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 578804475  14 MHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273    1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804475  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273   81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 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 578804475  14 MHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273    1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804475  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273   81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804475   27 YNAKFLGSTEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLH 96
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578804475   97 RISFCAD-DKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLA 148
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133

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

                         10        20        30
                 ....*....|....*....|....*....|..
gi 578804475 161 ETRKQIAGLQKRIQDLETENMELKNKVQDLEN 192
Cdd:COG2919   33 ELRQEIAELEAENAKLKARNAELEAEVADLKD 64

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 578804475  14 MHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273    1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804475  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273   81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 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 578804475  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKfarHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd00934    3 FQVKYLGSVEVGSSRGVDVVEEALKALA---AALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 578804475 107 DKRIFTFICKDSESNKHLCYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd00934   80 NPNVFAFIAGEEGGSGFRCHVFqcEDEEEAEEILQAIGQAF 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 578804475  13 WMHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKfarhIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHN 92
Cdd:cd01274    3 WRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLICE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804475  93 CQLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKC--AEEITLTIGQAFDLAYRKFLESGGK 158
Cdd:cd01274   79 HEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVdlATEIILTLGQAFEVAYQLALRAQKS 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 578804475  24 FIPYNAKFLGSTEVEQPKGTEVVRDAVRKlkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCAD 103
Cdd:cd13159    2 GVTFYLKYLGSTLVEKPKGEGATAEAVKT---IIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578804475 104 DKTDKRIFTFICKDSESNKHLCYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd13159   79 DANHDKVFAFIATNQDNEKLECHAFlcAKRKMAQAVTLTVAQAF 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 578804475  15 HTPEALSKHF----IPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhIKKSEGQKiPKVELQISIYGVKILEPKTKEVQ 90
Cdd:cd01215    2 KTAENLPERFrgdgVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGA--VKAAGEHK-QRIWLNISLEGIKILDEKTGALL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804475  91 HNCQLHRISFCADDKTDKRIFTFICkdSESNKHLCYVFDSEKCAEEITLTIGQAFDLAY 149
Cdd:cd01215   79 HHHPVHKISFIARDTTDNRAFGYVC--GLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVF 135

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects 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 insects, ticks, sea urchins, and nematodes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804475  30 KFLGSteveQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKiLEPKTKEVQHNCQ----LHRISFCADDK 105
Cdd:cd13160    6 KYLGR----MPARGLWGIKHTRKPLVDALKNLPKGKTLPKTKLEVSSDGVK-LEELRGGFGSSKTvffpIHTISYGVQDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 578804475 106 TDKRIFTFICK-DSESNKHL--CYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd13160   81 VHTRVFSMIVVgEQDSSNHPfeCHAFvcDSRADARNLTYWLAKAF 125

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an 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. This cd is part of the Shc-like subgroup.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804475  13 WMHTPEALSKH-FIPYNAKFLGSTEVEQ-------PKGTEVVRDAVRKL----KFARHIKKSEGQKI---------PK-- 69
Cdd:cd01209    2 GWLHPDQLGMGpGVSYPVRYVGCIEVLQsmrsldfNTRTQVTREAINRVceavGGAKGAKRKRKSKAlssilgksnLQfa 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804475  70 ---VELQISIYGVKILEPKTKEVQHNCQLHRISF--CADDKTDKRIfTFICKDsESNKHLCYVFD-SEKCAEEITLTIGQ 143
Cdd:cd01209   82 gmnISLTISTDGLNLVTPDTGQIIANHHMQSISFasGGDPDTYDYV-AYVAKD-PVNQRACHVLEcGDGLAQDVIATIGQ 159

                        170
                 ....*....|
gi 578804475 144 AFDLAYRKFL 153
Cdd:cd01209  160 AFELRFKQYL 169

X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is unknown to date. X11 has a PTB domain followed by two PDZ 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 578804475  17 PEALSKHFIpYNAKFLGSTEVEQPKGTevvRDAVRKLKfARH----IKKSEGQKIP--KVELQISIYGVKILEPKTKEVQ 90
Cdd:cd01208    1 PEDLIDGVI-FGANYLGSTQLLSERNP---SKNVRMAQ-AQEavsrVKAPEGESQPstEVDLFISTERIKVLNADTQETM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804475  91 HNCQLHRISFCAD-----------------DKTDKRIFTFICKDSESNKHLCYVFDSEKcAEEITLTIGQAFDLAYRKFL 153
Cdd:cd01208   76 MDHALRTISYIADignivvlmarrrmprssSQECVETTPPSQEGKRQYKMICHVFESED-AQLIAQSIGQAFSVAYQEFL 154

                 ....
gi 578804475 154 ESGG 157
Cdd:cd01208  155 RANG 158

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 578804475  26 PYNAKF-----LGSTEVEQPKGTEVVRD-AVRKLKF--ARHIKKSEGQKIPKVE-------LQISIYGVKILEPKTKEVQ 90
Cdd:cd01269    4 PSNSQFfevlyCGKIKVSHKKVPPTFIDdCLEKFRLheLEKSRSGPSSVQPTDSeenrtmlFQIGRSELRLISPDTKQVL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804475  91 HNCQLHRISFCADDKTDKRIFTFICKDSESNK---HLCYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd01269   84 LEKQFKDISSCSQGIKHVDHFGFICRESSEGGgfhFVCYVFkcQSESVVDEIMLTIKQAF 143

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 578804475   27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKipkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:pfam08416   2 YRVEHLTTFELDSLTGLQAVEDAIRKLQLLDAQGRVWTQE---MLLQVSDQGITLTDNETKEELESYPLDSISHCQAVLN 78

                          90       100
                  ....*....|....*....|....*
gi 578804475  107 DKR---IFTFICKDSESNKHLCYVF 128
Cdd:pfam08416  79 DGRynsILALVCQEPGQSKPDVHLF 103

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC 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 578804475  31 FLGSTEVEQPKgTEVvrDAVRKLKfarhIKKSEGQKIPKVELQI--SIYG-VKILEPKTKEVQHNCQLHRISFCA---DD 104
Cdd:cd01211    8 YLGCAKVNAPR-SET--EALRIMA----ILREQSAQPIKVTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILFCArgpDG 80

                         90       100
                 ....*....|....*....|....
gi 578804475 105 KTDKRIFTFICKDSESNKHLCYVF 128
Cdd:cd01211   81 TSESDCFAFTWSHGETAIFQCHVF 104

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 578804475 150 RKFLESGG---KDVET-RKQIAGLQKRIQDLETENMELKNKVQDLE 191
Cdd:cd21937    8 KQHLGAPGpedADVEAlRLENEELKQKNEELEEENKELKAKLQQYE 53

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 578804475 163 RK--QIAGLQKRIQDLETENMELKNKVQDLENQL 194
Cdd:cd14687   19 RKkqWVQQLEEKVRKLESENKALKAEVDKLREEV 52

basic region leucin zipper;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 578804475   163 RKQIAGLQKRIQDLETENMELKNKVQDLENQLR 195
Cdd:smart00338  25 KAEIEELERKVEQLEAENERLKKEIERLRRELE 57