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Conserved domains on  [gi|15220758|ref|NP_174337|]
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Homeobox-leucine zipper family protein / lipid-binding START domain-containing protein [Arabidopsis thaliana]

Protein Classification

homeobox-leucine zipper protein( domain architecture ID 11078723)

homeobox-leucine zipper protein containing a lipid-binding START domain and a C-terminal MEKHLA domain; belongs to the HD-ZIP homeobox family of transcription factors

CATH:  3.30.530.20
Gene Ontology:  GO:0003700|GO:0003677|GO:0008289
PubMed:  16805899|10322415|10881186|12770731|34440430|26464018|18922149|1357790
SCOP:  3000738|4000291

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 ...
 164-380 7.31e-70

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: 230.24  E-value: 7.31e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 164 PANLLSIAEETLAEFLCKATGTAVDWVQMIGMKP---GPDSIGIVAVSRN------CSGIAARACGLVSLEPMKVAEILK 234
Cdd:cd08875   1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRHGgskpggFTTEASRACGLVMMNAIKLVEILM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 235 DRPSWFR----DCRCVETLNVIPTGN----GGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLtsaTGG 306
Cdd:cd08875  81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSI---DGV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220758 307 PNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSsvPEVLRPLYESSKILAQKMTVAALRHVRQIA 380
Cdd:cd08875 158 QTAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 693-840 8.18e-67

MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins.


:

Pssm-ID: 462555 [Multi-domain]  Cd Length: 144  Bit Score: 218.54  E-value: 8.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   693 LTLVRWITRSYSIHTGADLFGADSQScgGDTLLKQLWDHSDAILCCSLKtnASPVFTFANQAGLDMLETTLVALQDIMLD 772
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGES--PDELAKALFHAPFAVLSHGTK--ADPIFNYANQAALDLWETTWEELTDLPSR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220758   773 KTLDDSGRRALCSEFAKIMQQGYANLPAGICVSSMGRPVSYEQATVWKVVDDNESNHCLAFTLVSWSF 840
Cdd:pfam08670  77 LSAEPDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLDEDGNYHGQAAMFSNWSF 144
Homeodomain pfam00046
Homeodomain;
21-79 1.08e-18

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 80.24  E-value: 1.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15220758    21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIREcpilCNIEPRQIKVWFQNRRCREKQ 79
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQ----LGLTERQVKVWFQNRRAKWKR 57
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 73-112 4.33e-06

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


:

Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 44.46  E-value: 4.33e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15220758  73 RRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVS 112
Cdd:cd14686  13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
 
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 ...
 164-380 7.31e-70

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: 230.24  E-value: 7.31e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 164 PANLLSIAEETLAEFLCKATGTAVDWVQMIGMKP---GPDSIGIVAVSRN------CSGIAARACGLVSLEPMKVAEILK 234
Cdd:cd08875   1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRHGgskpggFTTEASRACGLVMMNAIKLVEILM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 235 DRPSWFR----DCRCVETLNVIPTGN----GGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLtsaTGG 306
Cdd:cd08875  81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSI---DGV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220758 307 PNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSsvPEVLRPLYESSKILAQKMTVAALRHVRQIA 380
Cdd:cd08875 158 QTAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 693-840 8.18e-67

MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins.


Pssm-ID: 462555 [Multi-domain]  Cd Length: 144  Bit Score: 218.54  E-value: 8.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   693 LTLVRWITRSYSIHTGADLFGADSQScgGDTLLKQLWDHSDAILCCSLKtnASPVFTFANQAGLDMLETTLVALQDIMLD 772
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGES--PDELAKALFHAPFAVLSHGTK--ADPIFNYANQAALDLWETTWEELTDLPSR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220758   773 KTLDDSGRRALCSEFAKIMQQGYANLPAGICVSSMGRPVSYEQATVWKVVDDNESNHCLAFTLVSWSF 840
Cdd:pfam08670  77 LSAEPDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLDEDGNYHGQAAMFSNWSF 144
START pfam01852
START domain;
169-379 2.93e-54

