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Conserved domains on  [gi|1830828474|ref|XP_002137001|]
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ankyrin repeat and SAM domain-containing protein 1A [Drosophila pseudoobscura]

Protein Classification

ankyrin repeat and sterile alpha motif domain-containing protein( domain architecture ID 13334064)

ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein similar to Homo sapiens ankyrin repeat and SAM domain-containing protein 1A/1B

Gene Ontology:  GO:0046875|GO:1901187|GO:0005515
PubMed:  8987385|17176038|30306850

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 ...
 1180-1323 9.50e-79

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: 255.67  E-value: 9.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1180 TEWRHSAQTLLNEHINYEVQYLGSTVVKELRGTESTKKSIQKLKASgKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEH 1259
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKS-TREMKKIPTIILSISYKGVKFIDATTKNLICEH 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1830828474 1260 EIQNINCACQDSEDLRHFAYITKE--QDLHYCHVFQVQSTDLASEIILTLGQAFEVAYQLALRDGI 1323
Cdd:cd01274     80 EIRNISCACQDPEDLNTFAYITKDlkTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQK 145
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-272 1.55e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.55e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATANLQT 115
Cdd:COG0666     74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQD 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  116 IEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELIAhlaamergtrspsspa 195
Cdd:COG0666    151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA---------------- 214

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830828474  196 spsRTIFPHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:COG0666    215 ---KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1019-1083 6.36e-30

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


The actual alignment was detected with superfamily member cd09500:

Pssm-ID: 472832  Cd Length: 65  Bit Score: 113.17  E-value: 6.36e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1019 KQQGVATLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQTVLEINKLGHRRRILQSLAYI 1083
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 1180-1323 9.50e-79

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: 255.67  E-value: 9.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1180 TEWRHSAQTLLNEHINYEVQYLGSTVVKELRGTESTKKSIQKLKASgKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEH 1259
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKS-TREMKKIPTIILSISYKGVKFIDATTKNLICEH 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1830828474 1260 EIQNINCACQDSEDLRHFAYITKE--QDLHYCHVFQVQSTDLASEIILTLGQAFEVAYQLALRDGI 1323
Cdd:cd01274     80 EIRNISCACQDPEDLNTFAYITKDlkTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQK 145
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-272 1.55e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.55e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATANLQT 115
Cdd:COG0666     74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQD 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  116 IEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELIAhlaamergtrspsspa 195
Cdd:COG0666    151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA---------------- 214

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830828474  196 spsRTIFPHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:COG0666    215 ---KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1019-1083 6.36e-30

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 113.17  E-value: 6.36e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1019 KQQGVATLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQTVLEINKLGHRRRILQSLAYI 1083
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1196-1320 6.68e-30

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: 115.87  E-value: 6.68e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  1196 YEVQYLGSTVVKELRGTESTKKSIQKLKASGKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSEDLR 1275
Cdd:smart00462    6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLD 85

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1830828474  1276 HFAYITKEQD--LHYCHVFqvQSTDLASEIILTLGQAFEVAYQLALR 1320
Cdd:smart00462   86 VFGYIARDPGssRFACHVF--RCEKAAEDIALAIGQAFQLAYELKLK 130
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-148 2.26e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 2.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   53 LHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrpATANLQTiEQETPLHCAAQHGHTG 132
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKD-NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1830828474  133 ALALLLGHDADPNMRN 148
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
1196-1314 8.77e-18

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 80.87  E-value: 8.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1196 YEVQYLGST-VVKELRGTESTKKSI----------QKLKASGKGEGKS--GSPLSLAISHRGVEFIDVSSKRIICEHEIQ 1262
Cdd:pfam00640    1 FAVRYLGSVeVPEERAPDKNTRMQQareairrvkaAKINKIRGLSGETgpGTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1263 NIN-CACQDSEDLRHFAYITKEQDLHY--CHVFQvqSTDLASEIILTLGQAFEVA 1314
Cdd:pfam00640   81 SISfCADGDPDLMRYFAYIARDKATNKfaCHVFE--SEDGAQDIAQSIGQAFALA 133
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-272 4.23e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 4.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHE---DIVRLLLANDASPNLPDSRGSSPLHLAAWAGET-DIVRLLLthpYRPATA 111
Cdd:PHA03095    34 LAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLI---KAGADV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  112 NLQTIEQETPLH--CAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGR--LQAVQMLIRAHPELIA-------- 179
Cdd:PHA03095   111 NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAvddrfrsl 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  180 ---HL-------AAMERGTRspSSPASPSRTIFPHTCLHLASRNG--HKSVVEVLLAAGVSVNLLTPSG-TALHEASLCG 246
Cdd:PHA03095   191 lhhHLqsfkpraRIVRELIR--AGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGqTPLHYAAVFN 268

                          250       260
                   ....*....|....*....|....*.
gi 1830828474  247 KENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:PHA03095   269 NPRACRRLIALGADINAVSSDGNTPL 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-275 2.70e-13

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: 74.28  E-value: 2.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  113 LQTIE-QETPLHCAAQHGHTGALA-LLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELI--AHLAAMERGt 188
Cdd:cd22192     11 LQQKRiSESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnePMTSDLYQG- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  189 rspsspaspsrtifpHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSGTA--LHEASLC-------------GKENVVRT 253
Cdd:cd22192     90 ---------------ETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrPGPKNLIyygehplsfaacvGNEEIVRL 154

                          170       180
                   ....*....|....*....|..
gi 1830828474  254 LLKAGIDLSATDNEGRTALDIL 275
Cdd:cd22192    155 LIEHGADIRAQDSLGNTVLHIL 176
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1023-1089 3.13e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.83  E-value: 3.13e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830828474  1023 VATLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDvELQTVLEINKLGHRRRILQSlayIRQMRDS 1089
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSE-EDLKELGITKLGHRKKILKA---IQKLKEQ 68
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1025-1087 4.33e-06

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 45.34  E-value: 4.33e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830828474 1025 TLQQWLHSIALPEYLEFFNKHlYNTIESVCGVWDVELQtVLEINKLGHRRRILQSlayIRQMR 1087
Cdd:pfam00536    7 DVGEWLESIGLGQYIDSFRAG-YIDGDALLQLTEDDLL-KLGVTLLGHRKKILYA---IQRLK 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 5.05e-06

