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Conserved domains on  [gi|767939589|ref|XP_011512737|]
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ankyrin repeat and SAM domain-containing protein 1A isoform X8 [Homo sapiens]

Protein Classification

SAM_AIDA1AB-like_repeat1 and PTB_Anks domain-containing protein( domain architecture ID 13332801)

protein containing domains PHA02791, SAM_AIDA1AB-like_repeat1, SAM_AIDA1AB-like_repeat2, and PTB_Anks

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 ...
 926-1071 1.74e-100

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: 313.83  E-value: 1.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  926 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 1005
Cdd:cd01274     1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589 1006 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1071
Cdd:cd01274    81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
72-285 1.29e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 1.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   72 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDNET 151
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGET 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  152 ALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVV 231
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  232 QVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALD 285
Cdd:COG0666   203 KLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 697-763 1.82e-37

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 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 SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-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: 188898  Cd Length: 67  Bit Score: 134.73  E-value: 1.82e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  697 LEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSNVMEEQDLRDIGISDPQHRRKLLQAARSLPKVK 763
Cdd:cd09499     1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 768-832 3.48e-36

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: 130.89  E-value: 3.48e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVQLLGHRKRIIASLADR 832
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 ...
 926-1071 1.74e-100

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: 313.83  E-value: 1.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  926 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 1005
Cdd:cd01274     1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589 1006 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1071
Cdd:cd01274    81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
72-285 1.29e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 1.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   72 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDNET 151
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGET 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  152 ALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVV 231
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  232 QVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALD 285
Cdd:COG0666   203 KLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 697-763 1.82e-37

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 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 SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-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: 188898  Cd Length: 67  Bit Score: 134.73  E-value: 1.82e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  697 LEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSNVMEEQDLRDIGISDPQHRRKLLQAARSLPKVK 763
Cdd:cd09499     1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 768-832 3.48e-36

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: 130.89  E-value: 3.48e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVQLLGHRKRIIASLADR 832
Cdd:cd09500     1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 938-1071 6.65e-36

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: 132.82  E-value: 6.65e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    938 ESCGYEANYLGSMLIKDLRGTESTQDACAKMRKS-TEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDP 1016
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589   1017 EDLCTFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQLALQAQKS 1071
Cdd:smart00462   82 DDLDVFGYIARDPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARSE 134
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-284 2.02e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.03  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLH---HAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGD-AQIVRLLIHQGpshTRVNEQ 145
Cdd:PHA03095   37 GADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG---ADVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  146 NNDNETALH--CAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDlaALYGR----LEVVKMLLNAHPNLLSCNTKKHTPL 219
Cdd:PHA03095  114 DKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  220 HLAARNGH--KAVVQVLLDAGMDSNYQTEMG-SALHEAALFG--KTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:PHA03095  192 HHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPL 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-179 2.03e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 2.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    84 LHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIhqgpSHTRVNEQNNdNETALHCAAQYGHTE 163
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 767939589   164 VVKVLLEELTDPTMRN 179
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 700-759 1.06e-14

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: 69.63  E-value: 1.06e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    700 SVGEWLESIGLQQYESKLLLNGFDDVHFLgsNVMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLL--LLTSEEDLKELGITKLGHRKKILKAIQKL 65
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
942-1061 1.60e-14

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.63  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   942 YEANYLGSM-------LIKDLRgTESTQDA--CAKM------RKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEI 1006
Cdd:pfam00640    1 FAVRYLGSVevpeeraPDKNTR-MQQAREAirRVKAakinkiRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  1007 RNIS-CAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDvnLTYEIILTLGQAFEVA 1061
Cdd:pfam00640   80 VSISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 768-829 2.08e-13

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: 66.14  E-value: 2.08e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589   768 DGNSPPSVPSWLDSLGLQDYVHSFlSSGYSSIDTVKNLWELELVNvLKVQLLGHRKRIIASL 829
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAI 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 699-759 3.56e-13

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: 65.37  E-value: 3.56e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589   699 QSVGEWLESIGLQQYEsKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:pfam00536    6 EDVGEWLESIGLGQYI-DSFRAGYIDGDALLQ--LTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 767-829 1.84e-11

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: 60.39  E-value: 1.84e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939589    767 YDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVkNLWELELVNVLKVQLLGHRKRIIASL 829
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL-LLTSEEDLKELGITKLGHRKKILKAI 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 149-284 1.07e-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: 56.17  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  149 NETALHCAAQYGHTEVVKVLLE-ELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLL-----SCNTKKHTPLHLA 222
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepmtSDLYQGETALHIA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  223 ARNGHKAVVQVLLDAGMDSNYQTEMGSA---------------LHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-108 3.12e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.12e-05
                            10        20
                    ....*....|....*....|....*....
gi 767939589     80 GYTPLHHAALNGHKDVVEVLLRNDALTNV 108
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 72-268 2.39e-04

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: 45.46  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    72 NVNCVDSTGYTPLHHAAL-NGHKDVVEVLLRNDALTNVADSKgcypLHLAAwKGDAQIVRLLI-HQGPSHTR------VN 143
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAIS-LEYVDAVEAILlHLLAAFRKsgplelAN 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   144 EQNNDNE----TALHCAAQYGHTEVVKVLLEELTD-----------PTMRNNKF---ETPLDLAALYGRLEVVKMLLNAH 205
Cdd:TIGR00870  119 DQYTSEFtpgiTALHLAAHRQNYEIVKLLLERGASvparacgdffvKSQGVDSFyhgESPLNAAACLGSPSIVALLSEDP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   206 PNLLSCNTKKHTPLHLAA-----RNGHKAVVQ------VLLDAGMDS--------NYQTEmgSALHEAALFGKTDVVQIL 266
Cdd:TIGR00870  199 ADILTADSLGNTLLHLLVmenefKAEYEELSCqmynfaLSLLDKLRDskelevilNHQGL--TPLKLAAKEGRIVLFRLK 276