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 186.45  E-value: 2.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   169 SIAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAvsrNCSGIAARACGLVSLEPMK-VAEILKD---RPSWFRDCR 244
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVE---PDHGEASRASGVVPMVAALlVAELLKDmeyRAQWDKDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   245 CVETLNVIPTGngGTIELVNTQIYAPTTLAAaRDFWTLRYSTSLEDGSYVVCERSLTSATGGPngplSSSFVRAKMLSSG 324
Cdd:pfam01852  78 SAETLEVISSG--GDLQYYVAALVAPSPLSP-RDFVFLRYWRRLGGGVYVIVDRSVTHPQFPP----SSGYVRAERLPSG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15220758   325 FLIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQI 379
Cdd:pfam01852 151 YLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 170-378 8.60e-44

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 157.21  E-value: 8.60e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758    170 IAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAVSRNCsGIAARACGLVSLEPMK-VAEILKD---RPSWFRDCRC 245
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRKP-GEAFRLVGVVPMVCADlVEELMDDleyRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758    246 VETLNVIPtgNGGTIELVNTQIYAptTLAAARDFWTLRYSTSLEDGSYVVCERSLTSatggPNGPLSSSFVRAKMLSSGF 325
Cdd:smart00234  80 AETLEVID--NGTVIYHYVSKFAA--GPVSPRDFVFVRYWREDEDGSYAVVDVSVTH----PTSPPESGYVRAENLPSGL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15220758    326 LIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQ 378
Cdd:smart00234 152 LIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCA 204
Homeodomain pfam00046
Homeodomain;
21-79 1.08e-18

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 80.24  E-value: 1.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15220758    21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIREcpilCNIEPRQIKVWFQNRRCREKQ 79
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQ----LGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 21-81 4.78e-17

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: 75.74  E-value: 4.78e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220758  21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECpilcNIEPRQIKVWFQNRRCREKQRK 81
Cdd:cd00086   3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKEL----GLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 21-78 1.16e-16

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: 74.59  E-value: 1.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220758     21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECpilcNIEPRQIKVWFQNRRCREK 78
Cdd:smart00389   4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKL----GLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
2-106 5.49e-15

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 73.24  E-value: 5.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   2 MAHHSMD---------DRDSPDKGfdsgKYVRYTPEQVEALERVYAECPKPSSLRRQQLIrecpILCNIEPRQIKVWFQN 72
Cdd:COG5576  30 REVEAADsemklerkqDGSSPPKS----KRRRTTDEQLMVLEREFEINPYPSSITRIKLS----LLLNMPPKSVQIWFQN 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15220758  73 RRCREK----------QRKESARL-QTVNRKLSAMNKLLMEENDR 106
Cdd:COG5576 102 KRAKEKkkrsgkveqrPGEEEADLaKIGSLSTGQISIIETLEFSR 146
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 73-112 4.33e-06

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 44.46  E-value: 4.33e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15220758  73 RRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVS 112
Cdd:cd14686  13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
BRLZ smart00338
basic region leucin zipper;
73-118 1.45e-04

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 40.63  E-value: 1.45e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15220758     73 RRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNLVYEN 118
Cdd:smart00338  18 RRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSEL 63
PLN00188 PLN00188
enhanced disease resistance protein (EDR2); Provisional
 277-329 5.95e-03

enhanced disease resistance protein (EDR2); Provisional


Pssm-ID: 215094 [Multi-domain]  Cd Length: 719  Bit Score: 40.18  E-value: 5.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15220758  277 RDFWTLRYSTSLEDGSYVVCERSLTSATGGPNgplsSSFVRAKMLSSGFLIRP 329
Cdd:PLN00188 292 RDLCYVRYWRRNDDGSYVVLFRSREHENCGPQ----PGFVRAHLESGGFNISP 340
 
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 ...
 164-380 7.31e-70

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: 230.24  E-value: 7.31e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 164 PANLLSIAEETLAEFLCKATGTAVDWVQMIGMKP---GPDSIGIVAVSRN------CSGIAARACGLVSLEPMKVAEILK 234
Cdd:cd08875   1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRHGgskpggFTTEASRACGLVMMNAIKLVEILM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 235 DRPSWFR----DCRCVETLNVIPTGN----GGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLtsaTGG 306
Cdd:cd08875  81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSI---DGV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220758 307 PNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSsvPEVLRPLYESSKILAQKMTVAALRHVRQIA 380
Cdd:cd08875 158 QTAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 693-840 8.18e-67

MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins.


