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Conserved domains on  [gi|24649848|ref|NP_651311|]
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uncharacterized protein Dmel_CG11168, isoform A [Drosophila melanogaster]

Protein Classification

PTB_Anks domain-containing protein( domain architecture ID 13838464)

PTB_Anks domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 688-857 6.31e-73

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.


:

Pssm-ID: 269972  Cd Length: 146  Bit Score: 235.64  E-value: 6.31e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 688 SNWCHSPYTFIYGEIRYSLFYLGSTVIRKLQGTLSTRKSIQKLKIDEnlksaasvsdfsllencttstkylkaANHQTRL 767
Cdd:cd01274   1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKST--------------------------REMKKIP 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 768 NVDIAVSCVGVKFIDHDKKTAICCHDIENINCVCQDSEDLRYFAYITKE--QDLHYCHVFMVDSLELAKEIIMTLGQAFE 845
Cdd:cd01274  55 TIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDlkTDHHYCHVFCVLTVDLATEIILTLGQAFE 134

                       170
                ....*....|..
gi 24649848 846 VAYQLALSRQGT 857
Cdd:cd01274 135 VAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-271 6.46e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 6.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666  80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTP 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLilpykRLEDDNEEllgcmpikhif 201
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-----NAKDNDGK----------- 220

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848 202 thTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:COG0666 221 --TALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-69 8.42e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649848     6 HLLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLL 69
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG-------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 688-857 6.31e-73

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.


Pssm-ID: 269972  Cd Length: 146  Bit Score: 235.64  E-value: 6.31e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 688 SNWCHSPYTFIYGEIRYSLFYLGSTVIRKLQGTLSTRKSIQKLKIDEnlksaasvsdfsllencttstkylkaANHQTRL 767
Cdd:cd01274   1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKST--------------------------REMKKIP 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 768 NVDIAVSCVGVKFIDHDKKTAICCHDIENINCVCQDSEDLRYFAYITKE--QDLHYCHVFMVDSLELAKEIIMTLGQAFE 845
Cdd:cd01274  55 TIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDlkTDHHYCHVFCVLTVDLATEIILTLGQAFE 134

                       170
                ....*....|..
gi 24649848 846 VAYQLALSRQGT 857
Cdd:cd01274 135 VAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-271 6.46e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 6.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666  80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTP 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLilpykRLEDDNEEllgcmpikhif 201
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-----NAKDNDGK----------- 220

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848 202 thTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:COG0666 221 --TALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-148 3.66e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    53 LHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptgANPNAQTiENETPLHSGAQHGHNA 132
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 24649848   133 VVAILLSYGADPAIRN 148
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-271 3.51e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 3.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   42 INCQDMNGYTSLH-HACLNGHSNIVRLLLSHNALLDVPDIRGSTPL--FLAAWAGHQDIVKMLLMHsptGANPNAQTIEN 118
Cdd:PHA03095  76 VNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK---GADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  119 ETPLH----SgaqhgHNA---VVAILLSYGADPAIRNNSFQTALDLAAQFGRlqvvqtllrvypdlilPYKRLeddNEEL 191
Cdd:PHA03095 153 MTPLAvllkS-----RNAnveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFK----------------PRARI---VREL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  192 --LGCMPI-KHIFTHTCLHLASRNGHKK--VVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDG 265
Cdd:PHA03095 209 irAGCDPAaTDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSS 288


                 ....*.
gi 24649848  266 NGRTAL 271
Cdd:PHA03095 289 DGNTPL 294
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 702-854 2.28e-16

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 76.58  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    702 IRYSLFYLGSTVIRKLQGTLSTRKSIQKLKidenlksaasvsdfsllencttstKYLKAANHQTRlNVDIAVSCVGVKFI 781
Cdd:smart00462   4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLR------------------------AAQGSEKKEPQ-KVILSISSRGVKLI 58

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649848    782 DHDKKTAICCHDIENINCVCQDSEDLRYFAYITKEQD--LHYCHVFMVDSleLAKEIIMTLGQAFEVAYQLALSR 854
Cdd:smart00462  59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGssRFACHVFRCEK--AAEDIALAIGQAFQLAYELKLKA 131
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
768-847 2.26e-13

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 67.77  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   768 NVDIAVSCVGVKFIDHDKKTAICCHDIENIN-CVCQDSEDLRYFAYITKEQDLHY--CHVFMvdSLELAKEIIMTLGQAF 844
Cdd:pfam00640  53 KVDLFISTDGLKLLNPDTQELIHDHPLVSISfCADGDPDLMRYFAYIARDKATNKfaCHVFE--SEDGAQDIAQSIGQAF 130


                  ...
gi 24649848   845 EVA 847
Cdd:pfam00640 131 ALA 133
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-172 5.68e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 5.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  49 GYTSLHHACLNGHSNIVRLLLSHNAllDVPDIR----------------GSTPLFLAAWAGHQDIVKMLLMHsptGANPN 112
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEH---GADIR 163

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848 113 AQTIENETPLHSGAQHGhNAVVA-----ILLSYGA--DPA----IRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd22192 164 AQDSLGNTVLHILVLQP-NKTFAcqmydLILSYDKedDLQpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-69 8.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649848     6 HLLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLL 69
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG-------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-77 8.70e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 8.70e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 24649848     48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 688-857 6.31e-73

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.