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: 44.12  E-value: 5.05e-06
                            10        20
                    ....*....|....*....|....*....
gi 1830828474    49 GYSALHHACLNGHEDIVRLLLANDASPNL 77
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-165 1.32e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNL------------PDS--RGSSPLHLAAWAGETDIVRLLLTHPYRPATA--- 111
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTAdsl 207

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1830828474  112 -----NLQTIEQE-----TPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQ 165
Cdd:TIGR00870  208 gntllHLLVMENEfkaeyEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIV 271
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 1180-1323 9.50e-79

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: 255.67  E-value: 9.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1180 TEWRHSAQTLLNEHINYEVQYLGSTVVKELRGTESTKKSIQKLKASgKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEH 1259
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKS-TREMKKIPTIILSISYKGVKFIDATTKNLICEH 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1830828474 1260 EIQNINCACQDSEDLRHFAYITKE--QDLHYCHVFQVQSTDLASEIILTLGQAFEVAYQLALRDGI 1323
Cdd:cd01274     80 EIRNISCACQDPEDLNTFAYITKDlkTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQK 145
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-272 1.55e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.55e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATANLQT 115
Cdd:COG0666     74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQD 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  116 IEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELIAhlaamergtrspsspa 195
Cdd:COG0666    151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA---------------- 214

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830828474  196 spsRTIFPHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:COG0666    215 ---KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-274 1.23e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.23e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   33 LASLRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATAN 112
Cdd:COG0666     38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA---GADVN 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  113 LQTIEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELIAhlaamergtrsps 192
Cdd:COG0666    115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA------------- 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  193 spaspsRTIFPHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTA 271
Cdd:COG0666    182 ------RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255


                   ...
gi 1830828474  272 LDI 274
Cdd:COG0666    256 LLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-179 1.46e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.46e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474    7 FLEAARNGNISHIEKVLTQKAKragplaslrrgtgVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPL 86
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   87 HLAAWAGETDIVRLLLTHpyrPATANLQTIEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQA 166
Cdd:COG0666    158 HLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                          170
                   ....*....|...
gi 1830828474  167 VQMLIRAHPELIA 179
Cdd:COG0666    235 VKLLLEAGADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-277 1.05e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 1.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   50 YSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHPyrpATANLQTIEQETPLHCAAQHG 129
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  130 HTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELIAhlaamergtrspsspaspsRTIFPHTCLHL 209
Cdd:COG0666     99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-------------------QDNDGNTPLHL 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1830828474  210 ASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTALDILRE 277
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1019-1083 6.36e-30

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 113.17  E-value: 6.36e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1019 KQQGVATLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQTVLEINKLGHRRRILQSLAYI 1083
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1196-1320 6.68e-30

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: 115.87  E-value: 6.68e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  1196 YEVQYLGSTVVKELRGTESTKKSIQKLKASGKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSEDLR 1275
Cdd:smart00462    6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLD 85

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1830828474  1276 HFAYITKEQD--LHYCHVFqvQSTDLASEIILTLGQAFEVAYQLALR 1320
Cdd:smart00462   86 VFGYIARDPGssRFACHVF--RCEKAAEDIALAIGQAFQLAYELKLK 130
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 1196-1311 1.20e-25

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: 102.97  E-value: 1.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1196 YEVQYLGSTVVKELRGTESTKKSIQKLKASGKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSEDLR 1275
Cdd:cd00934      3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPN 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1830828474 1276 HFAYITKEQDL--HYCHVFQVQSTDLASEIILTLGQAF 1311
Cdd:cd00934     83 VFAFIAGEEGGsgFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 1184-1316 1.71e-25

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: 103.51  E-value: 1.71e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1184 HSAQTLLNEHINYEVQYLGSTVVKELRGTESTKKSIQKLKAS---GKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEHE 1260
Cdd:cd01273      2 HPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFArqlKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830828474 1261 IQNIN-CAcQDSEDLRHFAYITKEQDL--HYCHVFqvQSTDLASEIILTLGQAFEVAYQ 1316
Cdd:cd01273     82 LHRISfCA-DDKTDKRIFSFIAKDSESekHLCFVF--DSEKLAEEITLTIGQAFDLAYR 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-148 2.26e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 2.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   53 LHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrpATANLQTiEQETPLHCAAQHGHTG 132
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKD-NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1830828474  133 ALALLLGHDADPNMRN 148
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-155 2.27e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 2.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   10 AARNGNISHIEKVLTQKAKragplaslrrgtgVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLA 89
Cdd:COG0666    160 AAANGNLEIVKLLLEAGAD-------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1830828474   90 AWAGETDIVRLLLTHpyrPATANLQTIEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPL 155
Cdd:COG0666    227 AENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
1196-1314 8.77e-18

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 80.87  E-value: 8.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1196 YEVQYLGST-VVKELRGTESTKKSI----------QKLKASGKGEGKS--GSPLSLAISHRGVEFIDVSSKRIICEHEIQ 1262
Cdd:pfam00640    1 FAVRYLGSVeVPEERAPDKNTRMQQareairrvkaAKINKIRGLSGETgpGTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1263 NIN-CACQDSEDLRHFAYITKEQDLHY--CHVFQvqSTDLASEIILTLGQAFEVA 1314
Cdd:pfam00640   81 SISfCADGDPDLMRYFAYIARDKATNKfaCHVFE--SEDGAQDIAQSIGQAFALA 133
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 1192-1312 1.71e-17

