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Conserved domains on  [gi|729357759|ref|XP_010545672|]
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PREDICTED: homeobox-leucine zipper protein ATHB-15 isoform X1 [Tarenaya hassleriana]

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
START_ArGLABRA2_like cd08875
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
 155-371 6.17e-74

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: 241.02  E-value: 6.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 155 PAGLLSIAEETLAEFLSKATGTAVEWVQMPGMKP---GPDSIGIIAISH------GCTGVAARACGLVGLEPTRVAEIVK 225
Cdd:cd08875    1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRHggskpgGFTTEASRACGLVMMNAIKLVEILM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 226 DRSSWFR----ECRAVDVLNVLPTTN----GGTIELLYMQLYAPTTLAPPRDFWLLRYTSVLEDGSLVVCERSLKNTQsg 297
Cdd:cd08875   81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGVQ-- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 729357759 298 pNMPPVQHFVRAEMLPSGYLIRPCEGGGSIIHIVDHMDLEASsvPEVLRPLYESPKVLAQKTTMASLRQLKQIA 371
Cdd:cd08875  159 -TAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 696-838 2.02e-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: 220.08  E-value: 2.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  696 QTLARWICHSYRCFMGVELLKSSDGN-ESILKNLWNHSDAIMCCSLKALPVFTFANQAGLDMLETTLVALQDISLEKIFD 774
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGESpDELAKALFHAPFAVLSHGTKADPIFNYANQAALDLWETTWEELTDLPSRLSAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 729357759  775 DNGRKTLCSEFPQIMQQGFACLRGGICLSSMGRPVSYDKAVAWKVLNEEENAHCICFVFINWSF 838
Cdd:pfam08670  81 PDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLDEDGNYHGQAAMFSNWSF 144
Homeodomain pfam00046
Homeodomain;
17-75 1.76e-17

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 76.77  E-value: 1.76e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 729357759   17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQ 75
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQL----GLTERQVKVWFQNRRAKWKR 57
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 69-108 4.81e-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: 4.81e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 729357759  69 RRCREKQRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVS 108
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 ...
 155-371 6.17e-74

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: 241.02  E-value: 6.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 155 PAGLLSIAEETLAEFLSKATGTAVEWVQMPGMKP---GPDSIGIIAISH------GCTGVAARACGLVGLEPTRVAEIVK 225
Cdd:cd08875    1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRHggskpgGFTTEASRACGLVMMNAIKLVEILM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 226 DRSSWFR----ECRAVDVLNVLPTTN----GGTIELLYMQLYAPTTLAPPRDFWLLRYTSVLEDGSLVVCERSLKNTQsg 297
Cdd:cd08875   81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGVQ-- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 729357759 298 pNMPPVQHFVRAEMLPSGYLIRPCEGGGSIIHIVDHMDLEASsvPEVLRPLYESPKVLAQKTTMASLRQLKQIA 371
Cdd:cd08875  159 -TAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 696-838 2.02e-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: 220.08  E-value: 2.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  696 QTLARWICHSYRCFMGVELLKSSDGN-ESILKNLWNHSDAIMCCSLKALPVFTFANQAGLDMLETTLVALQDISLEKIFD 774
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGESpDELAKALFHAPFAVLSHGTKADPIFNYANQAALDLWETTWEELTDLPSRLSAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 729357759  775 DNGRKTLCSEFPQIMQQGFACLRGGICLSSMGRPVSYDKAVAWKVLNEEENAHCICFVFINWSF 838
Cdd:pfam08670  81 PDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLDEDGNYHGQAAMFSNWSF 144
START pfam01852
START domain;
160-370 3.03e-54