Pssm-ID: 269972  Cd Length: 146  Bit Score: 235.64  E-value: 6.31e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 688 SNWCHSPYTFIYGEIRYSLFYLGSTVIRKLQGTLSTRKSIQKLKIDEnlksaasvsdfsllencttstkylkaANHQTRL 767
Cdd:cd01274   1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKST--------------------------REMKKIP 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 768 NVDIAVSCVGVKFIDHDKKTAICCHDIENINCVCQDSEDLRYFAYITKE--QDLHYCHVFMVDSLELAKEIIMTLGQAFE 845
Cdd:cd01274  55 TIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDlkTDHHYCHVFCVLTVDLATEIILTLGQAFE 134

                       170
                ....*....|..
gi 24649848 846 VAYQLALSRQGT 857
Cdd:cd01274 135 VAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-271 6.46e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 6.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666  80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTP 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLilpykRLEDDNEEllgcmpikhif 201
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-----NAKDNDGK----------- 220

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848 202 thTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:COG0666 221 --TALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-239 1.31e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   7 LLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPL 86
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAG-------------ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  87 FLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQV 166
Cdd:COG0666 158 HLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649848 167 VQTLLRVYPDLILPYKRLEDDneellgcmpikhifthtcLHLASRNGHKKVVETLLAAGVDVNILTNAGSALH 239
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTA------------------LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-273 2.08e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 2.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA---GADINAKDDGGNTL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLrvypdlilpyKRLEDDNeellgcmpIKHIF 201
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL----------EAGADVN--------AQDND 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649848 202 THTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDI 273
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-273 1.44e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  64 IVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHSPtGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGAD 143
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLA-LLALALADALGALLLLAAALAGDLLVALLLLAAGAD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 144 PAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLILPYKRLEddneellgcmpikhifthTCLHLASRNGHKKVVETLLA 223
Cdd:COG0666  80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE------------------TPLHLAAYNGNLEIVKLLLE 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24649848 224 AGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDI 273
Cdd:COG0666 142 AGADVNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 702-844 3.18e-21

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.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 89.88  E-value: 3.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 702 IRYSLFYLGSTVIRKLQGTLSTRKSIQKLKIdenlksaasvsdfsllencttstkyLKAANHQTRLNVDIAVSCVGVKFI 781
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAA-------------------------ALKSSKRKPGPVLLEVSSKGVKLL 55

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649848 782 DHDKKTAICCHDIENINCVCQDSEDLRYFAYITKEQDL--HYCHVFMVDSLELAKEIIMTLGQAF 844
Cdd:cd00934  56 DLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGEEGGsgFRCHVFQCEDEEEAEEILQAIGQAF 120
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-148 3.66e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    53 LHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptgANPNAQTiENETPLHSGAQHGHNA 132
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 24649848   133 VVAILLSYGADPAIRN 148
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-114 3.23e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848     7 LLEASRAGDIKTVDKLLEHSSkrhgplssfrrspSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDirGSTPL 86
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-------------DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTAL 65

                          90       100
                  ....*....|....*....|....*...
gi 24649848    87 FLAAWAGHQDIVKMLLMHsptGANPNAQ 114
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEK---GADINVK 90
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 692-849 6.21e-19

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.


Pssm-ID: 269971  Cd Length: 144  Bit Score: 84.25  E-value: 6.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 692 HSPYTFIYGEIRYSLFYLGSTVIRKLQGTLSTRKSIQKLKIDENLKsaasvsdfsllencttstkylKAANHQTRlNVDI 771
Cdd:cd01273   2 HPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLK---------------------KSEGAKLP-KVEL 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 772 AVSCVGVKFIDHDKKTAICCHDIENINCVCQDSEDLRYFAYITKEQDL--HYCHVFmvDSLELAKEIIMTLGQAFEVAYQ 849
Cdd:cd01273  60 QISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSESekHLCFVF--DSEKLAEEITLTIGQAFDLAYR 137
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-271 3.51e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 3.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   42 INCQDMNGYTSLH-HACLNGHSNIVRLLLSHNALLDVPDIRGSTPL--FLAAWAGHQDIVKMLLMHsptGANPNAQTIEN 118
Cdd:PHA03095  76 VNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK---GADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  119 ETPLH----SgaqhgHNA---VVAILLSYGADPAIRNNSFQTALDLAAQFGRlqvvqtllrvypdlilPYKRLeddNEEL 191
Cdd:PHA03095 153 MTPLAvllkS-----RNAnveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFK----------------PRARI---VREL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  192 --LGCMPI-KHIFTHTCLHLASRNGHKK--VVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDG 265
Cdd:PHA03095 209 irAGCDPAaTDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSS 288