                   ..
gi 767939589   267 LA 268
Cdd:TIGR00870  277 LA 278
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 926-1071 1.74e-100

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: 313.83  E-value: 1.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  926 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 1005
Cdd:cd01274     1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589 1006 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1071
Cdd:cd01274    81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
72-285 1.29e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 1.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   72 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDNET 151
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGET 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  152 ALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVV 231
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  232 QVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALD 285
Cdd:COG0666   203 KLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-284 3.88e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.68  E-value: 3.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDN 149
Cdd:COG0666    77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  150 ETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKA 229
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  230 VVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 697-763 1.82e-37

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 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 SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-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: 188898  Cd Length: 67  Bit Score: 134.73  E-value: 1.82e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  697 LEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSNVMEEQDLRDIGISDPQHRRKLLQAARSLPKVK 763
Cdd:cd09499     1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 768-832 3.48e-36

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: 130.89  E-value: 3.48e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVQLLGHRKRIIASLADR 832
Cdd:cd09500     1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 938-1071 6.65e-36

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: 132.82  E-value: 6.65e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    938 ESCGYEANYLGSMLIKDLRGTESTQDACAKMRKS-TEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDP 1016
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589   1017 EDLCTFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQLALQAQKS 1071
Cdd:smart00462   82 DDLDVFGYIARDPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 940-1058 1.79e-24

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: 99.51  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  940 CGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPT-IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPED 1018
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGpVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767939589 1019 LCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAF 1058
Cdd:cd00934    81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
142-284 1.75e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  142 VNEQNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHL 221
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767939589  222 AARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:COG0666    94 AARNGDLEIVKLLLEAGADVNARDKDGeTPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-284 2.02e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.03  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLH---HAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGD-AQIVRLLIHQGpshTRVNEQ 145
Cdd:PHA03095   37 GADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG---ADVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  146 NNDNETALH--CAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDlaALYGR----LEVVKMLLNAHPNLLSCNTKKHTPL 219
Cdd:PHA03095  114 DKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  220 HLAARNGH--KAVVQVLLDAGMDSNYQTEMG-SALHEAALFG--KTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:PHA03095  192 HHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPL 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-179 2.03e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 2.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    84 LHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIhqgpSHTRVNEQNNdNETALHCAAQYGHTE 163
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 767939589   164 VVKVLLEELTDPTMRN 179
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-277 6.21e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 6.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   186 LDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDaGMDSNYQTEMGSALHEAALFGKTDVVQI 265
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 767939589   266 LLAAGTDVNIKD 277
Cdd:pfam12796   80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-244 5.18e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 5.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   153 LHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNaHPNlLSCNTKKHTPLHLAARNGHKAVVQ 232
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HAD-VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 767939589   233 VLLDAGMDSNYQ 244
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-319 1.16e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 96.19  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshTRVNEQNNDN 149
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG---AYANVKDNNG 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  150 ETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNtkKHTPLHLAArnghka 229
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHAI------ 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  230 vvqvlldagmdsNYQTEMgsalheaalfgktDVVQILLAAGTDVNIKDNHGLTALDTVRELPSQKSqqiaaLIEDHMTGK 309
Cdd:PHA02874  263 ------------NPPCDI-------------DIIDILLYHKADISIKDNKGENPIDTAFKYINKDP-----VIKDIIANA 312

                         250
                  ....*....|
gi 767939589  310 RSTKEVDKTP 319
Cdd:PHA02874  313 VLIKEADKLK 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 70-279 3.80e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 94.73  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGH-----KDVVEVLLRNDALTNVADSKGCYPLHLAAWK--GDAQIVRLLIHQGpshTRV 142
Cdd:PHA03100   58 GADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG---ANV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  143 NEQNNDNETALHCAAQYGH--TEVVKVLLEELTDPTMRNNkfetpldlaalygrlevVKMLLNAHPNLLSCNTKKHTPLH 220
Cdd:PHA03100  135 NIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLH 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  221 LAARNGHKAVVQVLLDAGMDSNYQTEMGSA-LHEAALFGKTDVVQILLAAGTDVNIKDNH 279
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTpLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 930-1067 1.06e-18

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: 83.87  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  930 HQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMrKSTEHMK-----KIPTIILSITYKGVKFIDASNKNVIAEH 1004
Cdd:cd01273     2 HPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKL-KFARQLKksegaKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939589 1005 EIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFstVDVNLTYEIILTLGQAFEVAYQLALQ 1067
Cdd:cd01273    81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVF--DSEKLAEEITLTIGQAFDLAYRRFLE 141
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 69-243 2.09e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   69 RGPNVNCVDSTGYTPLHHAALN--GHKDVVEVLLRNDALTNVADSKGCYPLHLAAW--KGDAQIVRLLIHQG---PSHTR 141
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGvdiNAKNR 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  142 V----------NEQNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLlsc 211
Cdd:PHA03100  175 VnyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI--- 251

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767939589  212 NTKKHTPLHLAARN----------GHKAVVQVLLDAGMDSNY 243
Cdd:PHA03100  252 KTIIETLLYFKDKDlntitkikmlKKSIMYMFLLDPGFYKNR 293
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 71-304 1.45e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   71 PNVNCVDstGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshTRVNEQ-NNDN 149
Cdd:PHA02875   28 PNFEIYD--GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG---KFADDVfYKDG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  150 ETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLN--AHPNLLSCntKKHTPLHLAARNGH 227
Cdd:PHA02875  103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDhkACLDIEDC--CGCTPLIIAMAKGD 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  228 KAVVQVLLDAGMDSNYQTEMG--SALHEAALFGKTDVVQILLAAGTDVNIK---DNHGLTALDTVRELPSQ-KSQQIAAL 301
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADCNIMfmiEGEECTILDMICNMCTNlESEAIDAL 260


