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Conserved domains on  [gi|922367679|ref|XP_013456006|]
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homeobox-leucine zipper protein REVOLUTA [Medicago truncatula]

Protein Classification

START_ArGLABRA2_like and MEKHLA domain-containing protein( domain architecture ID 11078723)

protein containing domains homeodomain, bZIP, START_ArGLABRA2_like, and MEKHLA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 701-845 2.20e-69

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: 225.47  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  701 VTLAQWICQSYSYYLGTDLLRSDSLVGDLMLKQLWHHQDAILCCSLKSQPVFVFANQAGLDMLETTLVALQDITLDKIFD 780
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGESPDELAKALFHAPFAVLSHGTKADPIFNYANQAALDLWETTWEELTDLPSRLSAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922367679  781 ESGRKALCADFAKLMQQGFAYLPAGICMSTMGRHVSYEQAIAWKVLTpEDNTVHCLAFSFINWSF 845
Cdd:pfam08670  81 PDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLD-EDGNYHGQAAMFSNWSF 144
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
 161-377 5.56e-69

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: 227.92  E-value: 5.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 161 PAGLLSIAEETLTEFLSKATGTAVDWVQMPGMKP---GPDSVGIFAIS------QSCSGVAARACGLVSLEPTKIAEILK 231
Cdd:cd08875    1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRhggskpGGFTTEASRACGLVMMNAIKLVEILM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 232 DRLSWFR----ECRNLEVFTMFPAGN----GGTIELIYTQTYAPTTLAPARDFWTLRYTTTLDNGSLVVCERSLSGSGTG 303
Cdd:cd08875   81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGVQTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922367679 304 PNPtaaAQFVRAEMLPSGYLIRPCDGGGSIIHIVDHLNLEPWsvPEVLRPLYESPKVVAQKMTIAALRYIRQIA 377
Cdd:cd08875  161 PPP---ASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
Homeodomain pfam00046
Homeodomain;
28-86 6.97e-18

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.93  E-value: 6.97e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922367679   28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQ 86
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQL----GLTERQVKVWFQNRRAKWKR 57
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 80-119 3.15e-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: 44.84  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 922367679  80 RRCREKQRKEASRLQTVNRKLSAMNKLLMEENDRLQKQVS 119
Cdd:cd14686   13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
 
Name Accession Description Interval E-value
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 701-845 2.20e-69

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: 225.47  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  701 VTLAQWICQSYSYYLGTDLLRSDSLVGDLMLKQLWHHQDAILCCSLKSQPVFVFANQAGLDMLETTLVALQDITLDKIFD 780
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGESPDELAKALFHAPFAVLSHGTKADPIFNYANQAALDLWETTWEELTDLPSRLSAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922367679  781 ESGRKALCADFAKLMQQGFAYLPAGICMSTMGRHVSYEQAIAWKVLTpEDNTVHCLAFSFINWSF 845
Cdd:pfam08670  81 PDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLD-EDGNYHGQAAMFSNWSF 144
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
 161-377 5.56e-69

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: 227.92  E-value: 5.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 161 PAGLLSIAEETLTEFLSKATGTAVDWVQMPGMKP---GPDSVGIFAIS------QSCSGVAARACGLVSLEPTKIAEILK 231
Cdd:cd08875    1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRhggskpGGFTTEASRACGLVMMNAIKLVEILM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 232 DRLSWFR----ECRNLEVFTMFPAGN----GGTIELIYTQTYAPTTLAPARDFWTLRYTTTLDNGSLVVCERSLSGSGTG 303
Cdd:cd08875   81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGVQTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922367679 304 PNPtaaAQFVRAEMLPSGYLIRPCDGGGSIIHIVDHLNLEPWsvPEVLRPLYESPKVVAQKMTIAALRYIRQIA 377
Cdd:cd08875  161 PPP---ASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
START pfam01852
START domain;
166-376 6.51e-47