                 ....*.
gi 24649848  266 NGRTAL 271
Cdd:PHA03095 289 DGNTPL 294
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 702-854 2.28e-16

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 76.58  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    702 IRYSLFYLGSTVIRKLQGTLSTRKSIQKLKidenlksaasvsdfsllencttstKYLKAANHQTRlNVDIAVSCVGVKFI 781
Cdd:smart00462   4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLR------------------------AAQGSEKKEPQ-KVILSISSRGVKLI 58

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649848    782 DHDKKTAICCHDIENINCVCQDSEDLRYFAYITKEQD--LHYCHVFMVDSleLAKEIIMTLGQAFEVAYQLALSR 854
Cdd:smart00462  59 DEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGssRFACHVFRCEK--AAEDIALAIGQAFQLAYELKLKA 131
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-230 1.82e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLlrvypdliLPYKRLEDDNEellgcmpikhif 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL--------LEHADVNLKDN------------ 60

                          90       100
                  ....*....|....*....|....*....
gi 24649848   202 THTCLHLASRNGHKKVVETLLAAGVDVNI 230
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINV 89
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
768-847 2.26e-13

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 67.77  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   768 NVDIAVSCVGVKFIDHDKKTAICCHDIENIN-CVCQDSEDLRYFAYITKEQDLHY--CHVFMvdSLELAKEIIMTLGQAF 844
Cdd:pfam00640  53 KVDLFISTDGLKLLNPDTQELIHDHPLVSISfCADGDPDLMRYFAYIARDKATNKfaCHVFE--SEDGAQDIAQSIGQAF 130


                  ...
gi 24649848   845 EVA 847
Cdd:pfam00640 131 ALA 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 16-231 1.34e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   16 IKTVDKLLEHSSkrhgplssfrrspSINCQDMNGYTSLHHACLNGHS-----NIVRLLLSHNALLDVPDIRGSTPLFLAA 90
Cdd:PHA03100  48 IDVVKILLDNGA-------------DINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   91 WA--GHQDIVKMLLMHsptGANPNAQTIENETPLHSGA--------------QHGHNA----VVAILLSYGADPAIRNNS 150
Cdd:PHA03100 115 SKksNSYSIVEYLLDN---GANVNIKNSDGENLLHLYLesnkidlkilklliDKGVDInaknRVNYLLSYGVPINIKDVY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  151 FQTALDLAAQFGRLQVVQTLLRvypdlilpykrleddneelLGCMP-IKHIFTHTCLHLASRNGHKKVVETLLAAGVDVN 229
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLD-------------------LGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ..
gi 24649848  230 IL 231
Cdd:PHA03100 253 TI 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-235 5.38e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   41 SINCQDMNGYTSLHhACLNG---HSNIVRLLLSHNALLDVPDIRGSTPL--FLAAWAGHQDIVKMLLMHsptGANPNAQT 115
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDA---GADVYAVD 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  116 IENETPLHSGAQ--HGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVqtllrvypdLILPYkrLE---DDNEE 190
Cdd:PHA03095 185 DRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRS---------LVLPL--LIagiSINAR 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24649848  191 llgcmpikHIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNAG 235
Cdd:PHA03095 254 --------NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-264 5.79e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   155 LDLAAQFGRLQVVQTLLRVYPDlilpyKRLEDDNEEllgcmpikhifthTCLHLASRNGHKKVVEtLLAAGVDVNILTNA 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-----ANLQDKNGR-------------TALHLAAKNGHLEIVK-LLLEHADVNLKDNG 61

                          90       100       110
                  ....*....|....*....|....*....|
gi 24649848   235 GSALHEAALCGKKSVVVTLLKAGIYVHATD 264
Cdd:pfam12796  62 RTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-271 1.10e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   13 AGDIKTVDKLLEHsskrhgplssfrRSPSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWA 92
Cdd:PHA02874  11 SGDIEAIEKIIKN------------KGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   93 GHQDIVKMLLMHSPTGANPNAQTIENETplhsgaqhghnavVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:PHA02874  79 GAHDIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  173 VYPDLilpykRLEDDNeellGCMPIkhifthtclHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVV 251
Cdd:PHA02874 146 YGADV-----NIEDDN----GCYPI---------HIAIKHNFFDIIKLLLEKGAYANVKDNNGeSPLHNAAEYGDYACIK 207