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 186.45  E-value: 3.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  160 SIAEETLAEFLSKATGTAVEWVQMPGMKPGPDSIGIIAISHGctgVAARACGLVGLEP-TRVAEIVKD---RSSWFRECR 235
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHG---EASRASGVVPMVAaLLVAELLKDmeyRAQWDKDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  236 AVDVLNVLPTtnGGTIELLYMQLYAPTTLaPPRDFWLLRYTSVLEDGSLVVCERSLKNTQsgpnMPPVQHFVRAEMLPSG 315
Cdd:pfam01852  78 SAETLEVISS--GGDLQYYVAALVAPSPL-SPRDFVFLRYWRRLGGGVYVIVDRSVTHPQ----FPPSSGYVRAERLPSG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 729357759  316 YLIRPCEGGGSIIHIVDHMDLEASSVPEVLRPLYESPKVLAQKTTMASLRQLKQI 370
Cdd:pfam01852 151 YLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 161-369 1.52e-37

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 139.49  E-value: 1.52e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759   161 IAEETLAEFLSKATGTAVEWVQMPGMKPGPDSIGIIAISHGCtGVAARACGLVGLEPTR-VAEIVKD---RSSWFRECRA 236
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRKP-GEAFRLVGVVPMVCADlVEELMDDleyRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759   237 VDVLNVLPttNGGTIelLYMQLYAPTTLAPPRDFWLLRYTSVLEDGSLVVCERSLKNTQSGPNMPpvqhFVRAEMLPSGY 316
Cdd:smart00234  80 AETLEVID--NGTVI--YHYVSKFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESG----YVRAENLPSGL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 729357759   317 LIRPCEGGGSIIHIVDHMDLEASSVPEVLRPLYESPKVLAQKTTMASLRQLKQ 369
Cdd:smart00234 152 LIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCA 204
Homeodomain pfam00046
Homeodomain;
17-75 1.76e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 76.77  E-value: 1.76e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 729357759   17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQ 75
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQL----GLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 17-77 1.09e-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: 1.09e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 729357759  17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQRK 77
Cdd:cd00086    3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKEL----GLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 17-74 1.68e-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: 74.21  E-value: 1.68e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 729357759    17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREK 74
Cdd:smart00389   4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKL----GLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1-112 5.86e-13

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 67.46  E-value: 5.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759   1 MEMSYKDGKAgSLDNGKYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREK------ 74
Cdd:COG5576   39 MKLERKQDGS-SPPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLL----NMPPKSVQIWFQNKRAKEKkkrsgk 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 729357759  75 -----QRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVSQLVY 112
Cdd:COG5576  114 veqrpGEEEADLAKIGSLSTGQISIIETLEFSRTSYEEGGLQY 156
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 69-108 4.81e-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: 4.81e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 729357759  69 RRCREKQRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVS 108
Cdd:cd14686   13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
BRLZ smart00338
basic region leucin zipper;
69-119 2.00e-04

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 40.24  E-value: 2.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 729357759    69 RRCREKQRKEASRLQS-VNRkmtamnklLMEENDRLQKQVSQLVYENSYFRQ 119
Cdd:smart00338  18 RRSRERKKAEIEELERkVEQ--------LEAENERLKKEIERLRRELEKLKS 61
 
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 ...
 155-371 6.17e-74

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: 241.02  E-value: 6.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 155 PAGLLSIAEETLAEFLSKATGTAVEWVQMPGMKP---GPDSIGIIAISH------GCTGVAARACGLVGLEPTRVAEIVK 225
Cdd:cd08875    1 KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPeilNPDEYERMFPRHggskpgGFTTEASRACGLVMMNAIKLVEILM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 226 DRSSWFR----ECRAVDVLNVLPTTN----GGTIELLYMQLYAPTTLAPPRDFWLLRYTSVLEDGSLVVCERSLKNTQsg 297
Cdd:cd08875   81 DVNKWSElfpgIVSKAKTLQVISTGNggnrNGTLQLMYAELQVPSPLVPTREFYFLRYCKQLEDGLWAVVDVSIDGVQ-- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 729357759 298 pNMPPVQHFVRAEMLPSGYLIRPCEGGGSIIHIVDHMDLEASsvPEVLRPLYESPKVLAQKTTMASLRQLKQIA 371
Cdd:cd08875  159 -TAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEK--PVHLLYRYLVSSGLAFGATRWVATLQRQCE 229
MEKHLA pfam08670
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ...
 696-838 2.02e-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: 220.08  E-value: 2.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  696 QTLARWICHSYRCFMGVELLKSSDGN-ESILKNLWNHSDAIMCCSLKALPVFTFANQAGLDMLETTLVALQDISLEKIFD 774
Cdd:pfam08670   1 LTLAQLLLQSYRRLTGRDLLPSDGESpDELAKALFHAPFAVLSHGTKADPIFNYANQAALDLWETTWEELTDLPSRLSAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 729357759  775 DNGRKTLCSEFPQIMQQGFACLRGGICLSSMGRPVSYDKAVAWKVLNEEENAHCICFVFINWSF 838
Cdd:pfam08670  81 PDERAERQALLAKVMQQGYIDLYSGIRISSTGRRFSIENAVVWNVLDEDGNYHGQAAMFSNWSF 144
START pfam01852
START domain;
160-370 3.03e-54