Pssm-ID: 462555 [Multi-domain]  Cd Length: 144  Bit Score: 218.54  E-value: 8.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   693 LTLVRWITRSYSIHTGADLFGADSQScgGDTLLKQLWDHSDAILCCSLKtnASPVFTFANQAGLDMLETTLVALQDIMLD 772
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGES--PDELAKALFHAPFAVLSHGTK--ADPIFNYANQAALDLWETTWEELTDLPSR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220758   773 KTLDDSGRRALCSEFAKIMQQGYANLPAGICVSSMGRPVSYEQATVWKVVDDNESNHCLAFTLVSWSF 840
Cdd:pfam08670  77 LSAEPDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLDEDGNYHGQAAMFSNWSF 144
START pfam01852
START domain;
169-379 2.93e-54

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 186.45  E-value: 2.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   169 SIAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAvsrNCSGIAARACGLVSLEPMK-VAEILKD---RPSWFRDCR 244
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVE---PDHGEASRASGVVPMVAALlVAELLKDmeyRAQWDKDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   245 CVETLNVIPTGngGTIELVNTQIYAPTTLAAaRDFWTLRYSTSLEDGSYVVCERSLTSATGGPngplSSSFVRAKMLSSG 324
Cdd:pfam01852  78 SAETLEVISSG--GDLQYYVAALVAPSPLSP-RDFVFLRYWRRLGGGVYVIVDRSVTHPQFPP----SSGYVRAERLPSG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15220758   325 FLIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQI 379
Cdd:pfam01852 151 YLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 170-378 8.60e-44

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 157.21  E-value: 8.60e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758    170 IAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAVSRNCsGIAARACGLVSLEPMK-VAEILKD---RPSWFRDCRC 245
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRKP-GEAFRLVGVVPMVCADlVEELMDDleyRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758    246 VETLNVIPtgNGGTIELVNTQIYAptTLAAARDFWTLRYSTSLEDGSYVVCERSLTSatggPNGPLSSSFVRAKMLSSGF 325
Cdd:smart00234  80 AETLEVID--NGTVIYHYVSKFAA--GPVSPRDFVFVRYWREDEDGSYAVVDVSVTH----PTSPPESGYVRAENLPSGL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15220758    326 LIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQ 378
Cdd:smart00234 152 LIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCA 204
Homeodomain pfam00046
Homeodomain;
21-79 1.08e-18

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 80.24  E-value: 1.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15220758    21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIREcpilCNIEPRQIKVWFQNRRCREKQ 79
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQ----LGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 21-81 4.78e-17

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: 75.74  E-value: 4.78e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220758  21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECpilcNIEPRQIKVWFQNRRCREKQRK 81
Cdd:cd00086   3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKEL----GLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 21-78 1.16e-16

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: 74.59  E-value: 1.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220758     21 KYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECpilcNIEPRQIKVWFQNRRCREK 78
Cdd:smart00389   4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKL----GLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
2-106 5.49e-15

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 73.24  E-value: 5.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758   2 MAHHSMD---------DRDSPDKGfdsgKYVRYTPEQVEALERVYAECPKPSSLRRQQLIrecpILCNIEPRQIKVWFQN 72
Cdd:COG5576  30 REVEAADsemklerkqDGSSPPKS----KRRRTTDEQLMVLEREFEINPYPSSITRIKLS----LLLNMPPKSVQIWFQN 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15220758  73 RRCREK----------QRKESARL-QTVNRKLSAMNKLLMEENDR 106
Cdd:COG5576 102 KRAKEKkkrsgkveqrPGEEEADLaKIGSLSTGQISIIETLEFSR 146
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 228-354 7.71e-12

