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Conserved domains on  [gi|18404500|ref|NP_566763|]
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Auxin-responsive family protein [Arabidopsis thaliana]

Protein Classification

cytochrome and DOMON domain-containing protein( domain architecture ID 10176448)

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
DOMON_CIL1_like cd09629
DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has ...
39-195 1.07e-65

DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has been described as involved in suppression of axillary meristem development. It contains a single DOMON domain, the function of which is unclear. Members in this diverse family of plant proteins may have a cytochrome b561 domain C-terminal to the DOMON domain, some members from Arabidopsis have been characterized as auxin-responsive or auxin-induced proteins. 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: 187687  Cd Length: 152  Bit Score: 205.96  E-value: 1.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500  39 YPHCLDLPQLKAFLHYSYDASNTTLAVVFSAPPAKPGGWIAWAINPKATGMVGSQTLVAYKDPgNGVAVVKTLNISSYSS 118
Cdd:cd09629   1 FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSSSGWVAWGINPTGTGMVGTQALVAFRNS-NGSVLVYTYNITSYTK 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18404500 119 LIPS-KLAFDVWDMKAEEAardGGSLRIFARVKVPADLvakGKVNQVWQVGPELGpGGMIGRHAFDSANLASMSSLDL 195
Cdd:cd09629  80 LGEPlPLSFDVSDLSAEYS---GGEMTIFATLKLPSNL---TSVNHVWQVGPAVT-GGSPGPHPTSGANLASKGTLDL 150
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
187-373 1.25e-54

Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


:

Pssm-ID: 176490  Cd Length: 191  Bit Score: 178.69  E-value: 1.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500 187 LASMSSLDL-KGDNSGGTISGGDEVNAKIKNRN----IHGILNAVSWGILFPIGAIIARYMRvfdSADPAWFYLHVSCQF 261
Cdd:cd08760   1 SKSSYSLDLaSGTSSSGGSPFLLPNGSSVGSSDtlikAHGVLMAIAWGILMPIGALLARYFL---LGDPVWFYLHAGLQL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500 262 SAYVIGVAGWATGLKLGNESEGIRFSAHRNIGIALFTLATIQMFAMLLRPKKDHKYRFYWNIYHHGVGYAILTLGIINVF 341
Cdd:cd08760  78 LAVLLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIF 157
                       170       180       190
                ....*....|....*....|....*....|....
gi 18404500 342 KGLNILKPQ--DTYKTAYIAVIAVLGGIALLLEA 373
Cdd:cd08760 158 LGLDLAGAGtpKAWKIAYGVVVAVLALVYLILEI 191
 
Name Accession Description Interval E-value
DOMON_CIL1_like cd09629
DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has ...
39-195 1.07e-65

DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has been described as involved in suppression of axillary meristem development. It contains a single DOMON domain, the function of which is unclear. Members in this diverse family of plant proteins may have a cytochrome b561 domain C-terminal to the DOMON domain, some members from Arabidopsis have been characterized as auxin-responsive or auxin-induced proteins. 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: 187687  Cd Length: 152  Bit Score: 205.96  E-value: 1.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500  39 YPHCLDLPQLKAFLHYSYDASNTTLAVVFSAPPAKPGGWIAWAINPKATGMVGSQTLVAYKDPgNGVAVVKTLNISSYSS 118
Cdd:cd09629   1 FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSSSGWVAWGINPTGTGMVGTQALVAFRNS-NGSVLVYTYNITSYTK 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18404500 119 LIPS-KLAFDVWDMKAEEAardGGSLRIFARVKVPADLvakGKVNQVWQVGPELGpGGMIGRHAFDSANLASMSSLDL 195
Cdd:cd09629  80 LGEPlPLSFDVSDLSAEYS---GGEMTIFATLKLPSNL---TSVNHVWQVGPAVT-GGSPGPHPTSGANLASKGTLDL 150
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
187-373 1.25e-54

Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176490  Cd Length: 191  Bit Score: 178.69  E-value: 1.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500 187 LASMSSLDL-KGDNSGGTISGGDEVNAKIKNRN----IHGILNAVSWGILFPIGAIIARYMRvfdSADPAWFYLHVSCQF 261
Cdd:cd08760   1 SKSSYSLDLaSGTSSSGGSPFLLPNGSSVGSSDtlikAHGVLMAIAWGILMPIGALLARYFL---LGDPVWFYLHAGLQL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500 262 SAYVIGVAGWATGLKLGNESEGIRFSAHRNIGIALFTLATIQMFAMLLRPKKDHKYRFYWNIYHHGVGYAILTLGIINVF 341
Cdd:cd08760  78 LAVLLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIF 157
                       170       180       190
                ....*....|....*....|....*....|....
gi 18404500 342 KGLNILKPQ--DTYKTAYIAVIAVLGGIALLLEA 373
Cdd:cd08760 158 LGLDLAGAGtpKAWKIAYGVVVAVLALVYLILEI 191
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
219-344 1.26e-38

Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.


Pssm-ID: 214769  Cd Length: 129  Bit Score: 135.05  E-value: 1.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500    219 IHGILNAVSWGILFPIGAIIARYmRVFDSADPAWFYLHVSCQFSAYVIGVAGWATGLKLGNESEG-IRFSAHRNIGIALF 297
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARP-LTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGIaNFYSLHSWLGLAAF 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 18404500    298 TLATIQMFAMLLRPKKD---HKYRFYWNIYHHGVGYAILTLGIINVFKGL 344
Cdd:smart00665  80 VLAGLQWLSGFLRPLPPglpSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
DUF568 pfam04526
Protein of unknown function (DUF568); Family of uncharacterized plant proteins.
89-195 3.88e-34

Protein of unknown function (DUF568); Family of uncharacterized plant proteins.


Pssm-ID: 461343  Cd Length: 100  Bit Score: 121.98  E-value: 3.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500    89 MVGSQTLVAYkDPGNGVAVVKTLNISSYSSLIPSKLAFDVWDMKAEEAardGGSLRIFARVKVPAdlVAKGKVNQVWQVG 168
Cdd:pfam04526   1 MVGAQALIAF-DPSNGSVVVKTYNLTSYTGISEPDLSFDVSDLSAEYS---GGEMTIFATLKLPP--GNSTTVNHVWQVG 74
                          90       100
                  ....*....|....*....|....*..
gi 18404500   169 PELGpGGMIGRHAFDSANLASMSSLDL 195
Cdd:pfam04526  75 PSVS-GGSPAIHPTSGDNLNSKGTLDL 100
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
47-199 4.21e-24

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: 96.72  E-value: 4.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500     47 QLKAFLHYSYDASNTtLAVVFSAPPAKpGGWIAWAINPKaTGMVGSQTLVAYKDPgNGVAVVKTLNISSYSSLIPsKLAF 126
Cdd:smart00664   1 SCDYFLSWSVDGENS-IAFELSGPTST-NGWVAIGFSPD-GQMAGADVVVAWVDN-NGRVTVKDYYTPGYGPPVE-DDQQ 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18404500    127 DVWDMKaeEAARDGGSLRIFARVKVPAD-----LVAKGKVNQVWQVGPeLGPGGMIGRHAFDsanLASMSSLDLKGDN 199
Cdd:smart00664  76 DVTDLL--SATYENGVLTCRFRRKLGSNdpddkSLLDGTVHVLWAKGP-LSPNGGLGYHDFS---LKSTKKVCLSSCT 147
 
Name Accession Description Interval E-value
DOMON_CIL1_like cd09629
DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has ...
39-195 1.07e-65

DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has been described as involved in suppression of axillary meristem development. It contains a single DOMON domain, the function of which is unclear. Members in this diverse family of plant proteins may have a cytochrome b561 domain C-terminal to the DOMON domain, some members from Arabidopsis have been characterized as auxin-responsive or auxin-induced proteins. 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: 187687  Cd Length: 152  Bit Score: 205.96  E-value: 1.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500  39 YPHCLDLPQLKAFLHYSYDASNTTLAVVFSAPPAKPGGWIAWAINPKATGMVGSQTLVAYKDPgNGVAVVKTLNISSYSS 118
Cdd:cd09629   1 FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSSSGWVAWGINPTGTGMVGTQALVAFRNS-NGSVLVYTYNITSYTK 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18404500 119 LIPS-KLAFDVWDMKAEEAardGGSLRIFARVKVPADLvakGKVNQVWQVGPELGpGGMIGRHAFDSANLASMSSLDL 195
Cdd:cd09629  80 LGEPlPLSFDVSDLSAEYS---GGEMTIFATLKLPSNL---TSVNHVWQVGPAVT-GGSPGPHPTSGANLASKGTLDL 150
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
187-373 1.25e-54

Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176490  Cd Length: 191  Bit Score: 178.69  E-value: 1.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500 187 LASMSSLDL-KGDNSGGTISGGDEVNAKIKNRN----IHGILNAVSWGILFPIGAIIARYMRvfdSADPAWFYLHVSCQF 261
Cdd:cd08760   1 SKSSYSLDLaSGTSSSGGSPFLLPNGSSVGSSDtlikAHGVLMAIAWGILMPIGALLARYFL---LGDPVWFYLHAGLQL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500 262 SAYVIGVAGWATGLKLGNESEGIRFSAHRNIGIALFTLATIQMFAMLLRPKKDHKYRFYWNIYHHGVGYAILTLGIINVF 341
Cdd:cd08760  78 LAVLLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIF 157
                       170       180       190
                ....*....|....*....|....*....|....
gi 18404500 342 KGLNILKPQ--DTYKTAYIAVIAVLGGIALLLEA 373
Cdd:cd08760 158 LGLDLAGAGtpKAWKIAYGVVVAVLALVYLILEI 191
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
219-344 1.26e-38

Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.


Pssm-ID: 214769  Cd Length: 129  Bit Score: 135.05  E-value: 1.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500    219 IHGILNAVSWGILFPIGAIIARYmRVFDSADPAWFYLHVSCQFSAYVIGVAGWATGLKLGNESEG-IRFSAHRNIGIALF 297
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARP-LTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGIaNFYSLHSWLGLAAF 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 18404500    298 TLATIQMFAMLLRPKKD---HKYRFYWNIYHHGVGYAILTLGIINVFKGL 344
Cdd:smart00665  80 VLAGLQWLSGFLRPLPPglpSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
DUF568 pfam04526
Protein of unknown function (DUF568); Family of uncharacterized plant proteins.
89-195 3.88e-34

Protein of unknown function (DUF568); Family of uncharacterized plant proteins.


Pssm-ID: 461343  Cd Length: 100  Bit Score: 121.98  E-value: 3.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500    89 MVGSQTLVAYkDPGNGVAVVKTLNISSYSSLIPSKLAFDVWDMKAEEAardGGSLRIFARVKVPAdlVAKGKVNQVWQVG 168
Cdd:pfam04526   1 MVGAQALIAF-DPSNGSVVVKTYNLTSYTGISEPDLSFDVSDLSAEYS---GGEMTIFATLKLPP--GNSTTVNHVWQVG 74
                          90       100
                  ....*....|....*....|....*..
gi 18404500   169 PELGpGGMIGRHAFDSANLASMSSLDL 195
Cdd:pfam04526  75 PSVS-GGSPAIHPTSGDNLNSKGTLDL 100
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
47-199 4.21e-24

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: 96.72  E-value: 4.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404500     47 QLKAFLHYSYDASNTtLAVVFSAPPAKpGGWIAWAINPKaTGMVGSQTLVAYKDPgNGVAVVKTLNISSYSSLIPsKLAF 126
Cdd:smart00664   1 SCDYFLSWSVDGENS-IAFELSGPTST-NGWVAIGFSPD-GQMAGADVVVAWVDN-NGRVTVKDYYTPGYGPPVE-DDQQ 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18404500    127 DVWDMKaeEAARDGGSLRIFARVKVPAD-----LVAKGKVNQVWQVGPeLGPGGMIGRHAFDsanLASMSSLDLKGDN 199
Cdd:smart00664  76 DVTDLL--SATYENGVLTCRFRRKLGSNdpddkSLLDGTVHVLWAKGP-LSPNGGLGYHDFS---LKSTKKVCLSSCT 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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