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 186.45  E-value: 3.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  160 SIAEETLAEFLSKATGTAVEWVQMPGMKPGPDSIGIIAISHGctgVAARACGLVGLEP-TRVAEIVKD---RSSWFRECR 235
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHG---EASRASGVVPMVAaLLVAELLKDmeyRAQWDKDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759  236 AVDVLNVLPTtnGGTIELLYMQLYAPTTLaPPRDFWLLRYTSVLEDGSLVVCERSLKNTQsgpnMPPVQHFVRAEMLPSG 315
Cdd:pfam01852  78 SAETLEVISS--GGDLQYYVAALVAPSPL-SPRDFVFLRYWRRLGGGVYVIVDRSVTHPQ----FPPSSGYVRAERLPSG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 729357759  316 YLIRPCEGGGSIIHIVDHMDLEASSVPEVLRPLYESPKVLAQKTTMASLRQLKQI 370
Cdd:pfam01852 151 YLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 161-369 1.52e-37

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 139.49  E-value: 1.52e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759   161 IAEETLAEFLSKATGTAVEWVQMPGMKPGPDSIGIIAISHGCtGVAARACGLVGLEPTR-VAEIVKD---RSSWFRECRA 236
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRKP-GEAFRLVGVVPMVCADlVEELMDDleyRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759   237 VDVLNVLPttNGGTIelLYMQLYAPTTLAPPRDFWLLRYTSVLEDGSLVVCERSLKNTQSGPNMPpvqhFVRAEMLPSGY 316
Cdd:smart00234  80 AETLEVID--NGTVI--YHYVSKFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESG----YVRAENLPSGL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 729357759   317 LIRPCEGGGSIIHIVDHMDLEASSVPEVLRPLYESPKVLAQKTTMASLRQLKQ 369
Cdd:smart00234 152 LIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCA 204
Homeodomain pfam00046
Homeodomain;
17-75 1.76e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 76.77  E-value: 1.76e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 729357759   17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQ 75
Cdd:pfam00046   3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQL----GLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 17-77 1.09e-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: 1.09e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 729357759  17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREKQRK 77
Cdd:cd00086    3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKEL----GLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 17-74 1.68e-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: 74.21  E-value: 1.68e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 729357759    17 KYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREK 74
Cdd:smart00389   4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKL----GLSERQVKVWFQNRRAKWK 57
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 198-336 1.35e-14

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: 73.14  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 198 ISHGCTGVAARACGLVGLEPTRVAEIVKD---RSSW---FRECRAVDvlnvlptTNGGTIELLYMQLYAPTtLAPPRDFW 271
Cdd:cd00177   32 PYEDSGLKLLKAEGVIPASPEQVFELLMDidlRKKWdknFEEFEVIE-------EIDEHTDIIYYKTKPPW-PVSPRDFV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 729357759 272 LLRYTSVLEDGSLVVCERSLKNtqsgPNMPPVQHFVRAEMLPSGYLIRPCEGGGSIIHIVDHMDL 336
Cdd:cd00177  104 YLRRRRKLDDGTYVIVSKSVDH----DSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDP 164
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1-112 5.86e-13

