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Conserved domains on  [gi|30680258|ref|NP_566306|]
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auxin-induced in root cultures-like protein [Arabidopsis thaliana]

Protein Classification

cytochrome and DOMON domain-containing protein; carbohydrate binding family 9 domain-containing protein( domain architecture ID 10176446)

cytochrome and DOMON domain-containing protein may bind heme and participate in electron transport reactions| carbohydrate binding family 9 (CBM9) domain-containing protein contains a DOMON-like carbohydrate binding module

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 ...
 61-213 9.11e-68

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: 207.12  E-value: 9.11e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258  61 FDSCEDLPVLNSYLHYTYNSSNSSLSVAFVATPSQAnGGWVAWAINPTGTKMAGSQAFLAYRSGGGAApVVKTYNISSYS 140
Cdd:cd09629   1 FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSS-SGWVAWGINPTGTGMVGTQALVAFRNSNGSV-LVYTYNITSYT 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30680258 141 -SLVEGKLAFDFWNLRAEsLSGGRIAIFTTVKVPAGADSVNQVWQIGGNVTNGRPGVHPFGPDNLGSHRVLSFT 213
Cdd:cd09629  79 kLGEPLPLSFDVSDLSAE-YSGGEMTIFATLKLPSNLTSVNHVWQVGPAVTGGSPGPHPTSGANLASKGTLDLL 151
 
Name Accession Description Interval E-value
DOMON_CIL1_like cd09629
DOMON-like domain of Brassica carinata CIL1 and similar proteins; Brassica carinata CIL1 has ...
 61-213 9.11e-68

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: 207.12  E-value: 9.11e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258  61 FDSCEDLPVLNSYLHYTYNSSNSSLSVAFVATPSQAnGGWVAWAINPTGTKMAGSQAFLAYRSGGGAApVVKTYNISSYS 140
Cdd:cd09629   1 FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSS-SGWVAWGINPTGTGMVGTQALVAFRNSNGSV-LVYTYNITSYT 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30680258 141 -SLVEGKLAFDFWNLRAEsLSGGRIAIFTTVKVPAGADSVNQVWQIGGNVTNGRPGVHPFGPDNLGSHRVLSFT 213
Cdd:cd09629  79 kLGEPLPLSFDVSDLSAE-YSGGEMTIFATLKLPSNLTSVNHVWQVGPAVTGGSPGPHPTSGANLASKGTLDLL 151
DUF568 pfam04526
Protein of unknown function (DUF568); Family of uncharacterized plant proteins.
 112-212 9.76e-35

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


Pssm-ID: 461343  Cd Length: 100  Bit Score: 120.83  E-value: 9.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258   112 MAGSQAFLAYRSGGGAaPVVKTYNISSYSSLVEGKLAFDFWNLRAEsLSGGRIAIFTTVKVPAGADS-VNQVWQIGGNVT 190
Cdd:pfam04526   1 MVGAQALIAFDPSNGS-VVVKTYNLTSYTGISEPDLSFDVSDLSAE-YSGGEMTIFATLKLPPGNSTtVNHVWQVGPSVS 78

                          90       100
                  ....*....|....*....|..
gi 30680258   191 NGRPGVHPFGPDNLGSHRVLSF 212
Cdd:pfam04526  79 GGSPAIHPTSGDNLNSKGTLDL 100
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 70-213 1.65e-27

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: 103.66  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258     70 LNSYLHYTYNSSNSslsVAFVATPSQANGGWVAWAINPTGtKMAGSQAFLAYRSGGGAaPVVKTYNISSYSSLVEgKLAF 149
Cdd:smart00664   2 CDYFLSWSVDGENS---IAFELSGPTSTNGWVAIGFSPDG-QMAGADVVVAWVDNNGR-VTVKDYYTPGYGPPVE-DDQQ 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30680258    150 DFWNLRAESLSGGRIAIFTTVKVPA--------GADSVNQVWQIGGNVTNGRPGVHPFGPDNLGSHRVLSFT 213
Cdd:smart00664  76 DVTDLLSATYENGVLTCRFRRKLGSndpddkslLDGTVHVLWAKGPLSPNGGLGYHDFSLKSTKKVCLSSCT 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 ...
 61-213 9.11e-68

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: 207.12  E-value: 9.11e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258  61 FDSCEDLPVLNSYLHYTYNSSNSSLSVAFVATPSQAnGGWVAWAINPTGTKMAGSQAFLAYRSGGGAApVVKTYNISSYS 140
Cdd:cd09629   1 FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSS-SGWVAWGINPTGTGMVGTQALVAFRNSNGSV-LVYTYNITSYT 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30680258 141 -SLVEGKLAFDFWNLRAEsLSGGRIAIFTTVKVPAGADSVNQVWQIGGNVTNGRPGVHPFGPDNLGSHRVLSFT 213
Cdd:cd09629  79 kLGEPLPLSFDVSDLSAE-YSGGEMTIFATLKLPSNLTSVNHVWQVGPAVTGGSPGPHPTSGANLASKGTLDLL 151
DUF568 pfam04526
Protein of unknown function (DUF568); Family of uncharacterized plant proteins.
 112-212 9.76e-35

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


Pssm-ID: 461343  Cd Length: 100  Bit Score: 120.83  E-value: 9.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258   112 MAGSQAFLAYRSGGGAaPVVKTYNISSYSSLVEGKLAFDFWNLRAEsLSGGRIAIFTTVKVPAGADS-VNQVWQIGGNVT 190
Cdd:pfam04526   1 MVGAQALIAFDPSNGS-VVVKTYNLTSYTGISEPDLSFDVSDLSAE-YSGGEMTIFATLKLPPGNSTtVNHVWQVGPSVS 78

                          90       100
                  ....*....|....*....|..
gi 30680258   191 NGRPGVHPFGPDNLGSHRVLSF 212
Cdd:pfam04526  79 GGSPAIHPTSGDNLNSKGTLDL 100
DoH smart00664
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ...
 70-213 1.65e-27

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: 103.66  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680258     70 LNSYLHYTYNSSNSslsVAFVATPSQANGGWVAWAINPTGtKMAGSQAFLAYRSGGGAaPVVKTYNISSYSSLVEgKLAF 149
Cdd:smart00664   2 CDYFLSWSVDGENS---IAFELSGPTSTNGWVAIGFSPDG-QMAGADVVVAWVDNNGR-VTVKDYYTPGYGPPVE-DDQQ 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30680258    150 DFWNLRAESLSGGRIAIFTTVKVPA--------GADSVNQVWQIGGNVTNGRPGVHPFGPDNLGSHRVLSFT 213
Cdd:smart00664  76 DVTDLLSATYENGVLTCRFRRKLGSndpddkslLDGTVHVLWAKGPLSPNGGLGYHDFSLKSTKKVCLSSCT 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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