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: 79.68  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1192 EHINYEVQYLGSTVVKELRGTEST----KKSIQKLKASGKGEGKsgspLSLAISHRGVEFIDVSSKRIICEHEIQNI-NC 1266
Cdd:cd13159      1 DGVTFYLKYLGSTLVEKPKGEGATaeavKTIIAMAKASGKKLQK----VTLTVSPKGIKVTDSATNETILEVSIYRIsYC 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1830828474 1267 ACQDSEDlRHFAYITKEQDL--HYCHVFQVQSTDLASEIILTLGQAFE 1312
Cdd:cd13159     77 TADANHD-KVFAFIATNQDNekLECHAFLCAKRKMAQAVTLTVAQAFN 123
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-272 4.23e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 4.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHE---DIVRLLLANDASPNLPDSRGSSPLHLAAWAGET-DIVRLLLthpYRPATA 111
Cdd:PHA03095    34 LAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLI---KAGADV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  112 NLQTIEQETPLH--CAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGR--LQAVQMLIRAHPELIA-------- 179
Cdd:PHA03095   111 NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAvddrfrsl 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  180 ---HL-------AAMERGTRspSSPASPSRTIFPHTCLHLASRNG--HKSVVEVLLAAGVSVNLLTPSG-TALHEASLCG 246
Cdd:PHA03095   191 lhhHLqsfkpraRIVRELIR--AGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGqTPLHYAAVFN 268

                          250       260
                   ....*....|....*....|....*.
gi 1830828474  247 KENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:PHA03095   269 NPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-104 4.48e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 4.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   10 AARNGNISHIeKVLtqkakragplasLRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANdASPNLPDSrGSSPLHLA 89
Cdd:pfam12796    4 AAKNGNLELV-KLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68

                           90
                   ....*....|....*
gi 1830828474   90 AWAGETDIVRLLLTH 104
Cdd:pfam12796   69 ARSGHLEIVKLLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-279 5.64e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 5.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   63 DIVRLLLANDASPNLPDSRGSSPLHL---AAWAGETDIVRLLLThpyrpATANLQTIEQ--ETPLHCAAQHGHT-GALAL 136
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLE-----AGADVNAPERcgFTPLHLYLYNATTlDVIKL 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  137 LLGHDADPNMRNSRGETPLdlaaqygrlqavqmlirahpeliahlaamergtrspsspaspsrtifpHTClhLASRNGHK 216
Cdd:PHA03095   103 LIKAGADVNAKDKVGRTPL------------------------------------------------HVY--LSGFNINP 132

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  217 SVVEVLLAAGVSVNLLTPSG-TALH------EASLcgkeNVVRTLLKAGIDLSATDNEGRTALDILREFP 279
Cdd:PHA03095   133 KVIRLLLRKGADVNALDLYGmTPLAvllksrNANV----ELLRLLIDAGADVYAVDDRFRSLLHHHLQSF 198
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 1196-1316 3.85e-15

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: 73.05  E-value: 3.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1196 YEVQYLGSTVVKELRGTESTKKSIQKLKAsgkgEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSEDLR 1275
Cdd:cd13161      4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKD----LKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1830828474 1276 HFAYITKEQDLH--YCHVFQVqsTDLASEIILTLGQAFEVAYQ 1316
Cdd:cd13161     80 LFAFISHDPRLGriTCHVFRC--KRGAQEICDTIAEAFKAAAE 120
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 1182-1320 5.67e-15

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: 74.17  E-value: 5.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1182 WRHSAQTLLNEHINYEVQYLGS----------------TVVKEL---------RGTESTKKSIQKLKAS--GKGEGK-SG 1233
Cdd:cd01209      3 WLHPDQLGMGPGVSYPVRYVGCievlqsmrsldfntrtQVTREAinrvceavgGAKGAKRKRKSKALSSilGKSNLQfAG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1234 SPLSLAISHRGVEFIDVSSKRIICEHEIQNINCA-CQDSEDLRHFAYITK-EQDLHYCHVFQVqSTDLASEIILTLGQAF 1311
Cdd:cd01209     83 MNISLTISTDGLNLVTPDTGQIIANHHMQSISFAsGGDPDTYDYVAYVAKdPVNQRACHVLEC-GDGLAQDVIATIGQAF 161


                   ....*....
gi 1830828474 1312 EVAYQLALR 1320
Cdd:cd01209    162 ELRFKQYLK 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-231 6.92e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 6.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  122 LHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQmlirahpELIAHLAAMERGTRspsspaspsrti 201
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-------LLLEHADVNLKDNG------------ 61

                           90       100       110
                   ....*....|....*....|....*....|
gi 1830828474  202 fpHTCLHLASRNGHKSVVEVLLAAGVSVNL 231
Cdd:pfam12796   62 --RTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-265 1.81e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  155 LDLAAQYGRLQAVQMLIRAHPELiahlaamergtrspsspasPSRTIFPHTCLHLASRNGHKSVVEVLLAaGVSVNLLTP 234
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADA-------------------NLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1830828474  235 SGTALHEASLCGKENVVRTLLKAGIDLSATD 265
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-275 2.70e-13

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: 74.28  E-value: 2.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  113 LQTIE-QETPLHCAAQHGHTGALA-LLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRAHPELI--AHLAAMERGt 188
Cdd:cd22192     11 LQQKRiSESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnePMTSDLYQG- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  189 rspsspaspsrtifpHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSGTA--LHEASLC-------------GKENVVRT 253
Cdd:cd22192     90 ---------------ETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrPGPKNLIyygehplsfaacvGNEEIVRL 154

                          170       180
                   ....*....|....*....|..
gi 1830828474  254 LLKAGIDLSATDNEGRTALDIL 275
Cdd:cd22192    155 LIEHGADIRAQDSLGNTVLHIL 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 36-171 6.65e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 6.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLThpyRPATANLQT 115
Cdd:PHA02874   111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE---KGAYANVKD 187

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1830828474  116 IEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRlQAVQMLI 171
Cdd:PHA02874   188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI 242
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 36-158 1.59e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLA-AWAGETDIVRLLLTHpyrPATANLQ 114
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEH---GVDVNAK 264

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1830828474  115 -TIEQETPLHCAAQHGHTgaLALLLGHDADPNMRNSRGETPLDLA 158
Cdd:PHA02878   265 sYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 36-161 3.30e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 3.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHP---------- 105
Cdd:PHA02874   144 FEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGnhimnkckng 223