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 166.04  E-value: 6.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  166 SIAEETLTEFLSKATGTAVDWVQMPGMKPGPDSVGIFAIsqsCSGVAARACGLVSLEPTKI-AEILKD---RLSW---FR 238
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEP---DHGEASRASGVVPMVAALLvAELLKDmeyRAQWdkdVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  239 ECRNLEVFTmfpagNGGTIELIYTQTYAPTTLAPaRDFWTLRYTTTLDNGSLVVCERSLSgSGTGPNPtaaAQFVRAEML 318
Cdd:pfam01852  78 SAETLEVIS-----SGGDLQYYVAALVAPSPLSP-RDFVFLRYWRRLGGGVYVIVDRSVT-HPQFPPS---SGYVRAERL 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 922367679  319 PSGYLIRPCDGGGSIIHIVDHLNLEPWSVPEVLRPLYESPKVVAQKMTIAALRYIRQI 376
Cdd:pfam01852 148 PSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 167-372 2.80e-35

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 132.94  E-value: 2.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679   167 IAEETLTEFLSKATGTAVDWVQMPGMKPGPDSVGIFAISQSCsGVAARACGLVSLE-PTKIAEILKD---RLSW---FRE 239
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRKP-GEAFRLVGVVPMVcADLVEELMDDleyRPEWdknVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679   240 CRNLEVFTmfpagNGGTIELIYTQTYAptTLAPARDFWTLRYTTTLDNGSLVVCERSLsgsgTGPNPTAAAQFVRAEMLP 319
Cdd:smart00234  80 AETLEVID-----NGTVIYHYVSKFAA--GPVSPRDFVFVRYWREDEDGSYAVVDVSV----THPTSPPESGYVRAENLP 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 922367679   320 SGYLIRPCDGGGSIIHIVDHLNLEPWSVPEVLRPLYESPKVVAQKMTIAALRY 372
Cdd:smart00234 149 SGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
Homeodomain pfam00046
Homeodomain;
28-86 6.97e-18

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.93  E-value: 6.97e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922367679   28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQ 86
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQL----GLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 28-88 1.18e-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: 74.59  E-value: 1.18e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922367679  28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQRK 88
Cdd:cd00086    3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKEL----GLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 28-85 2.16e-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: 73.82  E-value: 2.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 922367679    28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREK 85
Cdd:smart00389   4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKL----GLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
24-113 4.35e-13

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 67.85  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  24 LDSGKYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREK-----------QRKEASR 92
Cdd:COG5576   50 PPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLL----NMPPKSVQIWFQNKRAKEKkkrsgkveqrpGEEEADL 125

                         90       100
                 ....*....|....*....|.
gi 922367679  93 LQTVNRKLSAMNKLLMEENDR 113
Cdd:COG5576  126 AKIGSLSTGQISIIETLEFSR 146
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 80-119 3.15e-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: 44.84  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 922367679  80 RRCREKQRKEASRLQTVNRKLSAMNKLLMEENDRLQKQVS 119
Cdd:cd14686   13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
BRLZ smart00338
basic region leucin zipper;
80-133 7.47e-05

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 41.40  E-value: 7.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 922367679    80 RRCREKQRKEASRLQT-VNRklsamnklLMEENDRLQKQVSQLVCENGFMRQQLH 133
Cdd:smart00338  18 RRSRERKKAEIEELERkVEQ--------LEAENERLKKEIERLRRELEKLKSELE 64
bZIP_2 pfam07716
Basic region leucine zipper;
80-124 3.59e-03

Basic region leucine zipper;


Pssm-ID: 462244 [Multi-domain]  Cd Length: 51  Bit Score: 36.04  E-value: 3.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 922367679   80 RRCREKQR-KEASRLQTVNRklsamnklLMEENDRLQKQVSQLVCE 124
Cdd:pfam07716  14 KRSREKKKqKEEELEERVKE--------LERENAQLRQKVEQLEKE 51
 
Name Accession Description Interval E-value
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 701-845 2.20e-69