                  ...
gi 767939589  302 IED 304
Cdd:PHA02875  261 IAD 263
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 696-753 2.11e-15

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 71.78  E-value: 2.11e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939589  696 TLEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSnVMEEqDLRDIGISDPQHRRKLL 753
Cdd:cd09491     3 SWPKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSD-ITEE-DLEEAGVTNPAHKRRLL 58
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 700-759 1.06e-14

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: 69.63  E-value: 1.06e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    700 SVGEWLESIGLQQYESKLLLNGFDDVHFLgsNVMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLL--LLTSEEDLKELGITKLGHRKKILKAIQKL 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 99-284 1.27e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   99 LLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshTRVNEQNNDNETALHCAAQYGHT-----EVVKVLLEELT 173
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNG---ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  174 DPTMRNNKFETPLDLAALY--GRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGH------------------KAVVQV 233
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidlkilkllidkgvdinaKNRVNY 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767939589  234 LLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:PHA03100  178 LLSYGVPINIKDVYGfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
942-1061 1.60e-14

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.63  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   942 YEANYLGSM-------LIKDLRgTESTQDA--CAKM------RKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEI 1006
Cdd:pfam00640    1 FAVRYLGSVevpeeraPDKNTR-MQQAREAirRVKAakinkiRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  1007 RNIS-CAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDvnLTYEIILTLGQAFEVA 1061
Cdd:pfam00640   80 VSISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 81-243 1.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   81 YTPLHHAALNGHKDVVEVLLR--------------------------------------NDALTNVADSKGCYPLHLAAW 122
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDngadinsstknnstplhylsnikynltdvkeivkllleYGANVNAPDNNGITPLLYAIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  123 K--GDAQIVRLLIHQGpshTRVNEQNNDNETALHCAAQYGHTEV------------------VKVLLEELTDPTMRNNKF 182
Cdd:PHA03100  116 KksNSYSIVEYLLDNG---ANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYG 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939589  183 ETPLDLAALYGRLEVVKMLLN--AHPNLlsCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNY 243
Cdd:PHA03100  193 FTPLHYAVYNNNPEFVKYLLDlgANPNL--VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 942-1063 1.94e-14

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: 70.74  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  942 YEANYLGSMLIKDLRGTESTQDACAKMRksteHMKKIPT-IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDLC 1020
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRLK----DLKLKPKpVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767939589 1021 TFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQ 1063
Cdd:cd13161    80 LFAFISHDPRLGRITCHVFRCKRGA--QEICDTIAEAFKAAAE 120
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 942-1059 1.86e-13

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: 68.13  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  942 YEANYLGSMLIKDLRGTESTQDACA---KMRKSTEhmKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNIS-CAAqDPE 1017
Cdd:cd13159     5 FYLKYLGSTLVEKPKGEGATAEAVKtiiAMAKASG--KKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISyCTA-DAN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767939589 1018 DLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFE 1059
Cdd:cd13159    82 HDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 768-829 2.08e-13

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: 66.14  E-value: 2.08e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589   768 DGNSPPSVPSWLDSLGLQDYVHSFlSSGYSSIDTVKNLWELELVNvLKVQLLGHRKRIIASL 829
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAI 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 699-759 3.56e-13

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: 65.37  E-value: 3.56e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589   699 QSVGEWLESIGLQQYEsKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:pfam00536    6 EDVGEWLESIGLGQYI-DSFRAGYIDGDALLQ--LTEDDLLKLGVTLLGHRKKILYAIQRL 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 70-202 3.86e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWK-GDAQIVRLLIHQGpshTRVNEQNN- 147
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG---VDVNAKSYi 267

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  148 DNETALHCAAQygHTEVVKVLLEELTDPTMRNNKFETPLDLAAL-YGRLEVVKMLL 202
Cdd:PHA02878  268 LGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
163-284 4.44e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  163 EVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSN 242
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767939589  243 YQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:COG0666    82 AKDDGGnTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 70-274 7.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 7.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGH-KDVVEVLLRNDALTNVADSKGCYPLHLAAWKG-DAQIVRLLIHQGPShtrVNEQNN 147
Cdd:PHA02876  263 GFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGAD---VNAADR 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  148 DNETALHCAAQYG-HTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLA--AR 224
Cdd:PHA02876  340 LYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGT 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767939589  225 NGHKAvVQVLLDAGMDSNYQTE-MGSALHEAALFG-KTDVVQILLAAGTDVN 274
Cdd:PHA02876  420 NPYMS-VKTLIDRGANVNSKNKdLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
699-759 9.71e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.13  E-value: 9.71e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589   699 QSVGEWLESIGLQQYESKLLLNGFD-DVHFLGsnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:pfam07647    7 ESVADWLRSIGLEQYTDNFRDQGITgAELLLR---LTLEDLKRLGITSVGHRRKILKKIQEL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 767-829 1.84e-11

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: 60.39  E-value: 1.84e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939589    767 YDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVkNLWELELVNVLKVQLLGHRKRIIASL 829
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL-LLTSEEDLKELGITKLGHRKKILKAI 62
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 700-757 2.08e-11

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: 59.95  E-value: 2.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLgsnVMEEQDLRDIGISDPQHRRKLLQAAR 757
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALL---LLTDEDLKELGITSPGHRKKILRAIQ 55
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 90-286 3.06e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   90 NGHKDVVEVLLRNDA-LTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshTRVNEQNNDNETALHCAAQYGHTEVVKVL 168
Cdd:PHA02874   11 SGDIEAIEKIIKNKGnCINISVDETTTPLIDAIRSGDAKIVELFIKHG---ADINHINTKIPHPLLTAIKIGAHDIIKLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  169 LEELTDPTM-----------------------RNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARN 225
Cdd:PHA02874   88 IDNGVDTSIlpipciekdmiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  226 GHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALDT 286
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGeSPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 926-1043 3.11e-11