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474  106 YRP------------------ATANLQTIEQETPLHCAAQHG-HTGALALLLGHDADPNMRNSRGETPLDLAAQY 161
Cdd:PHA02874   224 FTPlhnaiihnrsaiellinnASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-171 4.61e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 4.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1830828474  120 TPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLI 171
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-230 4.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 4.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHE-----DIVRLLLANDASPNLPDSRGSSPLHLAAWA--GETDIVRLLLTHpyrP 108
Cdd:PHA03100    55 LDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN---G 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  109 ATANLQTIEQETPLHCAAQHGHT-----------GA-------LALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQML 170
Cdd:PHA03100   132 ANVNIKNSDGENLLHLYLESNKIdlkilkllidkGVdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830828474  171 I--RAHPELiahlaamergtrspsspaspsRTIFPHTCLHLASRNGHKSVVEVLLAAGVSVN 230
Cdd:PHA03100   212 LdlGANPNL---------------------VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 1191-1317 4.05e-11

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: 62.27  E-value: 4.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1191 NEHINYEVQYLGSTVVKELRGTESTKKSIQKLKASGKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQD 1270
Cdd:cd01215     13 GDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARD 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1830828474 1271 SEDLRHFAYITKEQDLHycHVFQVQSTDLASEIILTLGQAFEVAYQL 1317
Cdd:cd01215     93 TTDNRAFGYVCGLDGGH--RFFAIKTAKAAEPVVLDLRDLFQVVFEL 137
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 49-172 8.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 8.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATANLQTIEQETPLHCAAQH 128
Cdd:PHA02875   102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH---KACLDIEDCCGCTPLIIAMAK 178

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1830828474  129 GHTGALALLLGHDADPNMRNSRGE-TPLDLAAQYGRLQAVQMLIR 172
Cdd:PHA02875   179 GDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-102 1.42e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.42e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLL 102
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-310 1.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.63  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   52 ALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHPYRPataNLQTIEQETPLHCAAQHGHT 131
Cdd:PHA02875     5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP---DVKYPDIESELHDAVEEGDV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  132 GALALLL--GHDADpNMRNSRGETPLDLAAQYGRLQAVQMLIR--AHPELIA-------HLAAMERGTRSPSSPASPSRT 200
Cdd:PHA02875    82 KAVEELLdlGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIArgADPDIPNtdkfsplHLAVMMGDIKGIELLIDHKAC 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  201 I-----FPHTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG--TALHEASLCGKENVVRTLLKAGID---LSATDNEGRT 270
Cdd:PHA02875   161 LdiedcCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECT 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1830828474  271 ALDilrefpphvtkhivaVINNFRNQMDTDEVD----EVIYRQH 310
Cdd:PHA02875   241 ILD---------------MICNMCTNLESEAIDaliaDIAIRIH 269
Ank_5 pfam13857
Ankyrin repeats (many copies);
42-89 2.78e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.97  E-value: 2.78e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1830828474   42 VNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLA 89
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-295 1.77e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   32 PLASLRRGTGVNVQ---------------DSGGYSALHHACLNGH--EDIVRLLLANDASPNLPDSRGSSPLHLAAWAG- 93
Cdd:PHA03095   155 PLAVLLKSRNANVEllrllidagadvyavDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSs 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   94 --ETDIVRLLLthpyRPATANLQTIEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLI 171
Cdd:PHA03095   235 ckRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  172 RAHPELIAHLAAMERGTRspsspaspsRTIFPHTClhlASRNghkSVVEVLLAAGVSVnlLTPSGTALHEA--SLCGKEN 249
Cdd:PHA03095   311 AKNPSAETVAATLNTASV---------AGGDIPSD---ATRL---CVAKVVLRGAFSL--LPEPIRAYHADfiRECEAEI 373

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1830828474  250 VVRTLLKAGIDLSatdnegrtALDILREFPP---HVTKhivAVINNFRN 295
Cdd:PHA03095   374 AVMRTTRIGTGVS--------LLDILFARNPdilLVSN---ASLRKKAR 411
Ank_5 pfam13857
Ankyrin repeats (many copies);
101-158 7.22e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 7.22e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1830828474  101 LLTHpyRPATANLQTIEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLA 158
Cdd:pfam13857    1 LLEH--GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 63-232 8.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 8.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   63 DIVRLLLANDASPNLPD-SRGSSPLHLAAWAGETDIVRLLLTHPyrpATANLQTIEQETPLHCAAQHGHTGALALLLGHD 141
Cdd:PHA02878   148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG---ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  142 ADPNMRNSRGETPLDLAAqyGRLQAVQMLirahpELIahlaaMERGTrspssPASPSRTIFPHTCLHLASRNghKSVVEV 221
Cdd:PHA02878   225 ASTDARDKCGNTPLHISV--GYCKDYDIL-----KLL-----LEHGV-----DVNAKSYILGLTALHSSIKS--ERKLKL 285

                          170
                   ....*....|.
gi 1830828474  222 LLAAGVSVNLL 232
Cdd:PHA02878   286 LLEYGADINSL 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-118 1.80e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrpaTANLQT 115
Cdd:PHA03100   179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN-----GPSIKT 253


                   ...
gi 1830828474  116 IEQ 118
Cdd:PHA03100   254 IIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 36-158 1.94e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 1.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQD-SGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATANLQ 114
Cdd:PHA02878   154 LSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN---GASTDAR 230

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1830828474  115 TIEQETPLHCAAQH-GHTGALALLLGHDADPNMRNS-RGETPLDLA 158
Cdd:PHA02878   231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 8-169 5.74e-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: 57.33  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474    8 LEAARNGNISHIEKVLtqKAKRAGPLAslrRGtgvnvqdSGGYSALHHACLNGHEDIVRLLLanDASP---NLPDS---- 80
Cdd:cd22192     22 LLAAKENDVQAIKKLL--KCPSCDLFQ---RG-------ALGETALHVAALYDNLEAAVVLM--EAAPelvNEPMTsdly 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   81 RGSSPLHLAAWAGETDIVRLLLTH------P------YRPATANLqTIEQETPLHCAAQHGHTGALALLLGHDADPNMRN 148
Cdd:cd22192     88 QGETALHIAVVNQNLNLVRELIARgadvvsPratgtfFRPGPKNL-IYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          170       180
                   ....*....|....*....|..
gi 1830828474  149 SRGETPLD-LAAQYGRLQAVQM 169
Cdd:cd22192    167 SLGNTVLHiLVLQPNKTFACQM 188
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 1194-1315 8.48e-08

