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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571135   409 YDAAVMELGLEYTDKMAIPPGQTAFPLSGYCVADCTRAALPATGIIIFGSQLHTHLRGVRVLTRHFRGEQELREVNRDDY 488
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTIDCTDKALPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGRDNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571135   489 YSNHFQEMRTLHYKPRVLPGDALVTTCYYNTKDDKTAALGGFSISDEMCVNYIHYYPATKLEVCKSSVSEETLENYF 565
Cdd:pfam03712  81 YSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCKSSGPPEYLWNYF 157

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 28571135   106 IKLSWMVDWYKQEVLFHLQNafNEQHRWFYLGFSKRGGLADADICFFENQNGFFNaVTDTYTSPDGQWVRRDYQQDCEV- 184
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSG--KNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVY-VQDYYTTGGYGAPRIDDQQDITLl 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 28571135   185 ---FKMDEFTLAFRRKFDTCDPLDLRL-HEGTMYVVWAR 219
Cdd:pfam03351  78 sgsEEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571135   409 YDAAVMELGLEYTDKMAIPPGQTAFPLSGYCVADCTRAALPATGIIIFGSQLHTHLRGVRVLTRHFRGEQELREVNRDDY 488
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTIDCTDKALPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGRDNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571135   489 YSNHFQEMRTLHYKPRVLPGDALVTTCYYNTKDDKTAALGGFSISDEMCVNYIHYYPATKLEVCKSSVSEETLENYF 565
Cdd:pfam03712  81 YSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCKSSGPPEYLWNYF 157

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 28571135   106 IKLSWMVDWYKQEVLFHLQNafNEQHRWFYLGFSKRGGLADADICFFENQNGFFNaVTDTYTSPDGQWVRRDYQQDCEV- 184
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSG--KNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVY-VQDYYTTGGYGAPRIDDQQDITLl 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 28571135   185 ---FKMDEFTLAFRRKFDTCDPLDLRL-HEGTMYVVWAR 219
Cdd:pfam03351  78 sgsEEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116

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 28571135 103 DKEIKLSWMVDwYKQEVLFHLQNAFNEqhrWFYLGFSKRGGLADADICFFENQNGFFNaVTDTYTSpDGQWVRRDYQQDC 182
Cdd:cd09631   6 DGNFSLSWSVD-GEGTITFELSARTTG---WVGIGFSPDGGMVGADAVVGWVDGGNAY-VTDYYLT-GRSTPDVDGSQDL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 28571135 183 EVFKMDE----FTLAFRRKFDTCDPLDLRLHEGTM-YVVWARGET 222
Cdd:cd09631  80 TLLSGSEnngvTTLRFSRKLDTCDPTDLSITDGTTtYVIWAYGSE 124

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571135   409 YDAAVMELGLEYTDKMAIPPGQTAFPLSGYCVADCTRAALPATGIIIFGSQLHTHLRGVRVLTRHFRGEQELREVNRDDY 488
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTIDCTDKALPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGRDNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571135   489 YSNHFQEMRTLHYKPRVLPGDALVTTCYYNTKDDKTAALGGFSISDEMCVNYIHYYPATKLEVCKSSVSEETLENYF 565
Cdd:pfam03712  81 YSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCKSSGPPEYLWNYF 157

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 28571135   106 IKLSWMVDWYKQEVLFHLQNafNEQHRWFYLGFSKRGGLADADICFFENQNGFFNaVTDTYTSPDGQWVRRDYQQDCEV- 184
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSG--KNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVY-VQDYYTTGGYGAPRIDDQQDITLl 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 28571135   185 ---FKMDEFTLAFRRKFDTCDPLDLRL-HEGTMYVVWAR 219
Cdd:pfam03351  78 sgsEEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116

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 28571135 103 DKEIKLSWMVDwYKQEVLFHLQNAFNEqhrWFYLGFSKRGGLADADICFFENQNGFFNaVTDTYTSpDGQWVRRDYQQDC 182
Cdd:cd09631   6 DGNFSLSWSVD-GEGTITFELSARTTG---WVGIGFSPDGGMVGADAVVGWVDGGNAY-VTDYYLT-GRSTPDVDGSQDL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 28571135 183 EVFKMDE----FTLAFRRKFDTCDPLDLRLHEGTM-YVVWARGET 222
Cdd:cd09631  80 TLLSGSEnngvTTLRFSRKLDTCDPTDLSITDGTTtYVIWAYGSE 124