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: 61.94  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  926 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTehmKKIPTIILSITYKGVKFIDASNKNVIAEHE 1005
Cdd:cd01268     1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASR---KKPVRAVLWVSGDGLRVVDEKTKGLIVDQT 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767939589 1006 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVD 1043
Cdd:cd01268    78 IEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVK 115
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 69-240 3.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   69 RGPNVNCVDSTGYTPLHHAA-LNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNN 147
Cdd:PHA02876  330 LGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  148 dneTALHCAAqYGHTEV--VKVLLEELTDPTMRNNKFETPLDLAALYG-RLEVVKMLLNAHPNLLSCNTKKHTPLHLAAr 224
Cdd:PHA02876  410 ---TALHFAL-CGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL- 484

                         170
                  ....*....|....*.
gi 767939589  225 nGHKAVVQVLLDAGMD 240
Cdd:PHA02876  485 -EYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-202 8.44e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 8.44e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767939589   151 TALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLL 202
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 944-1062 9.11e-11

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: 60.48  E-value: 9.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  944 ANYLGSMLIKDLrgteSTQDACAKMRKSTEHMKKIPT----IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDl 1019
Cdd:cd13157     6 AQYIGSFPVSGL----DVADRADSVRKQLESLKESGSrgrpVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767939589 1020 CTFAYITKDLQ--TSHHYCHVFSTVDVNLTYEIILTLGQAFEVAY 1062
Cdd:cd13157    81 AQFAFVARNPGgpTNRQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PHA03095 PHA03095
ankyrin-like protein; Provisional
 163-285 1.17e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  163 EVVKVLLEELTDPTMRNNKFETPLDLAALYG---RLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKA-VVQVLLDAG 238
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767939589  239 MDSNYQTEMG-SALHeAALFGK---TDVVQILLAAGTDVNIKDNHGLTALD 285
Cdd:PHA03095  108 ADVNAKDKVGrTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLA 157
SAM_SASH-like cd09493
SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like ...
 699-758 3.72e-10

SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. Proteins of this subfamily are known to be involved in preventing DN thymocytes from premature initiation of programmed cell death and in B cells activation and differentiation. They have been found downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues.


Pssm-ID: 188892  Cd Length: 60  Bit Score: 56.74  E-value: 3.72e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLgsNVMEEQDLRDIGISDPQHRRKLLQAARS 758
Cdd:cd09493     3 KTVEELLERINLQEHTSTLLLNGYETLEDF--KDLKESHLNELNITDPEHRAKLLTAAEL 60
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 70-224 4.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 4.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVD-STGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNND 148
Cdd:PHA02878  157 GADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKC 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  149 NETALHCAAQY-GHTEVVKVLLEELTDPtmrnNKFETPLDLAALYGRL---EVVKMLLN--AHPNLLscNTKKHTPLHLA 222
Cdd:PHA02878  234 GNTPLHISVGYcKDYDILKLLLEHGVDV----NAKSYILGLTALHSSIkseRKLKLLLEygADINSL--NSYKLTPLSSA 307


                  ..
gi 767939589  223 AR 224
Cdd:PHA02878  308 VK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 83-284 4.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   83 PLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQ------GPSHTRVNEQNNDNETALH-- 154
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvFYTLVAIKDAFNNRNVEIFki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  155 -----------------CAAQYG---HTEVVKVLLEELTDPTMRN-NKFETPLDLAALYGRLEVVKMLL--NAHPNLLsc 211
Cdd:PHA02878  120 iltnrykniqtidlvyiDKKSKDdiiEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLsyGANVNIP-- 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  212 NTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMGSA-LHEAALFGKT-DVVQILLAAGTDVNIKDN-HGLTAL 284
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTpLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTAL 273
PHA03095 PHA03095
ankyrin-like protein; Provisional
 69-284 9.10e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 9.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   69 RGPNVNCVDSTGYTPLHhaalnghkdvveVLLRNdalTNVadskgcyplhlaawkgDAQIVRLLIHQGPSHTRVneqNND 148
Cdd:PHA03095  141 KGADVNALDLYGMTPLA------------VLLKS---RNA----------------NVELLRLLIDAGADVYAV---DDR 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  149 NETALHCAAQYGHT--EVVKVLLEELTDPTMRNNKFETPLDLAALYGrlevvkmllnahpnllSCNtkkhtplhlaarng 226
Cdd:PHA03095  187 FRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGS----------------SCK-------------- 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939589  227 hKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:PHA03095  237 -RSLVLPLLIAGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-287 1.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   69 RGPNVNCVDSTGYTPLH----HAALNGHKDVVEVLLRND-ALTNVADSKGCY--------PLHLAAWKG----------- 124
Cdd:PHA02878   59 RGHNVNQPDHRDLTPLHiickEPNKLGMKEMIRSINKCSvFYTLVAIKDAFNnrnveifkIILTNRYKNiqtidlvyidk 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  125 -------DAQIVRLLIHQGpSHTRVNEQNNDNeTALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEV 197
Cdd:PHA02878  139 kskddiiEAEITKLLLSYG-ADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPI 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  198 VKMLLNAHPNLLSCNTKKHTPLHLA-ARNGHKAVVQVLLDAGMDSNYQTEMG--SALHEAalFGKTDVVQILLAAGTDVN 274
Cdd:PHA02878  217 VHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILglTALHSS--IKSERKLKLLLEYGADIN 294

                         250
                  ....*....|...
gi 767939589  275 IKDNHGLTALDTV 287
Cdd:PHA02878  295 SLNSYKLTPLSSA 307
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 980-1067 1.74e-09