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: 52.39  E-value: 8.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1194 INYEVQYLGSTVVKELRGTESTKkSIQKLKASGKGEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSED 1273
Cdd:cd13157      2 VSRNAQYIGSFPVSGLDVADRAD-SVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1830828474 1274 lRHFAYITKE----QDLHYCHVFQVQSTDLASEIILTLGQAFEVAY 1315
Cdd:cd13157     81 -AQFAFVARNpggpTNRQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-266 8.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 8.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   62 EDIVRLLLANDASPNLPDSRGSSPLHLAAWAG--ETD---IVRLLLthpYRPATANLQTIEQETPLHCAAQH--GHTGAL 134
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKynLTDvkeIVKLLL---EYGANVNAPDNNGITPLLYAISKksNSYSIV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  135 ALLLGHDADPNMRNSRGETPLDLAAQYGR--LQAVQMLIrahpELIAHLAAMER-------GTrspsspASPSRTIFPHT 205
Cdd:PHA03100   125 EYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLI----DKGVDINAKNRvnyllsyGV------PINIKDVYGFT 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830828474  206 CLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDN 266
Cdd:PHA03100   195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGdTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 36-104 9.82e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 9.82e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTH 104
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 87-172 9.99e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 9.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   87 HLAAwAGETDIVRLLLTHPyrpATANLQTIEQETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQA 166
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGG---ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163


                   ....*.
gi 1830828474  167 VQMLIR 172
Cdd:PTZ00322   164 VQLLSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 36-171 1.11e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLL--LTHPYRPATANl 113
Cdd:PLN03192   545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAG- 623

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830828474  114 qtieqetPLHC-AAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLI 171
Cdd:PLN03192   624 -------DLLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 1027-1080 1.26e-07

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 49.60  E-value: 1.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1830828474 1027 QQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQTvLEINKLGHRRRILQSL 1080
Cdd:cd09490      7 AEWLASIHLEQYLDLFREHGYVTATDCQGINDSRLKQ-IGISPTGHRRRILKQL 59
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 49-172 1.56e-07

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: 55.66  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNLPDSR-------------GSSPLHLAAWAGETDIVRLLLTHPYRPATANLQT 115
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD 152

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830828474  116 IEQETPLHC----AAQHGHTGALA-----LLLGHDA--DPNMR-----NSRGETPLDLAAQYGRLQAVQMLIR 172
Cdd:cd21882    153 SLGNTVLHAlvlqADNTPENSAFVcqmynLLLSYGAhlDPTQQleeipNHQGLTPLKLAAVEGKIVMFQHILQ 225
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 1025-1088 2.93e-07

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 48.83  E-value: 2.93e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1025 TLQQWLHSIALPEYLEFFNKHLYNTIESVCGV-WDvELQtVLEINKLGHRRRILqsLAyIRQMRD 1088
Cdd:cd09498      9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLtWE-DLQ-DIGITKLGHQKKLM--LA-IKKLKD 68
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1023-1089 3.13e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.83  E-value: 3.13e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830828474  1023 VATLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDvELQTVLEINKLGHRRRILQSlayIRQMRDS 1089
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSE-EDLKELGITKLGHRKKILKA---IQKLKEQ 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-138 3.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 3.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1830828474   82 GSSPLHLAAWAGETDIVRLLLTHPYRPataNLQTIEQETPLHCAAQHGHTGALALLL 138
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADI---NAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-79 3.45e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 3.45e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   10 AARNGNIsHIEKVLTQKAKragplaslrrgtgVNVQDSGgYSALHHACLNGHEDIVRLLLANDASPNLPD 79
Cdd:pfam12796   37 AAKNGHL-EIVKLLLEHAD-------------VNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 1194-1311 5.36e-07

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: 50.02  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1194 INYEVQYLGSTVVkelrGTESTKKSIQKLKASGKGEGKSGS-PLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSE 1272
Cdd:cd13168      1 ALYKALYLGQVEV----GEDGGVEQIESAAIIVVLESDLTPkEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVD 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1830828474 1273 DLRHFAYITKE--QDL---HYCHVFQVQSTDLASEIILTLGQAF 1311
Cdd:cd13168     77 DPNYFAYIAGDtpCSLakhFVCYVFEAADEEEAETILQGIAQGF 120
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 1196-1316 5.97e-07

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: 50.35  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1196 YEVQYLGSTVVKELRGTESTKKSIQKLKASGKGEGKSGSPLS--LAISHRGVEFIDVSSKRII----CEHEIQ---NIN- 1265
Cdd:cd01212      5 FLLGFLGSVEVPYHKGNDVLCQAMQKIATARRLTVHLRPPQSciLEISDRGLKMVDRSKPNKKdgkpCIHYFYslkNISf 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474 1266 CACQDSeDLRHFAYITKEQDLH--YCHVFQVQST--DLASEIiltlGQAFEVAYQ 1316
Cdd:cd01212     85 CGFHPR-NSRYFGFITKHPLLQrfACHVFVSQEStrPVAESV----GRAFQRFYQ 134
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-172 7.15e-07

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: 53.86  E-value: 7.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNLPDSRGS--------------SPLHLAAWAGETDIVRLLLTHpyrpaTANL- 113
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygeHPLSFAACVGNEEIVRLLIEH-----GADIr 163

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  114 -QTIEQETPLH-CAAQHGHTGA---LALLLGHDADPN------MRNSRGETPLDLAAQYGRLQAVQMLIR 172
Cdd:cd22192    164 aQDSLGNTVLHiLVLQPNKTFAcqmYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 1253-1311 1.68e-06