                        250       260
                 ....*....|....*....|
gi 24649848  252 TLLKAGIYVHATDGNGRTAL 271
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPL 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 42-264 1.17e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLmhsPTGANPNAQTIENETP 121
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL---EKGAYANVKDNNGESP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVvqtllrvypDLILPYKRLEDdnEELLGCMPIKHIF 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI---------ELLINNASIND--QDIDGSTPLHHAI 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649848  202 THTClhlasrngHKKVVETLLAAGVDVNILTNAGSALHEAAL--CGKKSVVVTLLKAGIYVHATD 264
Cdd:PHA02874 263 NPPC--------DIDIIDILLYHKADISIKDNKGENPIDTAFkyINKDPVIKDIIANAVLIKEAD 319
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-231 5.40e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   62 SNIVRLLLSHNALLDVPDI-RGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSY 140
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY---GANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  141 GADPAIRNNSFQTALDLAAqfGRL---QVVQTLLrvypdlilpykrleddneELLGCMPIK-HIFTHTCLHLASRNghKK 216
Cdd:PHA02878 224 GASTDARDKCGNTPLHISV--GYCkdyDILKLLL------------------EHGVDVNAKsYILGLTALHSSIKS--ER 281

                        170
                 ....*....|....*
gi 24649848  217 VVETLLAAGVDVNIL 231
Cdd:PHA02878 282 KLKLLLEYGADINSL 296
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-289 8.72e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV--PDIRgsTPLFLAAWAGHQDIVKMLLMhSPTGANpNAQTIENETPLHSG 125
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVkyPDIE--SELHDAVEEGDVKAVEELLD-LGKFAD-DVFYKDGMTPLHLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  126 AQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRvypdlilpyKRLEDDNEELLGCMPikhifthtc 205
Cdd:PHA02875 110 TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID---------HKACLDIEDCCGCTP--------- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  206 LHLASRNGHKKVVETLLAAGVDVNILTNAGSAlheAALC-----GKKSVVVTLLKAGI---YVHATDGNGRTALDILSDY 277
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCV---AALCyaienNKIDIVRLFIKRGAdcnIMFMIEGEECTILDMICNM 248

                        250
                 ....*....|..
gi 24649848  278 PPHVTYDIVGAI 289
Cdd:PHA02875 249 CTNLESEAIDAL 260
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-189 1.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   42 INCQDMNGYTSLHHACLN--GHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQD--IVKMLLMHsptGANPNAQT-- 115
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDK---GVDINAKNrv 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  116 --------------IENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDL--IL 179
Cdd:PHA03100 176 nyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIktII 255

                        170
                 ....*....|
gi 24649848  180 PYKRLEDDNE 189
Cdd:PHA03100 256 ETLLYFKDKD 265
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-278 5.82e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   96 DIVKMLLmhsPTGANPNAQTIENETPLHsgaQHGHNA------VVAILLSYGADPAIRNNSFQTALDLAAQFG-RLQVVQ 168
Cdd:PHA03095  28 EEVRRLL---AAGADVNFRGEYGKTPLH---LYLHYSsekvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  169 TLLRVYPDLilpykrleddNEellgcmpiKHIFTHTCLH--LASRNGHKKVVETLLAAGVDVNILTNAG-SALHeaALCG 245
Cdd:PHA03095 102 LLIKAGADV----------NA--------KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGmTPLA--VLLK 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24649848  246 KKSVVV----TLLKAGIYVHATDGNGRTALDILSDYP 278
Cdd:PHA03095 162 SRNANVellrLLIDAGADVYAVDDRFRSLLHHHLQSF 198
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-171 6.96e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 6.96e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24649848   120 TPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLL 171
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-102 7.67e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 7.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24649848    49 GYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLL 102
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-171 8.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   10 ASRAGDIKTVDKLLEHSSkrhgplssfrrspSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLA 89
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGA-------------DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   90 AWAGHQDIVKMLLMHSP-------TGANP---------------------NAQTIENETPLHSGAQHGHNA-VVAILLSY 140
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNhimnkckNGFTPlhnaiihnrsaiellinnasiNDQDIDGSTPLHHAINPPCDIdIIDILLYH 277

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24649848  141 GADPAIRNNSFQTALDLAAQF-GRLQVVQTLL 171
Cdd:PHA02874 278 KADISIKDNKGENPIDTAFKYiNKDPVIKDII 309
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 701-845 9.47e-09

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.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 54.26  E-value: 9.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 701 EIRYSLFYLGSTVIRKLQGTLSTRKSIQKlkIDENLKSaasvsdfsllencttSTKYLKaanhqtrlNVDIAVSCVGVKF 780
Cdd:cd13159   2 GVTFYLKYLGSTLVEKPKGEGATAEAVKT--IIAMAKA---------------SGKKLQ--------KVTLTVSPKGIKV 56

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649848 781 IDHDKKTAICCHDIENI-NCVCQDSEDlRYFAYITKEQDL--HYCHVFMVDSLELAKEIIMTLGQAFE 845
Cdd:cd13159  57 TDSATNETILEVSIYRIsYCTADANHD-KVFAFIATNQDNekLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 763-849 9.91e-09

