing domains DOMON_DOH, Cu2_monooxygen, and Cu2_monoox_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
193-317 7.40e-53

Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


:

Pssm-ID: 460053  Cd Length: 130  Bit Score: 177.06  E-value: 7.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  193 HDLKISNFIIPEDDTTYACTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSV--LPTGIGECYGSD---PA 267
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECEGDPNepSPGYGGDCYSADnmpDD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 134948567  268 FSLCSHVIAGWAVGGLSYQFPDDVGISIGTPFDPQWIRLEIHYSNFQNLP 317
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNPDLKS 130
Cu2_monoox_C super family cl04225
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
336-482 2.09e-40

Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


The actual alignment was detected with superfamily member pfam03712:

Pssm-ID: 461021  Cd Length: 157  Bit Score: 144.32  E-value: 2.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  336 YDMGVLQLGISVFPIHFIPPGAEAFLSYGLCKTDkfeELNGA-PVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCK 414
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTID---CTDKAlPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134948567  415 DFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSCM 482
Cdd:pfam03712  78 DNPYSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCK 145
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
36-172 1.86e-34

DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


:

Pssm-ID: 187689  Cd Length: 138  Bit Score: 127.23  E-value: 1.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  36 LDPSRAVFLRWDFDYEaEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLpNGNVYFSDQHLLDEDTLEQDGSQDAE 115
Cdd:cd09631    3 LDLDGNFSLSWSVDGE-GTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVD-GGNAYVTDYYLTGRSTPDVDGSQDLT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134948567 116 LLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMR-VLAAYGPDDIPKMSREHTFVKS 172
Cdd:cd09631   81 LLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTyVIWAYGSEDPFSLLSYHGSKRG 138
 
Name Accession Description Interval E-value
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
193-317 7.40e-53

Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 460053  Cd Length: 130  Bit Score: 177.06  E-value: 7.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  193 HDLKISNFIIPEDDTTYACTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSV--LPTGIGECYGSD---PA 267
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECEGDPNepSPGYGGDCYSADnmpDD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 134948567  268 FSLCSHVIAGWAVGGLSYQFPDDVGISIGTPFDPQWIRLEIHYSNFQNLP 317
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNPDLKS 130
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
336-482 2.09e-40

Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 461021  Cd Length: 157  Bit Score: 144.32  E-value: 2.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  336 YDMGVLQLGISVFPIHFIPPGAEAFLSYGLCKTDkfeELNGA-PVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCK 414
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTID---CTDKAlPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134948567  415 DFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSCM 482
Cdd:pfam03712  78 DNPYSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCK 145
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
36-172 1.86e-34

DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


Pssm-ID: 187689  Cd Length: 138  Bit Score: 127.23  E-value: 1.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  36 LDPSRAVFLRWDFDYEaEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLpNGNVYFSDQHLLDEDTLEQDGSQDAE 115
Cdd:cd09631    3 LDLDGNFSLSWSVDGE-GTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVD-GGNAYVTDYYLTGRSTPDVDGSQDLT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134948567 116 LLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMR-VLAAYGPDDIPKMSREHTFVKS 172
Cdd:cd09631   81 LLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTyVIWAYGSEDPFSLLSYHGSKRG 138
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
39-183 3.92e-32

Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press).


Pssm-ID: 214768  Cd Length: 148  Bit Score: 121.38  E-value: 3.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567    39 SRAVFLRWDFDYEaEIITFELQVQTT--GWVGLGITDRYTFVGSDLVVGGVLPNGNVYFSDQHLLDEDTLEQDGSQDAE- 115
Cdd:smart00664   1 SCDYFLSWSVDGE-NSIAFELSGPTStnGWVAIGFSPDGQMAGADVVVAWVDNNGRVTVKDYYTPGYGPPVEDDQQDVTd 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134948567   116 LLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMRVLAAYGPDDIPKMSREHTFV-KSIFLLQMLQYDD 183
Cdd:smart00664  80 LLSATYENGVLTCRFRRKLGSNDPDDKSLLDGTVHVLWAKGPLSPNGGLGYHDFSlKSTKKVCLSSCTG 148
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
42-155 1.25e-22

DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families.


