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Conserved domains on  [gi|30456|emb|CAA68285|]
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unnamed protein product [Homo sapiens]

Protein Classification

Cu2_monooxygen and Cu2_monoox_C domain-containing protein( domain architecture ID 11141924)

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_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
 346-502 2.66e-96

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: 291.08  E-value: 2.66e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456      346 FNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNH 425
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTIDCTDKALPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGRDNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30456      426 YSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKTAVDAGFLQKYF 502
Cdd:pfam03712  81 YSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 200-323 1.32e-65

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: 210.57  E-value: 1.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456      200 MEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQC-APEMDSVPHFSGPC-DSKMKPDR 277
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECeGDPNEPSPGYGGDCySADNMPDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 30456      278 LNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNP 323
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNP 126
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
 45-158 2.87e-34

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: 125.93  E-value: 2.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456       45 LELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSD-QKGQIHLDPQQDYQLLQVQ 123
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSGKNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVYVQDYYTTgGYGAPRIDDQQDITLLSGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 30456      124 RTPEGLTLLFKRPFGTCDPKDYLI-EDGTVHLVYGI 158
Cdd:pfam03351  81 EEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116
 
Name Accession Description Interval E-value
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
 346-502 2.66e-96

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: 291.08  E-value: 2.66e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456      346 FNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNH 425
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTIDCTDKALPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGRDNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30456      426 YSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKTAVDAGFLQKYF 502
Cdd:pfam03712  81 YSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 200-323 1.32e-65

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: 210.57  E-value: 1.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456      200 MEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQC-APEMDSVPHFSGPC-DSKMKPDR 277
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECeGDPNEPSPGYGGDCySADNMPDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 30456      278 LNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNP 323
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNP 126
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
 45-158 2.87e-34

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: 125.93  E-value: 2.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456       45 LELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSD-QKGQIHLDPQQDYQLLQVQ 123
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSGKNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVYVQDYYTTgGYGAPRIDDQQDITLLSGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 30456      124 RTPEGLTLLFKRPFGTCDPKDYLI-EDGTVHLVYGI 158
Cdd:pfam03351  81 EEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
 37-155 2.24e-27

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: 107.59  E-value: 2.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456     37 IPLDPEGSLELSWNVSYTQEaIHFQLLVRRlKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQD 116
Cdd:cd09631   1 SSLDLDGNFSLSWSVDGEGT-ITFELSART-TGWVGIGFSPDGGMVGADAVVGWVDGGNAYVTDYYLTGRSTPDVDGSQD 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30456    117 YQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLV 155
Cdd:cd09631  79 LTLLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTYV 117
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 42-187 9.48e-23

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: 94.80  E-value: 9.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456        42 EGSLELSWNVSYTQEaIHFQLLVRRLKAG-VLFGMSDRGELENADLVVLWTDGD-TAYFADAWSDQKGQIHLDPQQDYQL 119
Cdd:smart00664   1 SCDYFLSWSVDGENS-IAFELSGPTSTNGwVAIGFSPDGQMAGADVVVAWVDNNgRVTVKDYYTPGYGPPVEDDQQDVTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30456       120 LQ-VQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQmGLQRVQLLKPN 187
Cdd:smart00664  80 LLsATYENGVLTCRFRRKLGSNDPDDKSLLDGTVHVLWAKGPLSPNGGLGYHDFSLK-STKKVCLSSCT 147
 
Name Accession Description Interval E-value
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
 346-502 2.66e-96

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: 291.08  E-value: 2.66e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456      346 FNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNH 425
Cdd:pfam03712   1 YDAGILLLGTVYSPKMAIPPGQKVFHLEGYCTIDCTDKALPESGIHPFASRLHTHLLGRVVSGYHVRDGQEWPLIGRDNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30456      426 YSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKTAVDAGFLQKYF 502
Cdd:pfam03712  81 YSPHYQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYYPRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 200-323 1.32e-65

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: 210.57  E-value: 1.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456      200 MEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQC-APEMDSVPHFSGPC-DSKMKPDR 277
Cdd:pfam01082   1 FDLLNPNVTVPAKDTTYWCTVFKLPDLTKKHHIIRFEPVIQPGNEGLVHHMLLYECeGDPNEPSPGYGGDCySADNMPDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 30456      278 LNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNP 323
Cdd:pfam01082  81 LDPCSSVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHYNNP 126
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
 45-158 2.87e-34

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: 125.93  E-value: 2.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456       45 LELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSD-QKGQIHLDPQQDYQLLQVQ 123
Cdd:pfam03351   1 YTVSWKVDGDNDEIEFELSGKNTNGWVAIGFSDDGKMGNADVVVGWVDNGRVYVQDYYTTgGYGAPRIDDQQDITLLSGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 30456      124 RTPEGLTLLFKRPFGTCDPKDYLI-EDGTVHLVYGI 158
Cdd:pfam03351  81 EEDGVTTCKFRRKLDTCDPQDNKIdLDTTYHLIWAA 116
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
 37-155 2.24e-27

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: 107.59  E-value: 2.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456     37 IPLDPEGSLELSWNVSYTQEaIHFQLLVRRlKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQD 116
Cdd:cd09631   1 SSLDLDGNFSLSWSVDGEGT-ITFELSART-TGWVGIGFSPDGGMVGADAVVGWVDGGNAYVTDYYLTGRSTPDVDGSQD 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30456    117 YQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLV 155
Cdd:cd09631  79 LTLLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTYV 117
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 42-187 9.48e-23

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: 94.80  E-value: 9.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30456        42 EGSLELSWNVSYTQEaIHFQLLVRRLKAG-VLFGMSDRGELENADLVVLWTDGD-TAYFADAWSDQKGQIHLDPQQDYQL 119
Cdd:smart00664   1 SCDYFLSWSVDGENS-IAFELSGPTSTNGwVAIGFSPDGQMAGADVVVAWVDNNgRVTVKDYYTPGYGPPVEDDQQDVTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30456       120 LQ-VQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQmGLQRVQLLKPN 187
Cdd:smart00664  80 LLsATYENGVLTCRFRRKLGSNDPDDKSLLDGTVHVLWAKGPLSPNGGLGYHDFSLK-STKKVCLSSCT 147
 
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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