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Conserved domains on  [gi|18416569|ref|NP_567722|]
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FLOWERING WAGENINGEN [Arabidopsis thaliana]

Protein Classification

SRPBCC family protein; homeobox-leucine zipper family START domain-containing protein( domain architecture ID 11078710)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket| homeobox-leucine zipper family START (steroidogenic acute regulatory protein (StAR)-related lipid transfer) domain-containing protein may bind lipids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
211-435 2.10e-98

C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells.


:

Pssm-ID: 176884  Cd Length: 229  Bit Score: 301.88  E-value: 2.10e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 211 SIFLNLAITALRELITLGEVDCPFWMIDPIVrsKGVSKIYEKYRSSFNNVT--KPPGQIVEASRAKGLVPMTCVTLVKTL 288
Cdd:cd08875   2 SGLLELAEEAMDELLKLAQGGEPLWIKSPGM--KPEILNPDEYERMFPRHGgsKPGGFTTEASRACGLVMMNAIKLVEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 289 MDTGKWVNVFAPIVPVASTHKVLSTGSGGTKSGSLQQIQAEFQVISPLVPKRKVTFIRYCKEIRQGLWVVVDVTPTQ--- 365
Cdd:cd08875  80 MDVNKWSELFPGIVSKAKTLQVISTGNGGNRNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGvqt 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 366 NPTLLPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCE 435
Cdd:cd08875 160 APPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEKPVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
Homeodomain pfam00046
Homeodomain;
40-96 1.87e-17

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 76.38  E-value: 1.87e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569    40 RMRRTHrrTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEK 96
Cdd:pfam00046   2 RKRTTF--TPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWK 56
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
479-632 7.44e-03

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd00177:

Pssm-ID: 472699 [Multi-domain]  Cd Length: 193  Bit Score: 38.09  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 479 SVDKWQKIQVENvaqNMSFMIRKNVNEPGELTGIVLSastsvwLPVNQHTLFAFISHLSFRHEWdiltnDTTMEETIRIQ 558
Cdd:cd00177  13 EPEGWKLVKEKD---GVKIYTKPYEDSGLKLLKAEGV------IPASPEQVFELLMDIDLRKKW-----DKNFEEFEVIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 559 KAKRHGNIIslLKIVNNGMLV--------LQEIWNDASGAMVVYAPVETNSIELVK---RGENsdsvkfLPSGFSIVPDG 627
Cdd:cd00177  79 EIDEHTDII--YYKTKPPWPVsprdfvylRRRRKLDDGTYVIVSKSVDHDSHPKEKgyvRAEI------KLSGWIIEPLD 150

                ....*
gi 18416569 628 VNGSY 632
Cdd:cd00177 151 PGKTK 155
 
Name Accession Description Interval E-value
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
211-435 2.10e-98

C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells.


Pssm-ID: 176884  Cd Length: 229  Bit Score: 301.88  E-value: 2.10e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 211 SIFLNLAITALRELITLGEVDCPFWMIDPIVrsKGVSKIYEKYRSSFNNVT--KPPGQIVEASRAKGLVPMTCVTLVKTL 288
Cdd:cd08875   2 SGLLELAEEAMDELLKLAQGGEPLWIKSPGM--KPEILNPDEYERMFPRHGgsKPGGFTTEASRACGLVMMNAIKLVEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 289 MDTGKWVNVFAPIVPVASTHKVLSTGSGGTKSGSLQQIQAEFQVISPLVPKRKVTFIRYCKEIRQGLWVVVDVTPTQ--- 365
Cdd:cd08875  80 MDVNKWSELFPGIVSKAKTLQVISTGNGGNRNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGvqt 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 366 NPTLLPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCE 435
Cdd:cd08875 160 APPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEKPVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
START pfam01852
START domain;
216-436 1.48e-59

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 199.17  E-value: 1.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569   216 LAITALRELITLGEVDCPFWMIDPivrskgVSKIYEKYRSSFNNvtkppgQIVEASRAKGLVPMTCVTLVKTLMDTG--- 292
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLS------SNENGDVVLQIVEP------DHGEASRASGVVPMVAALLVAELLKDMeyr 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569   293 -KWVNVFApivpVASTHKVLSTGsggtksGSLQQIQAEFQVISPLVPkRKVTFIRYCKEIRQGLWVVVD--VTPTQNPTL 369
Cdd:pfam01852  70 aQWDKDVR----SAETLEVISSG------GDLQYYVAALVAPSPLSP-RDFVFLRYWRRLGGGVYVIVDrsVTHPQFPPS 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569   370 LPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCES 436
Cdd:pfam01852 139 SGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
216-436 8.45e-53