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: 57.99  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  980 TIILSITYKGVKFIDASNKNVIAEHEIRNISCAA-QDPEDLCTFAYITKDlQTSHHYCHVFSTVDvNLTYEIILTLGQAF 1058
Cdd:cd01209    84 NISLTISTDGLNLVTPDTGQIIANHHMQSISFASgGDPDTYDYVAYVAKD-PVNQRACHVLECGD-GLAQDVIATIGQAF 161


                  ....*....
gi 767939589 1059 EVAYQLALQ 1067
Cdd:cd01209   162 ELRFKQYLK 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-133 1.77e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767939589    80 GYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLI 133
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 95-277 1.95e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   95 VVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDNETALHCAAQYGHTEVVKVLLEELTD 174
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD---VNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  175 ---------PTMRNNKFE--------------------TPLDLAALYGRL-EVVKMLLNAHPNLLSCNTKKHTPLHLAAR 224
Cdd:PHA02876  237 inkndlsllKAIRNEDLEtslllydagfsvnsiddcknTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  225 NGHKAV-VQVLLDAGMDSNYQTEM-GSALHEAALFGK-TDVVQILLAAGTDVNIKD 277
Cdd:PHA02876  317 NGYDTEnIRTLIMLGADVNAADRLyITPLHQASTLDRnKDIVITLLELGANVNARD 372
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 771-829 1.98e-09

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 54.54  E-value: 1.98e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939589  771 SPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVQLLGHRKRIIASL 829
Cdd:cd09488     1 AFRSVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTR-LGVTLVGHQKKILNSI 58
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 69-202 4.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   69 RGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKgDAQIVRLLIhqgpSHTRVNEQNND 148
Cdd:PHA02874  179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI----NNASINDQDID 253

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  149 NETALHCAAQYG-HTEVVKVLLEELTDPTMRNNKFETPLDLAALY-GRLEVVKMLL 202
Cdd:PHA02874  254 GSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-235 7.75e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767939589   184 TPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLL 235
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 769-826 9.55e-09

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: 53.07  E-value: 9.55e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  769 GNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNL-WE-LElvnVLKVQLLGHRKRII 826
Cdd:cd09498     4 DYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLtWEdLQ---DIGITKLGHQKKLM 60
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-169 1.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767939589   116 PLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDNETALHCAAQYGHTEVVKVLL 169
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 768-829 1.38e-08

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: 52.53  E-value: 1.38e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASL 829
Cdd:cd09543     1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNSIDKVLQM-TQEDIKHIGVRLPGHQKRIAYSI 61
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-120 1.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 1.56e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767939589    72 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLA 120
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 701-759 1.63e-08

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 52.06  E-value: 1.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939589  701 VGEWLESIGLQQYESKLLLNGFDDVHFlgSNVMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09527     5 VYDWLRTLQLEQYAEKFVDNGYDDLEV--CKQIGDPDLDAIGVMNPAHRKRILEAVRRL 61
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
767-831 2.20e-08

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 51.89  E-value: 2.20e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589   767 YDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASLAD 831
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRL-TLEDLKRLGITSVGHRRKILKKIQE 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 118-202 2.55e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  118 HLAAwKGDAQIVRLLIHQGPShtrVNEQNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEV 197
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGAD---PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163


                  ....*
gi 767939589  198 VKMLL 202
Cdd:PTZ00322  164 VQLLS 168
SAM_SAMSN1 cd09561
SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as ...
 695-759 2.80e-08

SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as HACS1 or NASH1) proteins is a predicted protein-protein interaction domain. Members of this group are putative signaling/adaptor proteins. They appear to mediate signal transduction in lymphoid tissues. Murine HACS1 protein likely plays a role in B cell activation and differentiation. Potential binding partners of HACS1 are SLAM, DEC205 and PIR-B receptors and also some unidentified tyrosine-phosphorylated proteins. Proteins of this group were found preferentially expressed in normal hematopietic tissues and in some malignancies including lymphoma, myeloid leukemia and myeloma.


Pssm-ID: 188960  Cd Length: 66  Bit Score: 51.40  E-value: 2.80e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  695 RTLEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09561     2 RPKPKTLQELLERIHLQEYTSTLLLNGYETLEDLKD--LKESHLIELNITDPEDRARLLSAAENL 64
SAM_SASH1_repeat2 cd09492
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ...
 700-759 7.39e-08

SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.


Pssm-ID: 188891  Cd Length: 70  Bit Score: 50.59  E-value: 7.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09492     9 SVSDWLVSIGLPMYSPPLLEAGFSTLSRVSS--LSETCLREAGITEERHIRKLLSAARLV 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-338 8.33e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 8.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  125 DAQIVRLLIHQGPSHTRVNEQNNdnetaLHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNA 204
Cdd:PLN03192  506 DLNVGDLLGDNGGEHDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  205 HPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEmGSALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:PLN03192  581 ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAA-GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATAL 659

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  285 ---------DTVRELPSQKSQQIAALIEDHMTG--------KR----STKEVDKTPPPQPPLISSMDSISQKSQG 338
Cdd:PLN03192  660 qvamaedhvDMVRLLIMNGADVDKANTDDDFSPtelrellqKRelghSITIVDSVPADEPDLGRDGGSRPGRLQG 734
Ank_4 pfam13637
Ankyrin repeats (many copies);
217-267 8.97e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 8.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767939589   217 TPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILL 267
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-189 1.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.00e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939589   132 LIHQGPShtRVNEQNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLA 189
Cdd:pfam13857    1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 149-284 1.07e-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: 56.17  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  149 NETALHCAAQYGHTEVVKVLLE-ELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLL-----SCNTKKHTPLHLA 222
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepmtSDLYQGETALHIA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  223 ARNGHKAVVQVLLDAGMDSNYQTEMGSA---------------LHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 942-1078 1.34e-07