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.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 54.18  E-value: 9.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 763 HQTRLNVDIAVSCVGVKFIDHDKKTAICCHDIENINCVCQDSEDLRYFAYITKEQDLH--YCHVFMVDSleLAKEIIMTL 840
Cdd:cd13161  34 KLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISHDPRLGriTCHVFRCKR--GAQEICDTI 111


                ....*....
gi 24649848 841 GQAFEVAYQ 849
Cdd:cd13161 112 AEAFKAAAE 120
Ank_5 pfam13857
Ankyrin repeats (many copies);
37-89 1.07e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 1.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24649848    37 RRSPSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLA 89
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-113 1.25e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.25e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848   43 NCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHSPTGANPNA 113
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 108-172 3.63e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 3.63e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649848  108 GANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 767-852 4.20e-08

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.


Pssm-ID: 269920  Cd Length: 170  Bit Score: 53.75  E-value: 4.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 767 LNVDIAVSCVGVKFIDHDKKTAICCHDIENINCV-CQDSEDLRYFAYITK-EQDLHYCHVFMVdSLELAKEIIMTLGQAF 844
Cdd:cd01209  83 MNISLTISTDGLNLVTPDTGQIIANHHMQSISFAsGGDPDTYDYVAYVAKdPVNQRACHVLEC-GDGLAQDVIATIGQAF 161


                ....*...
gi 24649848 845 EVAYQLAL 852
Cdd:cd01209 162 ELRFKQYL 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-172 5.68e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 5.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  49 GYTSLHHACLNGHSNIVRLLLSHNAllDVPDIR----------------GSTPLFLAAWAGHQDIVKMLLMHsptGANPN 112
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEH---GADIR 163

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848 113 AQTIENETPLHSGAQHGhNAVVA-----ILLSYGA--DPA----IRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd22192 164 AQDSLGNTVLHILVLQP-NKTFAcqmydLILSYDKedDLQpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-177 8.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 8.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLA-AWAGHQDIVKMLLMHsptGANPNAQ-TIENE 119
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEH---GVDVNAKsYILGL 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24649848  120 TPLHSGAQHghNAVVAILLSYGADPAIRNNSFQTALDLAA------QFGRLQVVQTLL--RVYPDL 177
Cdd:PHA02878 271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLlkRIKPDI 334
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 769-862 9.21e-08

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.


Pssm-ID: 269968  Cd Length: 179  Bit Score: 52.67  E-value: 9.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 769 VDIAVSCVGVKFIDHDKK-----------TAICCHDIENINCVCQDSEDLRYFAYITKE--QDLHYCHVFMVDSLELAKE 835
Cdd:cd01270  71 VTITVSVDGVKVVLRKKKkkkgwtwdeskLLLMQHPIYRIFYVSHDSQDLKIFSYIARDgsSNVFKCNVFKSKKKSQAMR 150

                        90       100
                ....*....|....*....|....*..
gi 24649848 836 IIMTLGQAFEVAYQLALSRQGTSLNEE 862
Cdd:cd01270 151 IVRTIGQAFEVCHKLSLQHMQGNADDE 177
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-228 1.45e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    3 KDQHLLEA--SRAGDIKTVDK-LLEHSSKRHGplssfrrspsINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALL---- 75
Cdd:PLN03192 475 KTSTLIEAmqTRQEDNVVILKnFLQHHKELHD----------LNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALleel 544

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   76 -------DVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGA--DPAI 146
Cdd:PLN03192 545 lkakldpDIGDSKGRTPLHIAASKGYEDCVLVLLKH---ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHA 621

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  147 RNNsfqtALDLAAQFGRLQVVQTLLRvypdlilpyKRLEDDNEELLGCmpikhifthTCLHLASRNGHKKVVETLLAAGV 226
Cdd:PLN03192 622 AGD----LLCTAAKRNDLTAMKELLK---------QGLNVDSEDHQGA---------TALQVAMAEDHVDMVRLLIMNGA 679


                 ..
gi 24649848  227 DV 228
Cdd:PLN03192 680 DV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-79 2.02e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 2.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649848     7 LLEASRAGDIKTVDKLLEHsskrhgplssfrrsPSINCQDmNGYTSLHHACLNGHSNIVRLLLSHNALLDVPD 79
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEH--------------ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-277 2.78e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   63 NIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQ---DIVKMLLmhsPTGANPNAQTIENETPLHSGAQHGHNA-VVAILL 138
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLL---EAGADVNAPERCGFTPLHLYLYNATTLdVIKLLI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  139 SYGADPAIRNNSFQTALD--LAAQFGRLQVVQTLLRVYPDLilpykrledDNEELLGCMPIkHIFthtclhLASRNGHKK 216
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADV---------NALDLYGMTPL-AVL------LKSRNANVE 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649848  217 VVETLLAAGVDVNILTNAG-SALHEAALCGKKS--VVVTLLKAGIYVHATDGNGRTALDILSDY 277
Cdd:PHA03095 169 LLRLLIDAGADVYAVDDRFrSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-138 4.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 4.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649848    82 GSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK---GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 15-118 7.39e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   15 DIKT-VDKLLEHSSKrhgplssfrrspsINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAG 93
Cdd:PHA03100 170 NAKNrVNYLLSYGVP-------------INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                         90       100
                 ....*....|....*....|....*
gi 24649848   94 HQDIVKMLLMHsptgaNPNAQTIEN 118
Cdd:PHA03100 237 NKEIFKLLLNN-----GPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-286 7.86e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  112 NAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDL-ILPYKRLEDDN-E 189
Cdd:PHA02874  29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsILPIPCIEKDMiK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  190 ELLGC---MPIKHIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNAGS-ALHEAALCGKKSVVVTLLKAGIYVHATDG 265
Cdd:PHA02874 109 TILDCgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCyPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188