Pssm-ID: 460893 [Multi-domain]  Cd Length: 116  Bit Score: 93.19  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567   42 VFLRWDFDYEAEIITFELQV-QTTGWVGLGITDRYTFVGSDLVVGGVLpNGNVYFSDQHLLDEDTL-EQDGSQDAELLRL 119
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSGkNTNGWVAIGFSDDGKMGNADVVVGWVD-NGRVYVQDYYTTGGYGApRIDDQQDITLLSG 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 134948567  120 TEDAVSTTMRFSRPFRTCDPHDRDITSD-TMRVLAAY 155
Cdd:pfam03351  80 SEEDGVTTCKFRRKLDTCDPQDNKIDLDtTYHLIWAA 116
 
Name Accession Description Interval E-value
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
193-317 7.40e-53

Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 460053  Cd Length: 130  Bit Score: 177.06  E-value: 7.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  193 HDLKISNFIIPEDDTTYACTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSV--LPTGIGECYGSD---PA 267
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECEGDPNepSPGYGGDCYSADnmpDD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 134948567  268 FSLCSHVIAGWAVGGLSYQFPDDVGISIGTPFDPQWIRLEIHYSNFQNLP 317
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNPDLKS 130
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
336-482 2.09e-40

Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 461021  Cd Length: 157  Bit Score: 144.32  E-value: 2.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  336 YDMGVLQLGISVFPIHFIPPGAEAFLSYGLCKTDkfeELNGA-PVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCK 414
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTID---CTDKAlPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134948567  415 DFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSCM 482
Cdd:pfam03712  78 DNPYSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCK 145
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
36-172 1.86e-34

DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


Pssm-ID: 187689  Cd Length: 138  Bit Score: 127.23  E-value: 1.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567  36 LDPSRAVFLRWDFDYEaEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLpNGNVYFSDQHLLDEDTLEQDGSQDAE 115
Cdd:cd09631    3 LDLDGNFSLSWSVDGE-GTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVD-GGNAYVTDYYLTGRSTPDVDGSQDLT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134948567 116 LLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMR-VLAAYGPDDIPKMSREHTFVKS 172
Cdd:cd09631   81 LLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTyVIWAYGSEDPFSLLSYHGSKRG 138
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
39-183 3.92e-32

Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press).


Pssm-ID: 214768  Cd Length: 148  Bit Score: 121.38  E-value: 3.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567    39 SRAVFLRWDFDYEaEIITFELQVQTT--GWVGLGITDRYTFVGSDLVVGGVLPNGNVYFSDQHLLDEDTLEQDGSQDAE- 115
Cdd:smart00664   1 SCDYFLSWSVDGE-NSIAFELSGPTStnGWVAIGFSPDGQMAGADVVVAWVDNNGRVTVKDYYTPGYGPPVEDDQQDVTd 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134948567   116 LLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMRVLAAYGPDDIPKMSREHTFV-KSIFLLQMLQYDD 183
Cdd:smart00664  80 LLSATYENGVLTCRFRRKLGSNDPDDKSLLDGTVHVLWAKGPLSPNGGLGYHDFSlKSTKKVCLSSCTG 148
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
42-155 1.25e-22

DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families.


Pssm-ID: 460893 [Multi-domain]  Cd Length: 116  Bit Score: 93.19  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948567   42 VFLRWDFDYEAEIITFELQV-QTTGWVGLGITDRYTFVGSDLVVGGVLpNGNVYFSDQHLLDEDTL-EQDGSQDAELLRL 119
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSGkNTNGWVAIGFSDDGKMGNADVVVGWVD-NGRVYVQDYYTTGGYGApRIDDQQDITLLSG 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 134948567  120 TEDAVSTTMRFSRPFRTCDPHDRDITSD-TMRVLAAY 155
Cdd:pfam03351  80 SEEDGVTTCKFRRKLDTCDPQDNKIDLDtTYHLIWAA 116
 
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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