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: 65.05  E-value: 7.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 228 KVAEILKD---RPSWfrdCRCVETLNVIPTgNGGTIELVNTQIYAPTtLAAARDFWTLRYSTSLEDGSYVVCERSLTSat 304
Cdd:cd00177  53 QVFELLMDidlRKKW---DKNFEEFEVIEE-IDEHTDIIYYKTKPPW-PVSPRDFVYLRRRRKLDDGTYVIVSKSVDH-- 125

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15220758 305 ggPNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSSVPEVL 354
Cdd:cd00177 126 --DSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPKGSIPKSLV 173
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 73-112 4.33e-06

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 44.46  E-value: 4.33e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15220758  73 RRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVS 112
Cdd:cd14686  13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 232-345 1.13e-04

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). 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. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 43.84  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 232 ILKDRPSWFRDC---RCVETLNViptgnggtielvNTQIYAPTTLAAA----RDFWTLR-YSTSLEDGSYVVCERSLTSA 303
Cdd:cd08869  63 ILRERHLWDDDLlqwKVVETLDE------------DTEVYQYVTNSMAphptRDYVVLRtWRTDLPKGACVLVETSVEHT 130

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15220758 304 TggpNGPLSSsfVRAKMLSSGFLIRPCDGGGSIIHIVDHVDL 345
Cdd:cd08869 131 E---PVPLGG--VRAVVLASRYLIEPCGSGKSRVTHICRVDL 167
BRLZ smart00338
basic region leucin zipper;
73-118 1.45e-04

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 40.63  E-value: 1.45e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15220758     73 RRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNLVYEN 118
Cdd:smart00338  18 RRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSEL 63
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 72-114 5.63e-04

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269835 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 5.63e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15220758  72 NR----RCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNL 114
Cdd:cd14687   9 NRiaasKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDL 55
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 196-344 8.12e-04

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). 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. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 41.86  E-value: 8.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 196 KPGPDSIGIVAVSRNCSGIAaracglvslePMKVAEILKD---RPSW---FRDCRCVETLNViptgnggtielvNTQI-- 267
Cdd:cd08871  40 NPENSSIKMIKVSAIFPDVP----------AETLYDVLHDpeyRKTWdsnMIESFDICQLNP------------NNDIgy 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220758 268 YA---PTTLAAaRDFWTLRySTSLEDGSYVVCERSLTSatggPNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVD 344
Cdd:cd08871  98 YSakcPKPLKN-RDFVNLR-SWLEFGGEYIIFNHSVKH----KKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVTQND 171
bZIP_CEBP cd14693
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ...
 73-117 9.53e-04

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar proteins: a DNA-binding and dimerization domain; CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269841 [Multi-domain]  Cd Length: 60  Bit Score: 37.92  E-value: 9.53e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15220758  73 RRCREKQRKESARLQTvnrKLsamnKLLMEENDRLQKQVSNLVYE 117
Cdd:cd14693  17 RKSREKAKQRQLETQQ---KV----QELRKENERLQKRVELLTKE 54
PLN00188 PLN00188
enhanced disease resistance protein (EDR2); Provisional
 277-329 5.95e-03

enhanced disease resistance protein (EDR2); Provisional


Pssm-ID: 215094 [Multi-domain]  Cd Length: 719  Bit Score: 40.18  E-value: 5.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15220758  277 RDFWTLRYSTSLEDGSYVVCERSLTSATGGPNgplsSSFVRAKMLSSGFLIRP 329
Cdd:PLN00188 292 RDLCYVRYWRRNDDGSYVVLFRSREHENCGPQ----PGFVRAHLESGGFNISP 340
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
 71-114 9.86e-03

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269840 [Multi-domain]  Cd Length: 63  Bit Score: 35.24  E-value: 9.86e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15220758  71 QNR----RCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNL 114
Cdd:cd14692   9 QNKnaatRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREINYL 56
 
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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