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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952 224 FDLVNQNVPIPNKGTTYWCQMFKIPIFQEKHHVIKVEPIIERGHESLVHHILLYQCSSNFNDSVLDFGHECYHP-NMPDA 302
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECEGDPNEPSPGYGGDCYSAdNMPDD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958651952 303 FLTCETVIFAWGIGGEGFTYPPHVGLSLGMPPDPRYVLLEVHYDNPARKK 352
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNPDLKS 130

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952  68 LDPEGKYWLLWGRQG-ERLAFRLEVRTNGYVGFGFSPTGTMAAADIVVGGVAHGRPYLQDYFTNADKELEKDAQQDYHLD 146
Cdd:cd09631     3 LDLDGNFSLSWSVDGeGTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVDGGNAYVTDYYLTGRSTPDVDGSQDLTLL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958651952 147 YAMENSTHTVIEFSRDLHTCDANDKSLTDSTVR-VIWAYHHEDPGeSGPKYHDSNRG 202
Cdd:cd09631    83 SGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTyVIWAYGSEDPF-SLLSYHGSKRG 138

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952 224 FDLVNQNVPIPNKGTTYWCQMFKIPIFQEKHHVIKVEPIIERGHESLVHHILLYQCSSNFNDSVLDFGHECYHP-NMPDA 302
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECEGDPNEPSPGYGGDCYSAdNMPDD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958651952 303 FLTCETVIFAWGIGGEGFTYPPHVGLSLGMPPDPRYVLLEVHYDNPARKK 352
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNPDLKS 130

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952  68 LDPEGKYWLLWGRQG-ERLAFRLEVRTNGYVGFGFSPTGTMAAADIVVGGVAHGRPYLQDYFTNADKELEKDAQQDYHLD 146
Cdd:cd09631     3 LDLDGNFSLSWSVDGeGTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVDGGNAYVTDYYLTGRSTPDVDGSQDLTLL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958651952 147 YAMENSTHTVIEFSRDLHTCDANDKSLTDSTVR-VIWAYHHEDPGeSGPKYHDSNRG 202
Cdd:cd09631    83 SGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTyVIWAYGSEDPF-SLLSYHGSKRG 138

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952  74 YWLLWGRQGERLAFRLEV---RTNGYVGFGFSPTGTMAAADIVVGGVAHGRPYLQDYFTNADKEL-EKDAQQDYHLDYAM 149
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELsgkNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVYVQDYYTTGGYGApRIDDQQDITLLSGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958651952 150 ENSTHTVIEFSRDLHTCDANDKSL-TDSTVRVIWAY 184
Cdd:pfam03351  81 EEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952 224 FDLVNQNVPIPNKGTTYWCQMFKIPIFQEKHHVIKVEPIIERGHESLVHHILLYQCSSNFNDSVLDFGHECYHP-NMPDA 302
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECEGDPNEPSPGYGGDCYSAdNMPDD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958651952 303 FLTCETVIFAWGIGGEGFTYPPHVGLSLGMPPDPRYVLLEVHYDNPARKK 352
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNPDLKS 130

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952  68 LDPEGKYWLLWGRQG-ERLAFRLEVRTNGYVGFGFSPTGTMAAADIVVGGVAHGRPYLQDYFTNADKELEKDAQQDYHLD 146
Cdd:cd09631     3 LDLDGNFSLSWSVDGeGTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVDGGNAYVTDYYLTGRSTPDVDGSQDLTLL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958651952 147 YAMENSTHTVIEFSRDLHTCDANDKSLTDSTVR-VIWAYHHEDPGeSGPKYHDSNRG 202
Cdd:cd09631    83 SGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTyVIWAYGSEDPF-SLLSYHGSKRG 138

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651952  74 YWLLWGRQGERLAFRLEV---RTNGYVGFGFSPTGTMAAADIVVGGVAHGRPYLQDYFTNADKEL-EKDAQQDYHLDYAM 149
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELsgkNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVYVQDYYTTGGYGApRIDDQQDITLLSGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958651952 150 ENSTHTVIEFSRDLHTCDANDKSL-TDSTVRVIWAY 184
Cdd:pfam03351  81 EEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116