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269968  Cd Length: 179  Bit Score: 52.67  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  942 YEANYLGSMLIKdlRGTeSTQDACAKMR------KSTEHMKKIPTIILSITykGVKFI-----------DASNKNVIAEH 1004
Cdd:cd01270    31 FQAKYIGSLEVP--RPS-SRVEIVAAMRriryefKAKNIKKKKVTITVSVD--GVKVVlrkkkkkkgwtWDESKLLLMQH 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767939589 1005 EIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKSRATGASA 1078
Cdd:cd01270   106 PIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEVCHKLSLQHMQGNADDEAE 179
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 774-829 2.37e-07

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 48.73  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASL 829
Cdd:cd09547     5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRM-TIDDIRRIGVTLIGHQRRIVSSI 59
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 774-831 2.62e-07

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: 48.77  E-value: 2.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASLAD 831
Cdd:cd09546     5 SVGEWLEAIKMGRYTEIFMENGYSSMDAVAQV-TLEDLRRLGVTLVGHQKKIMNSIQE 61
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 942-1035 2.72e-07

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: 51.10  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  942 YEANYLGSMLIKDLRGTESTQDACAKM----RKSTEHMKKIptiILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPE 1017
Cdd:cd01215    18 FKAKLIGIDEVPAARGDKMCQDAMMKLkgavKAAGEHKQRI---WLNISLEGIKILDEKTGALLHHHPVHKISFIARDTT 94

                          90
                  ....*....|....*...
gi 767939589 1018 DLCTFAYITKdLQTSHHY 1035
Cdd:cd01215    95 DNRAFGYVCG-LDGGHRF 111
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 87-249 6.20e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 6.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   87 AALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshTRVNEQNNDNETALHCAAQYGHTEVVK 166
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA---CNVHIRDANGNTALWNAISAKHHKIFR 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  167 VL--LEELTDPTMRNNKfetpLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMD---S 241
Cdd:PLN03192  609 ILyhFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkA 684


                  ....*...
gi 767939589  242 NYQTEMGS 249
Cdd:PLN03192  685 NTDDDFSP 692
PHA02791 PHA02791
ankyrin-like protein; Provisional
 77-247 6.90e-07

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 52.35  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   77 DSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKgcYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNNdneTALHCA 156
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGN---TALYYA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  157 AQYGHTEVVKVLLEELTDPTMRNNK-FETPLDLAALYGRLEVVKMLLNAHPN------LLSCntkkhtpLHLAARNGHKA 229
Cdd:PHA02791  102 VDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFYHAVMLNDVSIVSYFLSEIPStfdlaiLLSC-------IHITIKNGHVD 174

                         170
                  ....*....|....*...
gi 767939589  230 VVQVLLDAGMDSNYQTEM 247
Cdd:PHA02791  175 MMILLLDYMTSTNTNNSL 192
Ank_5 pfam13857
Ankyrin repeats (many copies);
234-285 7.11e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 7.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767939589   234 LLDAG-MDSNYQTEMG-SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALD 285
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
69-133 1.13e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589   69 RGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLI 133
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-208 1.15e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGHKD--VVEVLLRNDALTNVADSKGCYPLHLAAWKGD--AQIVRLLIHQGPShtrVNEQ 145
Cdd:PHA03095  177 GADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGIS---INAR 253

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939589  146 NNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNL 208
Cdd:PHA03095  254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 700-759 1.42e-06

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: 46.90  E-value: 1.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSNVMEeqDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09498     9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWE--DLQDIGITKLGHQKKLMLAIKKL 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-169 1.53e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   77 DSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPL-------H------------------------LAAWKGD 125
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasisdphaagdllcTAAKRND 634

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767939589  126 AQIVRLLIHQGpshTRVNEQNNDNETALHCAAQYGHTEVVKVLL 169
Cdd:PLN03192  635 LTAMKELLKQG---LNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
SAM_SASH1_repeat1 cd09559
SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins ...
 699-759 1.54e-06

SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.


Pssm-ID: 188958  Cd Length: 66  Bit Score: 46.55  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLgsNVMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09559     4 KSVEDLLDRINLKEHMPTFLFNGYEDLDTF--KLLEEEDLDELNIRDPEHRAVLLTAVELL 62
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-139 2.56e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   70 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSH 139
Cdd:PTZ00322  105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
SAM_SASH3 cd09560
SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) ...
 695-759 2.73e-06

SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative signaling/adaptor proteins. In addition to SAM, they contain SLY and SH3 domains. They appear to mediate signal transduction in lymphoid tissues. Murine SASH3 is involved in preventing DN thymocytes from premature initiation of programmed cell death and in mTOR (mammalian target of rapamycin) activation via signal integration of the Notch receptor and preTCR (T cell receptor) pathways.


Pssm-ID: 188959  Cd Length: 68  Bit Score: 45.85  E-value: 2.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  695 RTLEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09560     2 RPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKE--LRETHLNELNIMDPQHRAKLLTAAELL 64
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 768-831 5.14e-06

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 45.41  E-value: 5.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVQLLGHRKRIIASLAD 831
Cdd:cd09553     2 DYTTFTTVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRI-GVTLAGHQKKILSSIQD 64
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 966-1063 6.05e-06

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: 47.27  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  966 AKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIA-------EHEIRNIS-CAAQdPEDLCTFAYITK--DLQTSHhy 1035
Cdd:cd01212    32 ATARRLTVHLRPPQSCILEISDRGLKMVDRSKPNKKDgkpcihyFYSLKNISfCGFH-PRNSRYFGFITKhpLLQRFA-- 108