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: 48.83  E-value: 1.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1830828474 1253 KRIICEHEIQNINCACQDSEDLRHFAYITKEQDL----HY-CHVFQVQSTDLASEIILTLGQAF 1311
Cdd:cd01269     80 KQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEgggfHFvCYVFKCQSESVVDEIMLTIKQAF 143
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-288 2.60e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   13 NGNISHIEKVLTQkakragplaslrRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWA 92
Cdd:PHA02874    11 SGDIEAIEKIIKN------------KGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   93 GETDIVRLLLTH------------------------------------------------------PYRpATANLQTIEQ 118
Cdd:PHA02874    79 GAHDIIKLLIDNgvdtsilpipciekdmiktildcgidvnikdaelktflhyaikkgdlesikmlfEYG-ADVNIEDDNG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  119 ETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIrahpeliahlaamergTRSPSSPASPS 198
Cdd:PHA02874   158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI----------------DHGNHIMNKCK 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  199 RTIFPhtcLHLASRNgHKSVVEvLLAAGVSVNLLTPSG-TALHEA--SLCGKEnVVRTLLKAGIDLSATDNEGRTALDIL 275
Cdd:PHA02874   222 NGFTP---LHNAIIH-NRSAIE-LLINNASINDQDIDGsTPLHHAinPPCDID-IIDILLYHKADISIKDNKGENPIDTA 295

                          330
                   ....*....|....*
gi 1830828474  276 REFPPH--VTKHIVA 288
Cdd:PHA02874   296 FKYINKdpVIKDIIA 310
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 1252-1321 2.67e-06

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: 49.20  E-value: 2.67e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830828474 1252 SKRIICEHEIQNINCACQDSEDLRHFAYITKE--QDLHYCHVFQVQSTDLASEIILTLGQAFEVAYQLALRD 1321
Cdd:cd01270     98 SKLLLMQHPIYRIFYVSHDSQDLKIFSYIARDgsSNVFKCNVFKSKKKSQAMRIVRTIGQAFEVCHKLSLQH 169
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1025-1087 4.33e-06

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 45.34  E-value: 4.33e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830828474 1025 TLQQWLHSIALPEYLEFFNKHlYNTIESVCGVWDVELQtVLEINKLGHRRRILQSlayIRQMR 1087
Cdd:pfam00536    7 DVGEWLESIGLGQYIDSFRAG-YIDGDALLQLTEDDLL-KLGVTLLGHRKKILYA---IQRLK 64
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 1194-1283 5.03e-06

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


Pssm-ID: 241298  Cd Length: 135  Bit Score: 47.30  E-value: 5.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1194 INYEVQYLGSTVVKELRGTESTKKSIQKLKASGKGEGKSgsplSLAISHRGVEFIDVSSKRIICEHEIQNIN-CAcQDSE 1272
Cdd:cd01268     15 CSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRA----VLWVSGDGLRVVDEKTKGLIVDQTIEKVSfCA-PDRN 89

                           90
                   ....*....|.
gi 1830828474 1273 DLRHFAYITKE 1283
Cdd:cd01268     90 HERAFSYICRD 100
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 5.05e-06

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: 44.12  E-value: 5.05e-06
                            10        20
                    ....*....|....*....|....*....
gi 1830828474    49 GYSALHHACLNGHEDIVRLLLANDASPNL 77
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-272 5.87e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHPYRPATANLQT 115
Cdd:PHA02876   165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  116 IE--------------------------QETPLHCAAQHGHTGALA-LLLGHDADPNMRNSRGETPLDLAAQYG-RLQAV 167
Cdd:PHA02876   245 LKairnedletslllydagfsvnsiddcKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETPLYLMAKNGyDTENI 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  168 QMLIrahpELIAHLAAMERgtrspsspaspsrtiFPHTCLHLASR-NGHKSVVEVLLAAGVSVNLLT-PSGTALHEASLC 245
Cdd:PHA02876   325 RTLI----MLGADVNAADR---------------LYITPLHQASTlDRNKDIVITLLELGANVNARDyCDKTPIHYAAVR 385

                          250       260
                   ....*....|....*....|....*..
gi 1830828474  246 GKENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:PHA02876   386 NNVVIINTLLDYGADIEALSQKIGTAL 412
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 1198-1312 7.32e-06

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 46.86  E-value: 7.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1198 VQYLGSTVVKELRgtesTKKSIQKLKASGKGEGKSGSPLSLAISHRG---VEFIDVSSKRIICEHEIQNIN-CA--CQDS 1271
Cdd:cd01211      6 VTYLGCAKVNAPR----SETEALRIMAILREQSAQPIKVTLSVPNSSegsVRLYDPTSNTEIASYPIYRILfCArgPDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1830828474 1272 EDLRHFAyIT---KEQDLHYCHVFQVQSTDLASEIILTLGQAFE 1312
Cdd:cd01211     82 SESDCFA-FTwshGETAIFQCHVFRCEIPEAVSKVLYSFAKAFR 124
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-76 8.58e-06

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: 43.79  E-value: 8.58e-06
                           10        20
                   ....*....|....*....|....*...
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPN 76
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 13-172 9.36e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 50.18  E-value: 9.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   13 NGNISHIEKVLTQKAKRAGplaSLRRGTGVNVQDSG--GYSALHHACLNGHEDIVRLLLANDASPNL--------PDSR- 81
Cdd:cd22193     41 NPGTNDTIRILLDIAEKTD---NLKRFINAEYTDEYyeGQTALHIAIERRQGDIVALLVENGADVHAhakgrffqPKYQg 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   82 -----GSSPLHLAAWAGETDIVRLLLTHPYRPATANLQTIEQETPLHCAAQHG-----------HTGALALLLGHDADPN 145
Cdd:cd22193    118 egfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQDSRGNTVLHALVTVAdntkentkfvtRMYDMILIRGAKLCPT 197

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1830828474  146 -----MRNSRGETPLDLAAQYGRLQAVQMLIR 172
Cdd:cd22193    198 veleeIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-274 1.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474  222 LLAAG-VSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTALDI 274
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-165 1.32e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNL------------PDS--RGSSPLHLAAWAGETDIVRLLLTHPYRPATA--- 111
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTAdsl 207