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 180.71  E-value: 8.45e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569    216 LAITALRELITLGEVDCPFWMIDPivrskgVSKIYEKYRSSFNNVTKPpgqiVEASRAKGLVPMTCVTLVKTLMDTG--- 292
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSS------ENENGDEVRSIFSPGRKP----GEAFRLVGVVPMVCADLVEELMDDLeyr 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569    293 -KWVNVFApivpVASTHKVLSTGsggtksGSLQQIQAEFQViSPLVPkRKVTFIRYCKEIRQGLWVVVDVTPTQ--NPTL 369
Cdd:smart00234  71 pEWDKNVA----KAETLEVIDNG------TVIYHYVSKFAA-GPVSP-RDFVFVRYWREDEDGSYAVVDVSVTHptSPPE 138
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569    370 LPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCES 436
Cdd:smart00234 139 SGYVRAENLPSGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
Homeodomain pfam00046
Homeodomain;
40-96 1.87e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 76.38  E-value: 1.87e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569    40 RMRRTHrrTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEK 96
Cdd:pfam00046   2 RKRTTF--TPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWK 56
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
42-99 2.27e-16

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 73.43  E-value: 2.27e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18416569  42 RRTHRRTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEKINN 99
Cdd:cd00086   2 RKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
39-92 2.56e-15

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 70.36  E-value: 2.56e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18416569     39 GRMRRThRRTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKR 92
Cdd:smart00389   1 KRRKRT-SFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRR 53
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
25-138 9.55e-10

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 57.83  E-value: 9.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569  25 DMINDMSGVNDQDGGRMRRTHRR--TAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEKINNDHL 102
Cdd:COG5576  34 AADSEMKLERKQDGSSPPKSKRRrtTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGK 113
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18416569 103 ENVTLREEHDRllatqdqLRSAMLRSLCNICGKATN 138
Cdd:COG5576 114 VEQRPGEEEAD-------LAKIGSLSTGQISIIETL 142
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
479-632 7.44e-03

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 38.09  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 479 SVDKWQKIQVENvaqNMSFMIRKNVNEPGELTGIVLSastsvwLPVNQHTLFAFISHLSFRHEWdiltnDTTMEETIRIQ 558
Cdd:cd00177  13 EPEGWKLVKEKD---GVKIYTKPYEDSGLKLLKAEGV------IPASPEQVFELLMDIDLRKKW-----DKNFEEFEVIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 559 KAKRHGNIIslLKIVNNGMLV--------LQEIWNDASGAMVVYAPVETNSIELVK---RGENsdsvkfLPSGFSIVPDG 627
Cdd:cd00177  79 EIDEHTDII--YYKTKPPWPVsprdfvylRRRRKLDDGTYVIVSKSVDHDSHPKEKgyvRAEI------KLSGWIIEPLD 150

                ....*
gi 18416569 628 VNGSY 632
Cdd:cd00177 151 PGKTK 155
 
Name Accession Description Interval E-value
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
211-435 2.10e-98

C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells.


Pssm-ID: 176884  Cd Length: 229  Bit Score: 301.88  E-value: 2.10e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 211 SIFLNLAITALRELITLGEVDCPFWMIDPIVrsKGVSKIYEKYRSSFNNVT--KPPGQIVEASRAKGLVPMTCVTLVKTL 288
Cdd:cd08875   2 SGLLELAEEAMDELLKLAQGGEPLWIKSPGM--KPEILNPDEYERMFPRHGgsKPGGFTTEASRACGLVMMNAIKLVEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 289 MDTGKWVNVFAPIVPVASTHKVLSTGSGGTKSGSLQQIQAEFQVISPLVPKRKVTFIRYCKEIRQGLWVVVDVTPTQ--- 365
Cdd:cd08875  80 MDVNKWSELFPGIVSKAKTLQVISTGNGGNRNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGvqt 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 366 NPTLLPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCE 435
Cdd:cd08875 160 APPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEKPVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
START pfam01852
START domain;
216-436 1.48e-59