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767939589 1036 CHVF----STVDVNltyEIIltlGQAFEVAYQ 1063
Cdd:cd01212   109 CHVFvsqeSTRPVA---ESV---GRAFQRFYQ 134
Ank_4 pfam13637
Ankyrin repeats (many copies);
70-100 6.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 6.33e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767939589    70 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLL 100
Cdd:pfam13637   24 GADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 80-235 7.47e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 7.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   80 GYTPLHHAALNGHKDVVEVLLRND-ALTNVADS----KGCYPLHLAAWKGDAQIVRLLIHQGPS--HTRVN----EQNND 148
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADvvSPRATgtffRPGPK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  149 N-----ETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVK----MLLNAHPNLLSC------NT 213
Cdd:cd22192   131 NliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDDLQpldlvpNN 210

                         170       180
                  ....*....|....*....|..
gi 767939589  214 KKHTPLHLAARNGHKAVVQVLL 235
Cdd:cd22192   211 QGLTPFKLAAKEGNIVMFQHLV 232
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-759 8.96e-06

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 44.47  E-value: 8.96e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09549     9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVAR--MTAQDVLSLGITSLEHQELLLAGIQAL 66
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 80-203 9.41e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.76  E-value: 9.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   80 GYTPLHHAALNGHKDVVEVLLRNDALTNvADSKGC---------------YPLHLAAWKGDAQIVRLLIHQGpsHTRVNE 144
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVN-AHAKGVffnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE--STDITS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  145 QNNDNETALHCAAQYG-----HTEVVKVLLEELTD-------PTMRNNKFETPLDLAALYGRLEVVKMLLN 203
Cdd:cd22194   218 QDSRGNTVLHALVTVAedsktQNDFVKRMYDMILLksenknlETIRNNEGLTPLQLAAKMGKAEILKYILS 288
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 144-247 1.49e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.37  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  144 EQNNDNETALHCAAQYGHTEVVKVLLEELTD-----------PTMRNNKF---ETPLDLAALYGRLEVVKMLL-NAHPNL 208
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvffnPKYKHEGFyfgETPLALAACTNQPEIVQLLMeKESTDI 215

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767939589  209 LSCNTKKHTPLHlaarnghkAVVQVLLDAGMDSNYQTEM 247
Cdd:cd22194   216 TSQDSRGNTVLH--------ALVTVAEDSKTQNDFVKRM 246
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 941-1058 1.85e-05

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: 45.40  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  941 GYEANYLGSMLIKDLRGTESTQDACAKMRKStEHMKKIP-TIILSITykGVKFIDASNKNVIAEHEIRNISCAAQDPEDL 1019
Cdd:cd13168     2 LYKALYLGQVEVGEDGGVEQIESAAIIVVLE-SDLTPKEvLLELGEI--GVTVWDKSTSEVLFKHSFPEISSCGRRVDDP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767939589 1020 CTFAYITKDLQTS---HHYCHVFSTVDVNLTYEIILTLGQAF 1058
Cdd:cd13168    79 NYFAYIAGDTPCSlakHFVCYVFEAADEEEAETILQGIAQGF 120
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 125-286 1.88e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 48.75  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  125 DAQIVRLLIHQGpshTRVNEQNNDNETALHCAAQYGH--TEVVKVLLEELTDPTMRNNKFETPLdLAALYGRLEVVKMLL 202
Cdd:PHA02716  191 DIDILEWLCNNG---VNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPI-MTYIINIDNINPEIT 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  203 NAHPNLLSCNTKKHTP--LHL---AARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAAL--FGKTDVVQILLAAGTDVN 274
Cdd:PHA02716  267 NIYIESLDGNKVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGrTCLHQYILrhNISTDIIKLLHEYGNDLN 346

                         170
                  ....*....|..
gi 767939589  275 IKDNHGLTALDT 286
Cdd:PHA02716  347 EPDNIGNTVLHT 358
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-759 2.22e-05

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: 43.40  E-value: 2.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDD----VHflgsnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09545     5 SVDDWLQAIKMERYKDNFTAAGYTTleavVH------MNQDDLARIGISAIAHQNKILSSVQGM 62
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 774-829 2.37e-05

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 43.31  E-value: 2.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVQLLGHRKRIIASL 829
Cdd:cd09554     5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLR-MGVTLAGHQKKILSSI 59
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 700-753 2.64e-05

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 42.99  E-value: 2.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGF---DDVhflgsNVMEEQDLRDIGISDPQHRRKLL 753
Cdd:cd09488     4 SVGEWLESIKMGRYKENFTAAGYtslDAV-----AQMTAEDLTRLGVTLVGHQKKIL 55
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 768-829 2.78e-05

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: 43.09  E-value: 2.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASL 829
Cdd:cd09548     3 DFTSFCSVGEWLEAIKMERYKDNFTAAGYNSLESVARM-TIEDVMSLGITLVGHQKKIMSSI 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-108 3.12e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.12e-05
                            10        20
                    ....*....|....*....|....*....
gi 767939589     80 GYTPLHHAALNGHKDVVEVLLRNDALTNV 108
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-759 3.13e-05

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 42.95  E-value: 3.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09547     5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSR--MTIDDIRRIGVTLIGHQRRIVSSIQTL 62
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 774-829 3.23e-05

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 42.93  E-value: 3.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASL 829
Cdd:cd09550     4 SVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRM-NIEDIRRLGITLMGHQKKILTSI 58
Ank_2 pfam12796
Ankyrin repeats (3 copies);
251-290 3.27e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 3.27e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767939589   251 LHEAALFGKTDVVQILLAAGTDVNIKDNHGLTAL---------DTVREL 290
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALhlaaknghlEIVKLL 49
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 701-759 3.47e-05