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: 225.47  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  701 VTLAQWICQSYSYYLGTDLLRSDSLVGDLMLKQLWHHQDAILCCSLKSQPVFVFANQAGLDMLETTLVALQDITLDKIFD 780
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGESPDELAKALFHAPFAVLSHGTKADPIFNYANQAALDLWETTWEELTDLPSRLSAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922367679  781 ESGRKALCADFAKLMQQGFAYLPAGICMSTMGRHVSYEQAIAWKVLTpEDNTVHCLAFSFINWSF 845
Cdd:pfam08670  81 PDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLD-EDGNYHGQAAMFSNWSF 144
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
 161-377 5.56e-69

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: 227.92  E-value: 5.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 161 PAGLLSIAEETLTEFLSKATGTAVDWVQMPGMKP---GPDSVGIFAIS------QSCSGVAARACGLVSLEPTKIAEILK 231
Cdd:cd08875    1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRhggskpGGFTTEASRACGLVMMNAIKLVEILM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 232 DRLSWFR----ECRNLEVFTMFPAGN----GGTIELIYTQTYAPTTLAPARDFWTLRYTTTLDNGSLVVCERSLSGSGTG 303
Cdd:cd08875   81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGVQTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922367679 304 PNPtaaAQFVRAEMLPSGYLIRPCDGGGSIIHIVDHLNLEPWsvPEVLRPLYESPKVVAQKMTIAALRYIRQIA 377
Cdd:cd08875  161 PPP---ASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
START pfam01852
START domain;
166-376 6.51e-47

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 166.04  E-value: 6.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  166 SIAEETLTEFLSKATGTAVDWVQMPGMKPGPDSVGIFAIsqsCSGVAARACGLVSLEPTKI-AEILKD---RLSW---FR 238
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEP---DHGEASRASGVVPMVAALLvAELLKDmeyRAQWdkdVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  239 ECRNLEVFTmfpagNGGTIELIYTQTYAPTTLAPaRDFWTLRYTTTLDNGSLVVCERSLSgSGTGPNPtaaAQFVRAEML 318
Cdd:pfam01852  78 SAETLEVIS-----SGGDLQYYVAALVAPSPLSP-RDFVFLRYWRRLGGGVYVIVDRSVT-HPQFPPS---SGYVRAERL 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 922367679  319 PSGYLIRPCDGGGSIIHIVDHLNLEPWSVPEVLRPLYESPKVVAQKMTIAALRYIRQI 376
Cdd:pfam01852 148 PSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 167-372 2.80e-35

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 132.94  E-value: 2.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679   167 IAEETLTEFLSKATGTAVDWVQMPGMKPGPDSVGIFAISQSCsGVAARACGLVSLE-PTKIAEILKD---RLSW---FRE 239
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRKP-GEAFRLVGVVPMVcADLVEELMDDleyRPEWdknVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679   240 CRNLEVFTmfpagNGGTIELIYTQTYAptTLAPARDFWTLRYTTTLDNGSLVVCERSLsgsgTGPNPTAAAQFVRAEMLP 319
Cdd:smart00234  80 AETLEVID-----NGTVIYHYVSKFAA--GPVSPRDFVFVRYWREDEDGSYAVVDVSV----THPTSPPESGYVRAENLP 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 922367679   320 SGYLIRPCDGGGSIIHIVDHLNLEPWSVPEVLRPLYESPKVVAQKMTIAALRY 372
Cdd:smart00234 149 SGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
Homeodomain pfam00046
Homeodomain;
28-86 6.97e-18

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.93  E-value: 6.97e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922367679   28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQ 86
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQL----GLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 28-88 1.18e-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: 74.59  E-value: 1.18e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922367679  28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQRK 88
Cdd:cd00086    3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKEL----GLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 28-85 2.16e-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: 73.82  E-value: 2.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 922367679    28 KYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREK 85
Cdd:smart00389   4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKL----GLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
24-113 4.35e-13