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 67.46  E-value: 5.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759   1 MEMSYKDGKAgSLDNGKYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECpilsNIEPKQIKVWFQNRRCREK------ 74
Cdd:COG5576   39 MKLERKQDGS-SPPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLL----NMPPKSVQIWFQNKRAKEKkkrsgk 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 729357759  75 -----QRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVSQLVY 112
Cdd:COG5576  114 veqrpGEEEADLAKIGSLSTGQISIIETLEFSRTSYEEGGLQY 156
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 69-108 4.81e-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: 4.81e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 729357759  69 RRCREKQRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVS 108
Cdd:cd14686   13 RRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 211-334 1.42e-05

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. 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. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 46.83  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 211 GLVGLEPTRVAEIVKDRSSWFRECRAVDVLNVLPTTNGgTIELLYMQLYAPT-TLAPPRDFWLLRYTSVLEDGSLVVCeR 289
Cdd:cd08874   51 GVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTE-DICLVYLVHETPLcLLKQPRDFCCLQVEAKEGELSVVAC-Q 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 729357759 290 SLKNTqsgpNMP-PVQHFVRAEMLPSGYLIRPCEGGGSIIHIVDHM 334
Cdd:cd08874  129 SVYDK----SMPePGRSLVRGEILPSAWILEPVTVEGNQYTRVIYI 170
bZIP_CEBP cd14693
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ...
 69-113 1.32e-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: 40.62  E-value: 1.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 729357759  69 RRCREKQRKEAsrlQSVNRKMtamnKLLMEENDRLQKQVSQLVYE 113
Cdd:cd14693   17 RKSREKAKQRQ---LETQQKV----QELRKENERLQKRVELLTKE 54
BRLZ smart00338
basic region leucin zipper;
69-119 2.00e-04

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 40.24  E-value: 2.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 729357759    69 RRCREKQRKEASRLQS-VNRkmtamnklLMEENDRLQKQVSQLVYENSYFRQ 119
Cdd:smart00338  18 RRSRERKKAEIEELERkVEQ--------LEAENERLKKEIERLRRELEKLKS 61
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 68-110 3.57e-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: 39.43  E-value: 3.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 729357759  68 NR----RCREKQRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVSQL 110
Cdd:cd14687    9 NRiaasKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDL 55
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 266-334 4.78e-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: 42.30  E-value: 4.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 729357759 266 PPRDFWLLRYTSV-LEDGSLVVCERSLKNTQsgpNMPPVQhfVRAEMLPSGYLIRPCEGGGS-IIHI--VDHM 334
Cdd:cd08869  101 PTRDYVVLRTWRTdLPKGACVLVETSVEHTE---PVPLGG--VRAVVLASRYLIEPCGSGKSrVTHIcrVDLR 168
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
 67-110 9.63e-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: 38.33  E-value: 9.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 729357759  67 QNR----RCREKQRKEASRLQSVNRKMTAMNKLLMEENDRLQKQVSQL 110
Cdd:cd14692    9 QNKnaatRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREINYL 56
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 208-320 1.35e-03

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). 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. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 40.80  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 208 RACGLVGLEPTRVAEIVKDR----SSWFRECRAVDVLNVLpttnGGTIELLYmQLYAPTT--LAPPRDFWLLRYTSVLED 281
Cdd:cd08868   51 RLTGVLDCPAEFLYNELVLNveslPSWNPTVLECKIIQVI----DDNTDISY-QVAAEAGggLVSPRDFVSLRHWGIREN 125

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 729357759 282 GSLVVCerslkNTQSGPNMPPVQHFVRAEMLPSGYLIRP 320
Cdd:cd08868  126 CYLSSG-----VSVEHPAMPPTKNYVRGENGPGCWILRP 159
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 255-335 3.54e-03

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: 39.93  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729357759 255 YMQLYAPTTLAPpRDFWLLRytSVLE-DGSLVVCERSLKNtqsgPNMPPVQHFVRAEMLPSGYLIRPCEGGGSIIHIVDH 333
Cdd:cd08871   97 YYSAKCPKPLKN-RDFVNLR--SWLEfGGEYIIFNHSVKH----KKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVTQ 169


                 ..
gi 729357759 334 MD 335
Cdd:cd08871  170 ND 171
 
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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