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 1958802068   3 STEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd01273    21 CTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSF 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958802068  83 ICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 126
Cdd:cd01273   101 IAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 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 1958802068   3 STEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd01273    21 CTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSF 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958802068  83 ICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 126
Cdd:cd01273   101 IAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802068   3 STEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLHRISFCAD 72
Cdd:pfam00640   8 SVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958802068  73 -DKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLA 117
Cdd:pfam00640  88 gDPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133

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 1958802068   3 STEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd01273    21 CTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSF 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958802068  83 ICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 126
Cdd:cd01273   101 IAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 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 1958802068   3 STEVEQPKGTEVVRDAVRKLKfarHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd00934    10 SVEVGSSRGVDVVEEALKALA---AALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAF 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958802068  83 ICKDSESNKHLCFVF--DSEKCAEEITLTIGQAF 114
Cdd:cd00934    87 IAGEEGGSGFRCHVFqcEDEEEAEEILQAIGQAF 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 1958802068   3 STEVEQPKGTEVVRDAVRKLKfarhIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd01274    24 STEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAY 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958802068  83 ICKDSESNKHLCFVFDSEKC--AEEITLTIGQAFDLAYRKFLESGGK 127
Cdd:cd01274   100 ITKDLKTDHHYCHVFCVLTVdlATEIILTLGQAFEVAYQLALRAQKS 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 1958802068   3 STEVEQPKGTEVVRDAVRKlkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd13159    12 STLVEKPKGEGATAEAVKT---IIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHDKVFAF 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958802068  83 ICKDSESNKHLCFVF--DSEKCAEEITLTIGQAF 114
Cdd:cd13159    89 IATNQDNEKLECHAFlcAKRKMAQAVTLTVAQAF 122

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 1958802068   3 STEVEQPKGTEVVRDAVRKLKFARHikksegqKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTF 82
Cdd:cd01268    24 CVEVGESRGMQVCEEALKKLKASRK-------KPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHERAFSY 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958802068  83 ICKDSESNKHLCFVFDSEK-CAEEITLTIGQAFDLAYRK 120
Cdd:cd01268    97 ICRDGTTRRWMCHCFLAVKdSGERLSHAVGCAFAACLER 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 1958802068   3 STEVEQPKG-TEVVRdAVRKLKF---ARHIKKSegqkipKVELQISIYGVK-ILEPKTKEVQH----------NCQLHRI 67
Cdd:cd01270    38 SLEVPRPSSrVEIVA-AMRRIRYefkAKNIKKK------KVTITVSVDGVKvVLRKKKKKKGWtwdesklllmQHPIYRI 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958802068  68 SFCADDKTDKRIFTFICKDSESNKHLCFVFDSEK--CAEEITLTIGQAFDLAYRKFLESGGKDVE 130
Cdd:cd01270   111 FYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKksQAMRIVRTIGQAFEVCHKLSLQHMQGNAD 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 1958802068   3 STEVEQPKGTEVVRDAVRKLKFARHI----KKSEGQkipkveLQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKR 78
Cdd:cd13158    20 SMEVKSDRTSEVIYEAMRQVLAARAIhnifRMTESH------LLVTSDCLRLIDPQTQVTRARFPLADVVQFAAHQENKR 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958802068  79 IFTFICKDSES----NKHLCFVFDSEKCAEEITLTIGQA 113
Cdd:cd13158    94 LFGFVVRTPEGdgeePSFSCYVFESNTEGEKICDAIALA 132

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 1958802068  28 IKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLHRISFCAD-----------------DKTDKRIFTFICKDSE 88
Cdd:cd01208    42 VKAPEGESQPstEVDLFISTERIKVLNADTQETMMDHALRTISYIADignivvlmarrrmprssSQECVETTPPSQEGKR 121

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958802068  89 SNKHLCFVFDSEKcAEEITLTIGQAFDLAYRKFLESGG 126
Cdd:cd01208   122 QYKMICHVFESED-AQLIAQSIGQAFSVAYQEFLRANG 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958802068  48 VKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTFICKDSESNK---HLCFVF--DSEKCAEEITLTIGQAF 114
Cdd:cd01269    72 LRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGgfhFVCYVFkcQSESVVDEIMLTIKQAF 143

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 1958802068  27 HIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKTDKRIFTFICKD---SESNKHLCFVFDSEKCA 103
Cdd:cd13168    28 IVVLESDLTPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDtpcSLAKHFVCYVFEAADEE 107

                          90
                  ....*....|....
gi 1958802068 104 E--EITLTIGQAFD 115
Cdd:cd13168   108 EaeTILQGIAQGFK 121