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 67.85  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679  24 LDSGKYVRYTSEQVEALERVYAECPKPSSMRRQQLIRECpilsNIEPKQIKVWFQNRRCREK-----------QRKEASR 92
Cdd:COG5576   50 PPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLL----NMPPKSVQIWFQNKRAKEKkkrsgkveqrpGEEEADL 125

                         90       100
                 ....*....|....*....|.
gi 922367679  93 LQTVNRKLSAMNKLLMEENDR 113
Cdd:COG5576  126 AKIGSLSTGQISIIETLEFSR 146
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 204-378 4.34e-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: 65.82  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 204 ISQSCSGVAARACGLVSLEPTKIAEILKD---RLSW---FRECRNLEVFTmfpagngGTIELIYTQTYAPTTLAPaRDFW 277
Cdd:cd00177   32 PYEDSGLKLLKAEGVIPASPEQVFELLMDidlRKKWdknFEEFEVIEEID-------EHTDIIYYKTKPPWPVSP-RDFV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922367679 278 TLRYTTTLDNGSLVVCERSLSGSGTGPNPtaaaQFVRAEMLPSGYLIRPCDGGGSIIHIVDHLNLEPWSVPEVLrplyes 357
Cdd:cd00177  104 YLRRRRKLDDGTYVIVSKSVDHDSHPKEK----GYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPKGSIPKSLV------ 173

                        170       180
                 ....*....|....*....|.
gi 922367679 358 pKVVAQKMTIAALRYIRQIAQ 378
Cdd:cd00177  174 -NSAAKKQLASFLKDLRKAKK 193
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 80-119 3.15e-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: 44.84  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 922367679  80 RRCREKQRKEASRLQTVNRKLSAMNKLLMEENDRLQKQVS 119
Cdd:cd14686   13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
BRLZ smart00338
basic region leucin zipper;
80-133 7.47e-05

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 41.40  E-value: 7.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 922367679    80 RRCREKQRKEASRLQT-VNRklsamnklLMEENDRLQKQVSQLVCENGFMRQQLH 133
Cdd:smart00338  18 RRSRERKKAEIEELERkVEQ--------LEAENERLKKEIERLRRELEKLKSELE 64
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
 78-121 1.49e-04

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: 40.64  E-value: 1.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 922367679  78 QNR----RCREKQRKEASRLQTVNRKLSAMNKLLMEENDRLQKQVSQL 121
Cdd:cd14692    9 QNKnaatRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREINYL 56
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 79-121 2.08e-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: 39.82  E-value: 2.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 922367679  79 NR----RCREKQRKEASRLQTVNRKLSAMNKLLMEENDRLQKQVSQL 121
Cdd:cd14687    9 NRiaasKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDL 55
bZIP_CEBP cd14693
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ...
 80-121 2.80e-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: 39.46  E-value: 2.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 922367679  80 RRCREKQRKEAsrlQTVNRKLsamnKLLMEENDRLQKQVSQL 121
Cdd:cd14693   17 RKSREKAKQRQ---LETQQKV----QELRKENERLQKRVELL 51
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 272-336 1.81e-03

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: 40.37  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922367679 272 PARDFWTLR-YTTTLDNGSLVVCERSLSGSGTGPNPTaaaqfVRAEMLPSGYLIRPCDGGGS-IIHI 336
Cdd:cd08869  101 PTRDYVVLRtWRTDLPKGACVLVETSVEHTEPVPLGG-----VRAVVLASRYLIEPCGSGKSrVTHI 162
bZIP_2 pfam07716
Basic region leucine zipper;
80-124 3.59e-03

Basic region leucine zipper;


Pssm-ID: 462244 [Multi-domain]  Cd Length: 51  Bit Score: 36.04  E-value: 3.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 922367679   80 RRCREKQR-KEASRLQTVNRklsamnklLMEENDRLQKQVSQLVCE 124
Cdd:pfam07716  14 KRSREKKKqKEEELEERVKE--------LERENAQLRQKVEQLEKE 51
 
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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