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 199.17  E-value: 1.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569   216 LAITALRELITLGEVDCPFWMIDPivrskgVSKIYEKYRSSFNNvtkppgQIVEASRAKGLVPMTCVTLVKTLMDTG--- 292
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLS------SNENGDVVLQIVEP------DHGEASRASGVVPMVAALLVAELLKDMeyr 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569   293 -KWVNVFApivpVASTHKVLSTGsggtksGSLQQIQAEFQVISPLVPkRKVTFIRYCKEIRQGLWVVVD--VTPTQNPTL 369
Cdd:pfam01852  70 aQWDKDVR----SAETLEVISSG------GDLQYYVAALVAPSPLSP-RDFVFLRYWRRLGGGVYVIVDrsVTHPQFPPS 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569   370 LPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCES 436
Cdd:pfam01852 139 SGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
216-436 8.45e-53

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 180.71  E-value: 8.45e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569    216 LAITALRELITLGEVDCPFWMIDPivrskgVSKIYEKYRSSFNNVTKPpgqiVEASRAKGLVPMTCVTLVKTLMDTG--- 292
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSS------ENENGDEVRSIFSPGRKP----GEAFRLVGVVPMVCADLVEELMDDLeyr 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569    293 -KWVNVFApivpVASTHKVLSTGsggtksGSLQQIQAEFQViSPLVPkRKVTFIRYCKEIRQGLWVVVDVTPTQ--NPTL 369
Cdd:smart00234  71 pEWDKNVA----KAETLEVIDNG------TVIYHYVSKFAA-GPVSP-RDFVFVRYWREDEDGSYAVVDVSVTHptSPPE 138
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569    370 LPYGCSKRLPSGLIIDDLSNGYSQVTWIEQAEYNESHIHQLYQPLIGYGIGLGAKRWLATLQRHCES 436
Cdd:smart00234 139 SGYVRAENLPSGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
Homeodomain pfam00046
Homeodomain;
40-96 1.87e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 76.38  E-value: 1.87e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18416569    40 RMRRTHrrTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEK 96
Cdd:pfam00046   2 RKRTTF--TPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWK 56
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
42-99 2.27e-16

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 73.43  E-value: 2.27e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18416569  42 RRTHRRTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEKINN 99
Cdd:cd00086   2 RKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
39-92 2.56e-15

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 70.36  E-value: 2.56e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18416569     39 GRMRRThRRTAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKR 92
Cdd:smart00389   1 KRRKRT-SFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRR 53
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
25-138 9.55e-10

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 57.83  E-value: 9.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569  25 DMINDMSGVNDQDGGRMRRTHRR--TAYQTQELENFYMENPHPTEEQRYELGQRLNMGVNQVKNWFQNKRNLEKINNDHL 102
Cdd:COG5576  34 AADSEMKLERKQDGSSPPKSKRRrtTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGK 113
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18416569 103 ENVTLREEHDRllatqdqLRSAMLRSLCNICGKATN 138
Cdd:COG5576 114 VEQRPGEEEAD-------LAKIGSLSTGQISIIETL 142
Homeobox_KN pfam05920
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ...
55-92 9.24e-06

Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.


Pssm-ID: 428673  Cd Length: 39  Bit Score: 42.89  E-value: 9.24e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 18416569    55 LENFYmeNPHPTEEQRYELGQRLNMGVNQVKNWFQNKR 92
Cdd:pfam05920   2 YEHLH--NPYPSEEEKAELAKETGLSRKQISNWFINAR 37
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
479-632 7.44e-03

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 38.09  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 479 SVDKWQKIQVENvaqNMSFMIRKNVNEPGELTGIVLSastsvwLPVNQHTLFAFISHLSFRHEWdiltnDTTMEETIRIQ 558
Cdd:cd00177  13 EPEGWKLVKEKD---GVKIYTKPYEDSGLKLLKAEGV------IPASPEQVFELLMDIDLRKKW-----DKNFEEFEVIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416569 559 KAKRHGNIIslLKIVNNGMLV--------LQEIWNDASGAMVVYAPVETNSIELVK---RGENsdsvkfLPSGFSIVPDG 627
Cdd:cd00177  79 EIDEHTDII--YYKTKPPWPVsprdfvylRRRRKLDDGTYVIVSKSVDHDSHPKEKgyvRAEI------KLSGWIIEPLD 150

                ....*
gi 18416569 628 VNGSY 632
Cdd:cd00177 151 PGKTK 155
 
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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