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1830828474  112 -----NLQTIEQE-----TPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQ 165
Cdd:TIGR00870  208 gntllHLLVMENEfkaeyEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIV 271
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-255 1.54e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1830828474  205 TCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLL 255
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1025-1087 2.13e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 43.41  E-value: 2.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830828474 1025 TLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQtVLEINKLGHRRRILQSlayIRQMR 1087
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLK-RLGITSVGHRRKILKK---IQELK 66
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 94-272 2.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   94 ETDIVRLLLTHpyrPATANLQTIEQ-ETPLHCAAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIR 172
Cdd:PHA02878   146 EAEITKLLLSY---GADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  173 ahpeliahlaamergtrspSSPASPSRTIFPHTCLHLA-SRNGHKSVVEVLLAAGVSVNL------LTPSGTALHEaslc 245
Cdd:PHA02878   223 -------------------NGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAksyilgLTALHSSIKS---- 279

                          170       180
                   ....*....|....*....|....*..
gi 1830828474  246 gkENVVRTLLKAGIDLSATDNEGRTAL 272
Cdd:PHA02878   280 --ERKLKLLLEYGADINSLNSYKLTPL 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-79 2.50e-05

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: 42.28  E-value: 2.50e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1830828474   49 GYSALHHACL-NGHEDIVRLLLANDASPNLPD 79
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-177 6.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 6.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHAC-LNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLL------------ 102
Cdd:PHA02876   328 IMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLdygadiealsqk 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  103 -----------THPY--------RPATANLQTIEQETPLHCAAQHG-HTGALALLLGHDADPNMRNSRGETPLDLAAQYG 162
Cdd:PHA02876   408 igtalhfalcgTNPYmsvktlidRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYH 487

                          170
                   ....*....|....*
gi 1830828474  163 RLqaVQMLIRAHPEL 177
Cdd:PHA02876   488 GI--VNILLHYGAEL 500
PHA02946 PHA02946
ankyin-like protein; Provisional
 15-306 6.75e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   15 NISHIEKVLTQKAKRAGPLASLRRGTGVNVQDSGGYSALHHAC-LNG-HEDIVRLLLANDASPNLPDSRGSSPLHLAAWA 92
Cdd:PHA02946     3 NIMSAEYYLSLYAKYNSKNLDVFRNMLQAIEPSGNYHILHAYCgIKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   93 GETDIVRLLLTHPYRPataNLQTIEQETPLHcaaqhghtgalaLLLGHDADPNMRnsrgetpLDLAAQYGRLQAVQMLIR 172
Cdd:PHA02946    83 NNNRIVAMLLTHGADP---NACDKQHKTPLY------------YLSGTDDEVIER-------INLLVQYGAKINNSVDEE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  173 AHPELIAHLAAMERGTRSPSSPASPSRTIFP----HTCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHeaSLCGK 247
Cdd:PHA02946   141 GCGPLLACTDPSERVFKKIMSIGFEARIVDKfgknHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGnTPLH--IVCSK 218

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1830828474  248 --ENV-VRTLLKAGIDLSATDNEGRTALDILREF--PPHVTKHIVAVINNFRNQM-------DTDEVDEVI 306
Cdd:PHA02946   219 tvKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKTlsPAHLINKLLSTSNVITDQTvnicifyDRDDVLEII 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-292 9.50e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 9.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   64 IVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLTHpyrPATANLQTIEQETPLHCAAQHGHTGALALLLGHDAD 143
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY---GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  144 PN---------MRNSRGETPL------------DLAAQYGRLQAVQM--LIRAHPELiahlaaMERGTrspsspASPSRT 200
Cdd:PHA02876   237 INkndlsllkaIRNEDLETSLllydagfsvnsiDDCKNTPLHHASQApsLSRLVPKL------LERGA------DVNAKN 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  201 IFPHTCLHLASRNGHKSV-VEVLLAAGVSVNLL-TPSGTALHEASLCGK-ENVVRTLLKAGIDLSATDNEGRTALdilre 277
Cdd:PHA02876   305 IKGETPLYLMAKNGYDTEnIRTLIMLGADVNAAdRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPI----- 379

                          250
                   ....*....|....*
gi 1830828474  278 fpphvtkHIVAVINN 292
Cdd:PHA02876   380 -------HYAAVRNN 387
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-171 1.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   36 LRRGTGVNVQDSGGYSALHHACLNGHEDIVRLLLANDASPNLPDSRGSSPLHLAAWAGETDIVRLLLThpyrpATANLQT 115
Cdd:PHA02875   122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD-----SGANIDY 196

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830828474  116 IEQE---TPLHCAAQHGHTGALALLLGHDADPN-MRNSRGE--TPLDLAAQYG---RLQAVQMLI 171
Cdd:PHA02875   197 FGKNgcvAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDMICNMCtnlESEAIDALI 261
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 49-172 1.85e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 46.00  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   49 GYSALHHACLNGHEDIVRLLLANDASPNLPDSR-------------GSSPLHLAAWAGETDIVRLLLTHPYRPATANLQT 115
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQD 173

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830828474  116 IEQETPLHC----AAQHGHTGALA-------LLLGHDADPNMR-----NSRGETPLDLAAQYGRLQAVQMLIR 172
Cdd:cd22197    174 SLGNTVLHAlvmiADNSPENSALVikmydglLQAGARLCPTVQleeisNHEGLTPLKLAAKEGKIEIFRHILQ 246
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1026-1080 1.88e-04

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 40.69  E-value: 1.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1830828474 1026 LQQWLHSIALPEYLEFFNKHLYN--TIESVCgvwDVELQTvLEINKLGHRRRILQSL 1080
Cdd:cd09487      2 VAEWLESLGLEQYADLFRKNEIDgdALLLLT---DEDLKE-LGITSPGHRKKILRAI 54
PTB_X11 cd01208
X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is ...
 1190-1323 2.29e-04

X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is unknown to date. X11 has a PTB domain followed by two PDZ domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269919  Cd Length: 161  Bit Score: 43.05  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1190 LNEHINYEVQYLGSTVVKELRGTESTKKSIQKLKASGK-----GEGKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNI 1264
Cdd:cd01208      4 LIDGVIFGANYLGSTQLLSERNPSKNVRMAQAQEAVSRvkapeGESQPSTEVDLFISTERIKVLNADTQETMMDHALRTI 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1830828474 1265 -------------------NCACQDSEDLRHFAYITKEQDLHYCHVFQvqSTDlASEIILTLGQAFEVAYQLALR-DGI 1323
Cdd:cd01208     84 syiadignivvlmarrrmpRSSSQECVETTPPSQEGKRQYKMICHVFE--SED-AQLIAQSIGQAFSVAYQEFLRaNGI 159
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 1196-1311 2.50e-04

