Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. 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 767918496   5 DYVVAFQILIRKMFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHR 84
Cdd:cd01273    5 EALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918496  85 ISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 144
Cdd:cd01273   85 ISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. 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 767918496   5 DYVVAFQILIRKMFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHR 84
Cdd:cd01273    5 EALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918496  85 ISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 144
Cdd:cd01273   85 ISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918496   18 FLGSTEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLHRISF 87
Cdd:pfam00640   5 YLGSVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLVSISF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767918496   88 CAD-DKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLA 135
Cdd:pfam00640  85 CADgDPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133

basic region leucin zipper;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 767918496   150 RKQ--IAGLQKRIQDLETENMELKNKVQDLENQLR 182
Cdd:smart00338  23 RKKaeIEELERKVEQLEAENERLKKEIERLRRELE 57

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. 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 767918496   5 DYVVAFQILIRKMFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHR 84
Cdd:cd01273    5 EALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918496  85 ISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 144
Cdd:cd01273   85 ISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind 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 767918496  18 FLGSTEVEQPKGTEVVRDAVRKLKfarHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRI 97
Cdd:cd00934    7 YLGSVEVGSSRGVDVVEEALKALA---AALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNV 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767918496  98 FTFICKDSESNKHLCYVF--DSEKCAEEITLTIGQAF 132
Cdd:cd00934   84 FAFIAGEEGGSGFRCHVFqcEDEEEAEEILQAIGQAF 120

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 767918496  18 FLGSTEVEQPKGTEVVRDAVRKLKfarhIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRI 97
Cdd:cd01274   21 YLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNT 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767918496  98 FTFICKDSESNKHLCYVFDSEKC--AEEITLTIGQAFDLAYRKFLESGGK 145
Cdd:cd01274   97 FAYITKDLKTDHHYCHVFCVLTVdlATEIILTLGQAFEVAYQLALRAQKS 146

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains 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 contains mammals, insects, and sponges.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918496  18 FLGSTEVEQPKGTEVVRDAVRKlkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRI 97
Cdd:cd13159    9 YLGSTLVEKPKGEGATAEAVKT---IIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHDKV 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767918496  98 FTFICKDSESNKHLCYVF--DSEKCAEEITLTIGQAF 132
Cdd:cd13159   86 FAFIATNQDNEKLECHAFlcAKRKMAQAVTLTVAQAF 122

Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. 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 767918496  19 LGSTEVEQPKGTEVVRDAVRKLKFArhIKKSEGQKiPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIF 98
Cdd:cd01215   23 IGIDEVPAARGDKMCQDAMMKLKGA--VKAAGEHK-QRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNRAF 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767918496  99 TFICkdSESNKHLCYVFDSEKCAEEITLTIGQAFDLAY 136
Cdd:cd01215  100 GYVC--GLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVF 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 767918496   9 AFQ--ILIRKMFLGSTEVEQPKG-TEVVRdAVRKLKF---ARHIKKSegqkipKVELQISIYGVK-ILEPKTKEVQH--- 78
Cdd:cd01270   24 AFQhgITFQAKYIGSLEVPRPSSrVEIVA-AMRRIRYefkAKNIKKK------KVTITVSVDGVKvVLRKKKKKKGWtwd 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918496  79 -------NCQLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEK--CAEEITLTIGQAFDLAYRKFLESGGKDVE 148
Cdd:cd01270   97 esklllmQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKksQAMRIVRTIGQAFEVCHKLSLQHMQGNAD 175

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 767918496  18 FLGSTEVEQPKGTEVVRDAVRKLKFARhikKSEGQKIPK--VELQISIYGVKI------LEPKTKEVQHNCQ-LHRISFC 88
Cdd:cd01212    9 FLGSVEVPYHKGNDVLCQAMQKIATAR---RLTVHLRPPqsCILEISDRGLKMvdrskpNKKDGKPCIHYFYsLKNISFC 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767918496  89 ADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLE 141
Cdd:cd01212   86 GFHPRNSRYFGFITKHPLLQRFACHVFVSQESTRPVAESVGRAFQRFYQEFIE 138

TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. 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 767918496  17 MFLGSTEVEQPKGTEVVRD-AVRKLKF--ARHIKKSEGQKIPKVE-------LQISIYGVKILEPKTKEVQHNCQLHRIS 86
Cdd:cd01269   13 LYCGKIKVSHKKVPPTFIDdCLEKFRLheLEKSRSGPSSVQPTDSeenrtmlFQIGRSELRLISPDTKQVLLEKQFKDIS 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767918496  87 FCADDKTDKRIFTFICKDSESNK---HLCYVF--DSEKCAEEITLTIGQAF 132
Cdd:cd01269   93 SCSQGIKHVDHFGFICRESSEGGgfhFVCYVFkcQSESVVDEIMLTIKQAF 143

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 767918496  46 IKKSEGQKIPkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRiFTFICKD--SESNKHLCYVF--DSEKCA 121
Cdd:cd13157   33 LKESGSRGRP-VILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAHAQ-FAFVARNpgGPTNRQYCHVFvtRSPREA 110

                         90
                 ....*....|....*..
gi 767918496 122 EEITLTIGQAFDLAYRK 138
Cdd:cd13157  111 QELNLLLCRAFQLAYLK 127

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918496   19 LGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKipkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKR-- 96
Cdd:pfam08416   7 LTTFELDSLTGLQAVEDAIRKLQLLDAQGRVWTQE---MLLQVSDQGITLTDNETKEELESYPLDSISHCQAVLNDGRyn 83

                          90       100
                  ....*....|....*....|
gi 767918496   97 -IFTFICKDSESNKHLCYVF 115
Cdd:pfam08416  84 sILALVCQEPGQSKPDVHLF 103

leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767918496 137 RKFLESGG---KDVET-RKQIAGLQKRIQDLETENMELKNKVQDLE 178
Cdd:cd21937    8 KQHLGAPGpedADVEAlRLENEELKQKNEELEEENKELKAKLQQYE 53

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 767918496 150 RKQ--IAGLQKRIQDLETENMELKNKVQDLENQ 180
Cdd:cd14689   20 RKKeyIDGLESRVAACTAENQELKKKVEELEKQ 52

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 767918496  45 HIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTFICKD---SESNKHLCYVFDSEKCA 121
Cdd:cd13168   28 IVVLESDLTPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDtpcSLAKHFVCYVFEAADEE 107

                         90
                 ....*....|....
gi 767918496 122 E--EITLTIGQAFD 133
Cdd:cd13168  108 EaeTILQGIAQGFK 121

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

                         10        20        30
                 ....*....|....*....|....*....|..
gi 767918496 148 ETRKQIAGLQKRIQDLETENMELKNKVQDLEN 179
Cdd:COG2919   33 ELRQEIAELEAENAKLKARNAELEAEVADLKD 64

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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 767918496 150 RKQIAGLQKRIQDLETENMELKNKVQDLENQLR 182
Cdd:cd14699   21 RELMEELQAEVEQLEDENEKLQSEIANLRSEKE 53