                        170       180
                 ....*....|....*....|.
gi 24649848  266 NGRTALDILSDYPPHVTYDIV 286
Cdd:PHA02874 189 NGESPLHNAAEYGDYACIKLL 209
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-229 1.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   36 FRRSPSINCQDMNGYTSLHHACLNGH-SNIVRLLLSHNALLDVPDIRGSTPLFLAAWAG-HQDIVKMLLmhsPTGANPNA 113
Cdd:PHA02876 294 LERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLL---ELGANVNA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  114 QTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAaqfgrlqvvqtLLRVYPdlILPYKRLEDDNEELLG 193
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-----------LCGTNP--YMSVKTLIDRGANVNS 437

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24649848  194 cmpiKHIFTHTCLHLASRNGHK-KVVETLLAAGVDVN 229
Cdd:PHA02876 438 ----KNKDLSTPLHYACKKNCKlDVIEMLLDNGADVN 470
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 7-172 1.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    7 LLEASRAGDIKTVDKLLEhsskrhgpLSSFrrspsinCQDM---NGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGS 83
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLD--------LGKF-------ADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   84 TPLFLAAWAGHQDIVKMLLMHSptgANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPA-IRNNSFQTALDLAAQFG 162
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHK---ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENN 213

                        170
                 ....*....|
gi 24649848  163 RLQVVQTLLR 172
Cdd:PHA02875 214 KIDIVRLFIK 223
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 118-274 1.90e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 118 NETPLHSGAQHghNAVVAI---LLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLIlpykrleddNEELLGC 194
Cdd:cd22192  17 SESPLLLAAKE--NDVQAIkklLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELV---------NEPMTSD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 195 MpikhIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNAGSA---------------LHEAALCGKKSVVVTLLKAGIY 259
Cdd:cd22192  86 L----YQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGAD 161

                       170
                ....*....|....*
gi 24649848 260 VHATDGNGRTALDIL 274
Cdd:cd22192 162 IRAQDSLGNTVLHIL 176
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-143 2.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   42 INCQDMN-GYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENET 120
Cdd:PHA02878 160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNT 236

                         90       100
                 ....*....|....*....|....
gi 24649848  121 PLHSGAQHGHN-AVVAILLSYGAD 143
Cdd:PHA02878 237 PLHISVGYCKDyDILKLLLEHGVD 260
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-254 4.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24649848   204 TCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLL 254
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-123 6.79e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649848    68 LLSH-NALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLH 123
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY---GVDLNLKDEEGLTALD 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-264 7.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 7.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   94 HQDIVKMLLMHSPTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGAD------------------------------ 143
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADvniialddlsvlecavdsknidtikaiidn 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  144 ------------PAIRNNSFQTAL------------DLAAQFGRLQVVQT--LLRVYPDLIlpyKRLEDDNEellgcmpi 197
Cdd:PHA02876 234 rsninkndlsllKAIRNEDLETSLllydagfsvnsiDDCKNTPLHHASQApsLSRLVPKLL---ERGADVNA-------- 302

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  198 KHIFTHTCLHLASRNGH-KKVVETLLAAGVDVNILTNA-GSALHEAALCGK-KSVVVTLLKAGIYVHATD 264
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLyITPLHQASTLDRnKDIVITLLELGANVNARD 372
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-69 8.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649848     6 HLLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLL 69
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG-------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-158 1.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24649848   103 MHSPTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLA 158
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 751-850 2.03e-05

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.


Pssm-ID: 269926  Cd Length: 147  Bit Score: 45.32  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 751 CTTSTKYLKAA-----NHQTRLNVDIAVScvGVKFIDHDKKTAICCHDIENINCVCQDSEDLRYFAYITKEQDLHycHVF 825
Cdd:cd01215  37 CQDAMMKLKGAvkaagEHKQRIWLNISLE--GIKILDEKTGALLHHHPVHKISFIARDTTDNRAFGYVCGLDGGH--RFF 112

                        90       100
                ....*....|....*....|....*
gi 24649848 826 MVDSLELAKEIIMTLGQAFEVAYQL 850
Cdd:cd01215 113 AIKTAKAAEPVVLDLRDLFQVVFEL 137
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 765-848 6.53e-05

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.