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains insects, ticks, sea urchins, and nematodes.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 42.32  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1196 YEVQYLGSTVVKELRGTESTKKS-IQKLKASGKGegKSGSPLSLAISHRGVEFIDVSSKRIICEHEIQNINCACQDSEDL 1274
Cdd:cd13160      3 FTVKYLGRMPARGLWGIKHTRKPlVDALKNLPKG--KTLPKTKLEVSSDGVKLEELRGGFGSSKTVFFPIHTISYGVQDL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1830828474 1275 RH---FAYITK-EQDLHY----CHVFQVQSTDLASEIILTLGQAF 1311
Cdd:cd13160     81 VHtrvFSMIVVgEQDSSNhpfeCHAFVCDSRADARNLTYWLAKAF 125
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-148 2.52e-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: 39.58  E-value: 2.52e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1830828474  119 ETPLHCAA-QHGHTGALALLLGHDADPNMRN 148
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-69 3.41e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 3.41e-04
                           10        20
                   ....*....|....*....|....*...
gi 1830828474   42 VNVQDSGGYSALHHACLNGHEDIVRLLL 69
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 204-231 4.61e-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: 38.72  E-value: 4.61e-04
                            10        20
                    ....*....|....*....|....*...
gi 1830828474   204 HTCLHLASRNGHKSVVEVLLAAGVSVNL 231
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-274 4.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 4.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1830828474  237 TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTALDI 274
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 120-146 9.62e-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: 37.95  E-value: 9.62e-04
                            10        20
                    ....*....|....*....|....*..
gi 1830828474   120 TPLHCAAQHGHTGALALLLGHDADPNM 146
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 108-223 9.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  108 PATANLQTIEQetpLHCAAQHGHTGALALLLGhDADPNMRNSRGETPLDLAAQYGRLQAVQMLIrahpELIAHLAAMERG 187
Cdd:PTZ00322    76 PVVAHMLTVEL---CQLAASGDAVGARILLTG-GADPNCRDYDGRTPLHIACANGHVQVVRVLL----EFGADPTLLDKD 147

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1830828474  188 TRspsspaspsrtifphTCLHLASRNGHKSVVEVLL 223
Cdd:PTZ00322   148 GK---------------TPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-274 1.11e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  125 AAQHGHTGALALLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLIRaHPELIaHLaamergtrspsspaspsRTIFPH 204
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNV-HI-----------------RDANGN 592

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474  205 TCLHLASRNGHKSVVEVLLAAGVSVNLLTpSGTALHEASLCGKENVVRTLLKAGIDLSATDNEGRTALDI 274
Cdd:PLN03192   593 TALWNAISAKHHKIFRILYHFASISDPHA-AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 208-277 1.24e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 1.24e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1830828474  208 HLASrNGHKSVVEVLLAAGVSVNLLTPSG-TALHEASLCGKENVVRTLLKAGIDLSATDNEGRTALDILRE 277
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
205-242 1.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1830828474  205 TCLHLASRNGHKSVVEVLLAAGVSVNLLTPSG-TALHEA 242
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGlTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-233 2.04e-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: 36.88  E-value: 2.04e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1830828474  204 HTCLHLAS-RNGHKSVVEVLLAAGVSVNLLT 233
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 1025-1087 2.58e-03

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 37.60  E-value: 2.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830828474 1025 TLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQTVlEINKLGHRRRILQSlayIRQMR 1087
Cdd:cd09546      5 SVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRL-GVTLVGHQKKIMNS---IQEMR 63
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 1025-1080 3.50e-03

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 37.51  E-value: 3.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1830828474 1025 TLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELQTvLEINKLGHRRRILQSL 1080
Cdd:cd09543      7 TVAEWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKH-IGVRLPGHQKRIAYSI 61
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 1028-1086 3.99e-03

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188947  Cd Length: 70  Bit Score: 37.31  E-value: 3.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1028 QWLHSIALPEYLEFFNKHLYNTIESVCGVwDVELQTVLEINKLGHRRRILQSLAYIR-QM 1086
Cdd:cd09548     12 EWLEAIKMERYKDNFTAAGYNSLESVARM-TIEDVMSLGITLVGHQKKIMSSIQTMRaQM 70
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-171 4.41e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 4.41e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1830828474  136 LLLGHDADPNMRNSRGETPLDLAAQYGRLQAVQMLI 171
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL 36
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 1023-1088 5.25e-03

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 36.85  E-value: 5.25e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474 1023 VATLQQWLHSIALPEYLEFFNKHLYNTIESVCGVWDVELqTVLEINKLGHRRRILQS----LAYIRQMRD 1088
Cdd:cd09545      3 VASVDDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDL-ARIGISAIAHQNKILSSvqgmRSQMQQMQG 71
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-146 5.55e-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: 35.70  E-value: 5.55e-03
                           10        20
                   ....*....|....*....|....*...
gi 1830828474  119 ETPLHCAAQHGHTGALALLLGHDADPNM 146
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-159 9.29e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474    1 MGKDQEFLEAARNGNISHIEKVLTQKakragplaslRRGtgvnvqdSGGYSALHHACLNGH---EDIVRLLLANDASPNL 77
Cdd:TIGR00870   51 LGRSALFVAAIENENLELTELLLNLS----------CRG-------AVGDTLLHAISLEYVdavEAILLHLLAAFRKSGP 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830828474   78 PD----------SRGSSPLHLAAWAGETDIVRLLLTHPYR-PATAN----LQTIEQ------ETPLHCAAQHGHTGALAL 136
Cdd:TIGR00870  114 LElandqytsefTPGITALHLAAHRQNYEIVKLLLERGASvPARACgdffVKSQGVdsfyhgESPLNAAACLGSPSIVAL 193

                          170       180
                   ....*....|....*....|...
gi 1830828474  137 LLGHDADPNMRNSRGETPLDLAA 159
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLV 216
 
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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