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Conserved domains on  [gi|386765490|ref|NP_001247027|]
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skeletor, isoform E [Drosophila melanogaster]

Protein Classification

cytochrome and DOMON domain-containing protein( domain architecture ID 11274691)

cytochrome and DOMON domain-containing protein may bind heme and participate in electron transport reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DM13 smart00686
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ...
 158-264 1.14e-51

Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9;


:

Pssm-ID: 128929  Cd Length: 108  Bit Score: 177.16  E-value: 1.14e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    158 RGVHGVSSDNIVIVDAQTLLVPNFSYDGEAPDAKFWVGRGQRPTSD-GLRIPDENGKENPLRRYERKTIVLTLPEDLTIF 236
Cdd:smart00686    1 SLQHGVSSDPVEIVDAKTLRIPNFSYDGSGPDAYFWVGAGSRPDNEgGKKVPDEYGYCNPLRRYHNEDIVLRLPESLTID 80

                            90       100
                    ....*....|....*....|....*...
gi 386765490    237 DIGHFGVWCEAFTVDFGHVRLPEGLNVP 264
Cdd:smart00686   81 DIKWFSVWCLKTAHNFGHVLFPENLNIP 108
DM13 smart00686
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ...
 42-149 6.23e-48

Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9;


:

Pssm-ID: 128929  Cd Length: 108  Bit Score: 166.38  E-value: 6.23e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490     42 RLHHGVSGD-VYAVDSRTIFIKKFNYDGEAPAAYFYVGNTARPSNEGAARLRDERGgTASLTRRYRNKDVTLSLPEGKTL 120
Cdd:smart00686    1 SLQHGVSSDpVEIVDAKTLRIPNFSYDGSGPDAYFWVGAGSRPDNEGGKKVPDEYG-YCNPLRRYHNEDIVLRLPESLTI 79

                            90       100
                    ....*....|....*....|....*....
gi 386765490    121 RDIKWFSVWCDEFAVNFGDVSIPPNLDFP 149
Cdd:smart00686   80 DDIKWFSVWCLKTAHNFGHVLFPENLNIP 108
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 286-447 1.20e-28

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: 112.90  E-value: 1.20e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    286 DLAFEVRWAVAGE-SIVVQLVAKLEPNHYMSFGISPNKnisQMIGADAVVAWVDPqTGNGFATDYFLEGKAQCSggrgac 364
Cdd:smart00664    1 SCDYFLSWSVDGEnSIAFELSGPTSTNGWVAIGFSPDG---QMAGADVVVAWVDN-NGRVTVKDYYTPGYGPPV------ 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    365 PDTKISEKTNsirlLNAAMVNGYSIVTYQRSLAATDRLDLPISiTGAESVVWAIGPLNDYQEVSFHTFYNKHLHQIEFGR 444
Cdd:smart00664   71 EDDQQDVTDL----LSATYENGVLTCRFRRKLGSNDPDDKSLL-DGTVHVLWAKGPLSPNGGLGYHDFSLKSTKKVCLSS 145


                    ...
gi 386765490    445 QPK 447
Cdd:smart00664  146 CTG 148
 
Name Accession Description Interval E-value
DM13 smart00686
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ...
 158-264 1.14e-51

Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9;


Pssm-ID: 128929  Cd Length: 108  Bit Score: 177.16  E-value: 1.14e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    158 RGVHGVSSDNIVIVDAQTLLVPNFSYDGEAPDAKFWVGRGQRPTSD-GLRIPDENGKENPLRRYERKTIVLTLPEDLTIF 236
Cdd:smart00686    1 SLQHGVSSDPVEIVDAKTLRIPNFSYDGSGPDAYFWVGAGSRPDNEgGKKVPDEYGYCNPLRRYHNEDIVLRLPESLTID 80

                            90       100
                    ....*....|....*....|....*...
gi 386765490    237 DIGHFGVWCEAFTVDFGHVRLPEGLNVP 264
Cdd:smart00686   81 DIKWFSVWCLKTAHNFGHVLFPENLNIP 108
DM13 smart00686
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ...
 42-149 6.23e-48

Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9;


Pssm-ID: 128929  Cd Length: 108  Bit Score: 166.38  E-value: 6.23e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490     42 RLHHGVSGD-VYAVDSRTIFIKKFNYDGEAPAAYFYVGNTARPSNEGAARLRDERGgTASLTRRYRNKDVTLSLPEGKTL 120
Cdd:smart00686    1 SLQHGVSSDpVEIVDAKTLRIPNFSYDGSGPDAYFWVGAGSRPDNEGGKKVPDEYG-YCNPLRRYHNEDIVLRLPESLTI 79

                            90       100
                    ....*....|....*....|....*....
gi 386765490    121 RDIKWFSVWCDEFAVNFGDVSIPPNLDFP 149
Cdd:smart00686   80 DDIKWFSVWCLKTAHNFGHVLFPENLNIP 108
DM13 pfam10517
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 40-142 1.77e-36