Pssm-ID: 269979  Cd Length: 129  Bit Score: 43.53  E-value: 6.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 765 TRLNVDIAVSCVGVKFIDHDKKTAICCHDIENIN-CVCqDSEDLRyFAYITKE----QDLHYCHVFMVDSLELAKEIIMT 839
Cdd:cd13157  39 RGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSySTC-RPAHAQ-FAFVARNpggpTNRQYCHVFVTRSPREAQELNLL 116


                ....*....
gi 24649848 840 LGQAFEVAY 848
Cdd:cd13157 117 LCRAFQLAY 125
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 22-172 8.66e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 8.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  22 LLEHSSKRHGPLSSFRRSPSInCQDMNGYTSLHHACLNGHSNIVRLLLSHNAllDV--------------PDIR-GSTPL 86
Cdd:cd21882  47 LLLEAAPDSGNPKELVNAPCT-DEFYQGQTALHIAIENRNLNLVRLLVENGA--DVsaratgrffrkspgNLFYfGELPL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  87 FLAAWAGHQDIVKMLLMHSPTGANPNAQTIENETPLHSGAQHGHNAVVA---------ILLSYGA--DPA-----IRNNS 150
Cdd:cd21882 124 SLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHALVLQADNTPENsafvcqmynLLLSYGAhlDPTqqleeIPNHQ 203

                       170       180
                ....*....|....*....|..
gi 24649848 151 FQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd21882 204 GLTPLKLAAVEGKIVMFQHILQ 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-77 8.70e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 8.70e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 24649848     48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 53-140 1.03e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   53 LHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLmhsPTGANPNAQTIENETPLHSGAQHGHNA 132
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL---EFGADPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 24649848  133 VVAILLSY 140
Cdd:PTZ00322 163 VVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 79-271 1.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   79 DIRGSTPLFLAAWAGH-QDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAV-VAILLSYGADPAIRNNSFQTALD 156
Cdd:PHA02876 270 DDCKNTPLHHASQAPSlSRLVPKLLER---GADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  157 LAAQFGRLQ-VVQTLLrvypdlilpykrleddneELLGCMPIKHIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNA- 234
Cdd:PHA02876 347 QASTLDRNKdIVITLL------------------ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKi 408

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24649848  235 GSALHeAALCGKK--SVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:PHA02876 409 GTALH-FALCGTNpyMSVKTLIDRGANVNSKNKDLSTPL 446
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-115 1.14e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 24649848    81 RGSTPLFLAAW-AGHQDIVKMLLMHsptGANPNAQT 115
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSK---GADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 203-233 1.27e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 24649848   203 HTCLHLAS-RNGHKKVVETLLAAGVDVNILTN 233
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 203-230 1.37e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.37e-04
                           10        20
                   ....*....|....*....|....*...
gi 24649848    203 HTCLHLASRNGHKKVVETLLAAGVDVNI 230
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-77 1.51e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 24649848    48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV 77
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 702-844 2.18e-04

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.


Pssm-ID: 269989  Cd Length: 125  Bit Score: 41.93  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 702 IRYSLFYLGSTVIrklqGTLSTRKSIQKLKIDENLKSaasvsdfsllencttstkylkaanHQTRLNVDIAVSCVGVKFI 781
Cdd:cd13168   1 ALYKALYLGQVEV----GEDGGVEQIESAAIIVVLES------------------------DLTPKEVLLELGEIGVTVW 52

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649848 782 DHDKKTAICCHDIENINCVCQDSEDLRYFAYITKE--QDL---HYCHVFMVDSLELAKEIIMTLGQAF 844
Cdd:cd13168  53 DKSTSEVLFKHSFPEISSCGRRVDDPNYFAYIAGDtpCSLakhFVCYVFEAADEEEAETILQGIAQGF 120
PHA03095 PHA03095
ankyrin-like protein; Provisional
 6-158 2.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848    6 HLLEASRAGDIKTVDKLLEHSSKRHGplssfrrspsincQDMNGYTSLHHACLNGHSN--IVRLLLSHNALLDVPDIRGS 83
Cdd:PHA03095 157 AVLLKSRNANVELLRLLIDAGADVYA-------------VDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGN 223

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649848   84 TPLFLAAWAG---HQDIVKMLLmhspTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLA 158
Cdd:PHA03095 224 TPLHSMATGSsckRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-271 2.92e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848   93 GHQDIVKMLLmhsPTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:PHA02875  13 GELDIARRLL---DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  173 V--YPDLILpYKRleddneellGCMPikhifthtcLHLASRNGHKKVVETLLAAGVDVNIL-TNAGSALHEAALCGKKSV 249
Cdd:PHA02875  90 LgkFADDVF-YKD---------GMTP---------LHLATILKKLDIMKLLIARGADPDIPnTDKFSPLHLAVMMGDIKG 150

                        170       180
                 ....*....|....*....|..
gi 24649848  250 VVTLLKAGIYVHATDGNGRTAL 271
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPL 172
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 773-849 3.76e-04

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.


