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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1773095124 163 RKQIAGLQKRIQDLETENMELKNKVQDLENQLR 195
Cdd:cd14686    20 KERIEELEEEVEELEEENEELKAELEELRAEVE 52

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124   27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhiKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAA---QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1773095124  107 DKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFL 153
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKL 129

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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1773095124 163 RKQIAGLQKRIQDLETENMELKNKVQDLENQLR 195
Cdd:cd14686    20 KERIEELEEEVEELEEENEELKAELEELRAEVE 52

basic region leucin zipper;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1773095124  163 RKQIAGLQKRIQDLETENMELKNKVQDLENQLR 195
Cdd:smart00338  25 KAEIEELERKVEQLEAENERLKKEIERLRRELE 57

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124   27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhiKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAA---QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1773095124  107 DKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFL 153
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKL 129

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  13 WMHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKfarhIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHN 92
Cdd:cd01274     3 WRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLICE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1773095124  93 CQLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKC--AEEITLTIGQAFDLAYRKFLESGGK 158
Cdd:cd01274    79 HEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVdlATEIILTLGQAFEVAYQLALRAQKS 146

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKfarhikkSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRLK-------DLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1773095124 107 DKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYR 150
Cdd:cd13161    77 DKKLFAFISHDPRLGRITCHVFRCKRGAQEICDTIAEAFKAAAE 120

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHikksegqKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd01268    17 FPVKYLGCVEVGESRGMQVCEEALKKLKASRK-------KPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRN 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1773095124 107 DKRIFTFICKDSESNKHLCYVFDSEK-CAEEITLTIGQAFDLAYRK 151
Cdd:cd01268    90 HERAFSYICRDGTTRRWMCHCFLAVKdSGERLSHAVGCAFAACLER 135

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  14 MHTPEALsKHFIPYNAKFLGSTEVEQPKG-TEVVRdAVRKLKF---ARHIKKSegqkipKVELQISIYGVK-ILEPKTKE 88
Cdd:cd01270    19 LHNEEAF-QHGITFQAKYIGSLEVPRPSSrVEIVA-AMRRIRYefkAKNIKKK------KVTITVSVDGVKvVLRKKKKK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  89 VQH----------NCQLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEK--CAEEITLTIGQAFDLAYRKFLESG 156
Cdd:cd01270    91 KGWtwdesklllmQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKksQAMRIVRTIGQAFEVCHKLSLQHM 170

                  ....*
gi 1773095124 157 GKDVE 161
Cdd:cd01270   171 QGNAD 175

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain; APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  29 AKFLGSTEVEQPKGTEVVRDAVRKLKFARHI----KKSEGQkipkveLQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13158    15 VRFLGSMEVKSDRTSEVIYEAMRQVLAARAIhnifRMTESH------LLVTSDCLRLIDPQTQVTRARFPLADVVQFAAH 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1773095124 105 KTDKRIFTFICKDSES----NKHLCYVFDSEKCAEEITLTIGQA 144
Cdd:cd13158    89 QENKRLFGFVVRTPEGdgeePSFSCYVFESNTEGEKICDAIALA 132

JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARhikKSEGQKIPK--VELQISIYGVKI------LEPKTKEVQHNCQ-LHR 97
Cdd:cd01212     5 FLLGFLGSVEVPYHKGNDVLCQAMQKIATAR---RLTVHLRPPqsCILEISDRGLKMvdrskpNKKDGKPCIHYFYsLKN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1773095124  98 ISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLE 154
Cdd:cd01212    82 ISFCGFHPRNSRYFGFITKHPLLQRFACHVFVSQESTRPVAESVGRAFQRFYQEFIE 138

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  25 IPYNAKFLGSTEVEQPKGTEVVrDAVRKLKFArhIKKSEGQKIPkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13157     2 VSRNAQYIGSFPVSGLDVADRA-DSVRKQLES--LKESGSRGRP-VILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1773095124 105 KTDKRiFTFICKD--SESNKHLCYVF--DSEKCAEEITLTIGQAFDLAYRK 151
Cdd:cd13157    78 PAHAQ-FAFVARNpgGPTNRQYCHVFvtRSPREAQELNLLLCRAFQLAYLK 127

uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  25 IPYNAKFLGSTEVEQPKGTEVVRDAvrklkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13168     1 ALYKALYLGQVEVGEDGGVEQIESA------AIIVVLESDLTPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1773095124 105 KTDKRIFTFICKD---SESNKHLCYVFDSEKCAE--EITLTIGQAFD 146
Cdd:cd13168    75 VDDPNYFAYIAGDtpcSLAKHFVCYVFEAADEEEaeTILQGIAQGFK 121

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773095124  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLkfARHIKKSegQKIPkVELQISIYGVKIL-EPKTKEVQHNCQLHRISFCADDK 105
Cdd:cd01271     9 LKALYLGSTPVSKPTGMDVLNEAIDTL--LSSVPKE--QWTP-VNVSVAPSTVTILsQKDEEEVLVECRVRFLSFMGIGK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1773095124 106 TDKRiFTFICkDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRK 151
Cdd:cd01271    84 DVHT-FAFIM-DTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127

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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1773095124 163 RKQIAGLQKRIQDLETENMELKNKVQDLENQLR 195
Cdd:cd14686    20 KERIEELEEEVEELEEENEELKAELEELRAEVE 52

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. 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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1773095124 163 RKQ--IAGLQKRIQDLETENMELKNKVQDLENQ 193
Cdd:cd14689    20 RKKeyIDGLESRVAACTAENQELKKKVEELEKQ 52

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1773095124 161 ETRKQIAGLQKRIQDLETENMELKNKVQDLEN 192
Cdd:COG2919    33 ELRQEIAELEAENAKLKARNAELEAEVADLKD 64

Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1773095124 161 ETRKQIAGLQKRIQDLETENMELKNKVQDLENQLRITQV 199
Cdd:COG4839    66 ELNREIQSLESKISEQQKENEDLEQEVSELSSPERIYKI 104