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


Pssm-ID: 463130  Cd Length: 105  Bit Score: 133.52  E-value: 1.77e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    40 LTRLHHGVSGDVYAVDSRTIFIKKFNYDGEAPAAYFYVGNTARPSNEGAARLRDERGGTASLTRRYRNKD-VTLSLPEGK 118
Cdd:pfam10517    2 FVSGEHGTSGTVYIVDDRTLELEGFATDGPGPDLYVWLGDSPVPSGKDGFKVPDEDGVTLGPLKGYSGEQrYTLTLPAGV 81

                           90       100
                   ....*....|....*....|....
gi 386765490   119 TLRDIKWFSVWCDEFAVNFGDVSI 142
Cdd:pfam10517   82 DLADYKSVSIWCERFNVNFGAAPL 105
DM13 pfam10517
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 161-257 1.75e-30

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


Pssm-ID: 463130  Cd Length: 105  Bit Score: 116.58  E-value: 1.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490   161 HGVSSDnIVIVDAQTLLVPNFSYDGEAPDAKFWVGRGQRPTS-DGLRIPDENGKEN-PLRRYERKT-IVLTLPEDLTIFD 237
Cdd:pfam10517    7 HGTSGT-VYIVDDRTLELEGFATDGPGPDLYVWLGDSPVPSGkDGFKVPDEDGVTLgPLKGYSGEQrYTLTLPAGVDLAD 85

                           90       100
                   ....*....|....*....|
gi 386765490   238 IGHFGVWCEAFTVDFGHVRL 257
Cdd:pfam10517   86 YKSVSIWCERFNVNFGAAPL 105
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 286-447 1.20e-28

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: 112.90  E-value: 1.20e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    286 DLAFEVRWAVAGE-SIVVQLVAKLEPNHYMSFGISPNKnisQMIGADAVVAWVDPqTGNGFATDYFLEGKAQCSggrgac 364
Cdd:smart00664    1 SCDYFLSWSVDGEnSIAFELSGPTSTNGWVAIGFSPDG---QMAGADVVVAWVDN-NGRVTVKDYYTPGYGPPV------ 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    365 PDTKISEKTNsirlLNAAMVNGYSIVTYQRSLAATDRLDLPISiTGAESVVWAIGPLNDYQEVSFHTFYNKHLHQIEFGR 444
Cdd:smart00664   71 EDDQQDVTDL----LSATYENGVLTCRFRRKLGSNDPDDKSLL-DGTVHVLWAKGPLSPNGGLGYHDFSLKSTKKVCLSS 145


                    ...
gi 386765490    445 QPK 447
Cdd:smart00664  146 CTG 148
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
 289-435 1.05e-24

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: 101.04  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490  289 FEVRWAVAG-ESIVVQLVAKlePNHYMSFGISPNKnisQMIGADAVVAWVDPqtGNGFATDYFLEGKAqcsggrgaCPDT 367
Cdd:cd09631     9 FSLSWSVDGeGTITFELSAR--TTGWVGIGFSPDG---GMVGADAVVGWVDG--GNAYVTDYYLTGRS--------TPDV 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765490  368 KiseKTNSIRLLNAAMVNGYSIVTYQRSLAATDRLDLPISITGAESVVWAIGPLNDYQEVSFHTFYNK 435
Cdd:cd09631    74 D---GSQDLTLLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTYVIWAYGSEDPFSLLSYHGSKRG 138
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
 289-418 1.86e-19

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: 85.49  E-value: 1.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490   289 FEVRWAV--AGESIVVQLVAKlEPNHYMSFGISPNKnisQMIGADAVVAWVDPqtGNGFATDYFLEGkaqcsGGRGACPD 366
Cdd:pfam03351    1 YTVSWKVdgDNDEIEFELSGK-NTNGWVAIGFSDDG---KMGNADVVVGWVDN--GRVYVQDYYTTG-----GYGAPRID 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386765490   367 TkisekTNSIRLLNAAMVNGYSIVTYQRSLAATDRLDLPISITGAESVVWAI 418
Cdd:pfam03351   70 D-----QQDITLLSGSEEDGVTTCKFRRKLDTCDPQDNKIDLDTTYHLIWAA 116
 
Name Accession Description Interval E-value
DM13 smart00686
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ...
 158-264 1.14e-51

Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9;


Pssm-ID: 128929  Cd Length: 108  Bit Score: 177.16  E-value: 1.14e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    158 RGVHGVSSDNIVIVDAQTLLVPNFSYDGEAPDAKFWVGRGQRPTSD-GLRIPDENGKENPLRRYERKTIVLTLPEDLTIF 236
Cdd:smart00686    1 SLQHGVSSDPVEIVDAKTLRIPNFSYDGSGPDAYFWVGAGSRPDNEgGKKVPDEYGYCNPLRRYHNEDIVLRLPESLTID 80

                            90       100
                    ....*....|....*....|....*...
gi 386765490    237 DIGHFGVWCEAFTVDFGHVRLPEGLNVP 264
Cdd:smart00686   81 DIKWFSVWCLKTAHNFGHVLFPENLNIP 108
DM13 smart00686
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ...
 42-149 6.23e-48

Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9;