Pssm-ID: 269923  Cd Length: 149  Bit Score: 41.49  E-value: 3.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848 773 VSCVGVKFIDHDKK---TAICCHD----IENIN-CVCQDSeDLRYFAYITKEQDLH--YCHVFMvdSLELAKEIIMTLGQ 842
Cdd:cd01212  51 ISDRGLKMVDRSKPnkkDGKPCIHyfysLKNISfCGFHPR-NSRYFGFITKHPLLQrfACHVFV--SQESTRPVAESVGR 127


                ....*..
gi 24649848 843 AFEVAYQ 849
Cdd:cd01212 128 AFQRFYQ 134
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-79 5.02e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 5.02e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 24649848    48 NGYTSLHHACL-NGHSNIVRLLLSHNALLDVPD 79
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 126-222 8.63e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  126 AQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLILPYKrleDDNeellgcmpikhifthTC 205
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK---DGK---------------TP 151

                         90
                 ....*....|....*..
gi 24649848  206 LHLASRNGHKKVVETLL 222
Cdd:PTZ00322 152 LELAEENGFREVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 45-171 1.26e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  45 QDMNGYTSLHHACLNGHSNIVRLLLSHNALLDV--------PDIR------GSTPLFLAAWAGHQDIVKMLLMHSPTgaN 110
Cdd:cd22194 137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnPKYKhegfyfGETPLALAACTNQPEIVQLLMEKEST--D 214

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649848 111 PNAQTIENETPLH-----SGAQHGHNAVV-----AILLSYGAD--PAIRNNSFQTALDLAAQFGRLQVVQTLL 171
Cdd:cd22194 215 ITSQDSRGNTVLHalvtvAEDSKTQNDFVkrmydMILLKSENKnlETIRNNEGLTPLQLAAKMGKAEILKYIL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-113 1.53e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.53e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 24649848     81 RGSTPLFLAAWAGHQDIVKMLLMHsptGANPNA 113
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK---GADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 213-271 1.61e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  213 GHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-149 1.77e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.77e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 24649848   119 ETPLHSGA-QHGHNAVVAILLSYGADPAIRNN 149
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 102-274 1.83e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  102 LMHSptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRlQVVQTLlrvypDLILPY 181
Cdd:PHA02946  58 LLHR--GYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDD-EVIERI-----NLLVQY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  182 KRLEDDNEELLGCMPIkhifthtclhLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCG--KKSVVVTLLKAGI 258
Cdd:PHA02946 130 GAKINNSVDEEGCGPL----------LACTDPSERVFKKIMSIGFEARIVDKFGkNHIHRHLMSDnpKASTISWMMKLGI 199

                        170
                 ....*....|....*.
gi 24649848  259 YVHATDGNGRTALDIL 274
Cdd:PHA02946 200 SPSKPDHDGNTPLHIV 215
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 204-286 2.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  204 TCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDILSDYPphVT 282
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNnSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYC--KD 247


                 ....
gi 24649848  283 YDIV 286
Cdd:PHA02878 248 YDIL 251
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-230 2.34e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 2.34e-03
                          10        20
                  ....*....|....*....|....*..
gi 24649848   204 TCLHLASRNGHKKVVETLLAAGVDVNI 230
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-264 2.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649848  120 TPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQfgrLQVVQTLLRVYPDLILPY---KRLEDDNeellGCMP 196
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSN---IKYNLTDVKEIVKLLLEYganVNAPDNN----GITP 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649848  197 IkHIFTHTCLhlasrnGHKKVVETLLAAGVDVNILTNAG-SALHEAALCG--KKSVVVTLLKAGIYVHATD 264
Cdd:PHA03100 110 L-LYAISKKS------NSYSIVEYLLDNGANVNIKNSDGeNLLHLYLESNkiDLKILKLLIDKGVDINAKN 173
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 770-844 3.12e-03

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.


Pssm-ID: 269967  Cd Length: 143  Bit Score: 38.82  E-value: 3.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24649848 770 DIAvSCV-GVKFIDHdkktaicchdienINCVCQDSEDLRYFAYItkeqdlhyCHVFMVDSLELAKEIIMTLGQAF 844
Cdd:cd01269  90 DIS-SCSqGIKHVDH-------------FGFICRESSEGGGFHFV--------CYVFKCQSESVVDEIMLTIKQAF 143
Ank_5 pfam13857
Ankyrin repeats (many copies);
221-273 5.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24649848   221 LLAAG-VDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDI 273
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
236-273 7.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 7.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 24649848   236 SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDI 273
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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