Pssm-ID: 128929  Cd Length: 108  Bit Score: 166.38  E-value: 6.23e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490     42 RLHHGVSGD-VYAVDSRTIFIKKFNYDGEAPAAYFYVGNTARPSNEGAARLRDERGgTASLTRRYRNKDVTLSLPEGKTL 120
Cdd:smart00686    1 SLQHGVSSDpVEIVDAKTLRIPNFSYDGSGPDAYFWVGAGSRPDNEGGKKVPDEYG-YCNPLRRYHNEDIVLRLPESLTI 79

                            90       100
                    ....*....|....*....|....*....
gi 386765490    121 RDIKWFSVWCDEFAVNFGDVSIPPNLDFP 149
Cdd:smart00686   80 DDIKWFSVWCLKTAHNFGHVLFPENLNIP 108
DM13 pfam10517
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 40-142 1.77e-36

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


Pssm-ID: 463130  Cd Length: 105  Bit Score: 133.52  E-value: 1.77e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    40 LTRLHHGVSGDVYAVDSRTIFIKKFNYDGEAPAAYFYVGNTARPSNEGAARLRDERGGTASLTRRYRNKD-VTLSLPEGK 118
Cdd:pfam10517    2 FVSGEHGTSGTVYIVDDRTLELEGFATDGPGPDLYVWLGDSPVPSGKDGFKVPDEDGVTLGPLKGYSGEQrYTLTLPAGV 81

                           90       100
                   ....*....|....*....|....
gi 386765490   119 TLRDIKWFSVWCDEFAVNFGDVSI 142
Cdd:pfam10517   82 DLADYKSVSIWCERFNVNFGAAPL 105
DM13 pfam10517
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 161-257 1.75e-30

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


Pssm-ID: 463130  Cd Length: 105  Bit Score: 116.58  E-value: 1.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490   161 HGVSSDnIVIVDAQTLLVPNFSYDGEAPDAKFWVGRGQRPTS-DGLRIPDENGKEN-PLRRYERKT-IVLTLPEDLTIFD 237
Cdd:pfam10517    7 HGTSGT-VYIVDDRTLELEGFATDGPGPDLYVWLGDSPVPSGkDGFKVPDEDGVTLgPLKGYSGEQrYTLTLPAGVDLAD 85

                           90       100
                   ....*....|....*....|
gi 386765490   238 IGHFGVWCEAFTVDFGHVRL 257
Cdd:pfam10517   86 YKSVSIWCERFNVNFGAAPL 105
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 286-447 1.20e-28

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: 112.90  E-value: 1.20e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    286 DLAFEVRWAVAGE-SIVVQLVAKLEPNHYMSFGISPNKnisQMIGADAVVAWVDPqTGNGFATDYFLEGKAQCSggrgac 364
Cdd:smart00664    1 SCDYFLSWSVDGEnSIAFELSGPTSTNGWVAIGFSPDG---QMAGADVVVAWVDN-NGRVTVKDYYTPGYGPPV------ 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490    365 PDTKISEKTNsirlLNAAMVNGYSIVTYQRSLAATDRLDLPISiTGAESVVWAIGPLNDYQEVSFHTFYNKHLHQIEFGR 444
Cdd:smart00664   71 EDDQQDVTDL----LSATYENGVLTCRFRRKLGSNDPDDKSLL-DGTVHVLWAKGPLSPNGGLGYHDFSLKSTKKVCLSS 145


                    ...
gi 386765490    445 QPK 447
Cdd:smart00664  146 CTG 148
DOMON_DOH cd09631
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ...
 289-435 1.05e-24

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: 101.04  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490  289 FEVRWAVAG-ESIVVQLVAKlePNHYMSFGISPNKnisQMIGADAVVAWVDPqtGNGFATDYFLEGKAqcsggrgaCPDT 367
Cdd:cd09631     9 FSLSWSVDGeGTITFELSAR--TTGWVGIGFSPDG---GMVGADAVVGWVDG--GNAYVTDYYLTGRS--------TPDV 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765490  368 KiseKTNSIRLLNAAMVNGYSIVTYQRSLAATDRLDLPISITGAESVVWAIGPLNDYQEVSFHTFYNK 435
Cdd:cd09631    74 D---GSQDLTLLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTYVIWAYGSEDPFSLLSYHGSKRG 138
DOMON pfam03351
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ...
 289-418 1.86e-19

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: 85.49  E-value: 1.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765490   289 FEVRWAV--AGESIVVQLVAKlEPNHYMSFGISPNKnisQMIGADAVVAWVDPqtGNGFATDYFLEGkaqcsGGRGACPD 366
Cdd:pfam03351    1 YTVSWKVdgDNDEIEFELSGK-NTNGWVAIGFSDDG---KMGNADVVVGWVDN--GRVYVQDYYTTG-----GYGAPRID 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386765490   367 TkisekTNSIRLLNAAMVNGYSIVTYQRSLAATDRLDLPISITGAESVVWAI 418
Cdd:pfam03351   70 D-----QQDITLLSGSEEDGVTTCKFRRKLDTCDPQDNKIDLDTTYHLIWAA 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.
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