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 42.78  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  701 VGEWLESIGLQQYESKLLLNgfdDVHflGSNVM--EEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09507    10 VGAWLESLQLGEYRDIFARN---DIR--GSELLhlERRDLKDLGITKVGHVKRILQAIKDL 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 80-104 3.58e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 3.58e-05
                           10        20
                   ....*....|....*....|....*
gi 767939589    80 GYTPLHHAALNGHKDVVEVLLRNDA 104
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGA 26
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 774-829 3.77e-05

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 42.69  E-value: 3.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGyssIDTVKNLWEL--ELVNVLKVQLLGHRKRIIASL 829
Cdd:cd09542     6 SVSEWLESIRMKRYILHFRSAG---LDTMECVLELtaEDLTQMGITLPGHQKRILCSI 60
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 699-758 4.24e-05

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 42.60  E-value: 4.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLGsnvMEEQDL-RDIGISDPQHRRKLLQAARS 758
Cdd:cd09563     7 EQVCDWLAELGLGQYVDECRRWVKSGQTLLK---ASPQELeKELGIKHPLHRKKLQLALQA 64
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 703-754 5.01e-05

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 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 apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 42.25  E-value: 5.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767939589  703 EWLESIGLQQYESKLLLNGFDdvhfLGS-NVMEEQDLRDIGISDPQHRRKLLQ 754
Cdd:cd09497     9 DWLREFGLEEYTPNFIKAGYD----LPTiSRMTPEDLTAIGITKPGHRKKLKS 57
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-759 5.75e-05

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 42.33  E-value: 5.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09553     8 TVGDWLDAIKMGRYKENFVSAGFASFDLVAQ--MTAEDLLRIGVTLAGHQKKILSSIQDM 65
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 111-285 5.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  111 SKGCYPLHLAAWKGDAQIVRLLIhqgpshTRVNEQNNDNETALH-CAAQ-YGHTEVVKVLLEELTDPT--MRNNKFeTPL 186
Cdd:PHA02859   19 YRYCNPLFYYVEKDDIEGVKKWI------KFVNDCNDLYETPIFsCLEKdKVNVEILKFLIENGADVNfkTRDNNL-SAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  187 DLAALYGR---LEVVKMLLNAHPNLLSCNTKKHTPLH--LAARNGHKAVVQVLLDAGMDS-NYQTEMGSALHEAALFGKT 260
Cdd:PHA02859   92 HHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFlNKDFDNNNILYSYILFHSD 171

                         170       180
                  ....*....|....*....|....*.
gi 767939589  261 D-VVQILLAAGTDVNIKDNHGLTALD 285
Cdd:PHA02859  172 KkIFDFLTSLGIDINETNKSGYNCYD 197
Ank_5 pfam13857
Ankyrin repeats (many copies);
174-222 5.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 5.95e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767939589   174 DPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLA 222
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_SARM1-like_repeat2 cd09502
SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like ...
 703-757 6.47e-05

SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188901  Cd Length: 70  Bit Score: 42.28  E-value: 6.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  703 EWLESIG--LQQYESKLLLNGFDDVHFlgSNVMEEQDLRDIGISDPQHRRKLLQAAR 757
Cdd:cd09502    12 NWLQSLGpeYSQYTYQMLNAGIDRNSL--PSLTEDQLLEDCGITNGIHRLRILNAIK 66
Ank_5 pfam13857
Ankyrin repeats (many copies);
201-254 6.50e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589   201 LLNAHPNLLSC-NTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEA 254
Cdd:pfam13857    1 LLEHGPIDLNRlDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGlTALDLA 56
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 768-829 6.92e-05

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 41.95  E-value: 6.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVQLLGHRKRIIASL 829
Cdd:cd09551     2 DFTAFTSVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRI-GVTLAGHQKKILNSI 62
PTB_X11 cd01208
X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is ...
 944-1068 6.99e-05

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: 44.59  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  944 ANYLGSMLIKdlrgTESTQDACAKMRKSTEHMKKIPT----------IILSITYKGVKFIDASNKNVIAEHEIRNISCAA 1013
Cdd:cd01208    12 ANYLGSTQLL----SERNPSKNVRMAQAQEAVSRVKApegesqpsteVDLFISTERIKVLNADTQETMMDHALRTISYIA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589 1014 -----------------QDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLtyeIILTLGQAFEVAYQLALQA 1068
Cdd:cd01208    88 dignivvlmarrrmprsSSQECVETTPPSQEGKRQYKMICHVFESEDAQL---IAQSIGQAFSVAYQEFLRA 156
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 768-829 7.42e-05

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 41.92  E-value: 7.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  768 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVQLLGHRKRIIASL 829
Cdd:cd09552     2 DYTSFSTVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRV-GVTLAGHQKKILNSI 62
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 699-759 9.42e-05

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: 41.46  E-value: 9.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09546     4 RSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQ--VTLEDLRRLGVTLVGHQKKIMNSIQEM 62
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 775-825 9.48e-05

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 41.28  E-value: 9.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767939589  775 VPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELvNVLKVQLLGHRKRI 825
Cdd:cd09527     5 VYDWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDL-DAIGVMNPAHRKRI 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 80-203 9.52e-05

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: 46.54  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   80 GYTPLHHAALNGHKDVVEVLLRNDAltNVADSKGC----------------YPLHLAAWKGDAQIVRLLIHQGPShTRVn 143
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGA--DVVSPRATgtffrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGAD-IRA- 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  144 eQNNDNETALHCAAQYGHTEVVKVLLE-------ELTDP---TMRNNKFETPLDLAALYGRLEVVKMLLN 203
Cdd:cd22192   165 -QDSLGNTVLHILVLQPNKTFACQMYDlilsydkEDDLQpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-243 1.05e-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: 40.26  E-value: 1.05e-04
                            10        20
                    ....*....|....*....|....*...
gi 767939589    216 HTPLHLAARNGHKAVVQVLLDAGMDSNY 243
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 699-752 1.40e-04

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: 41.36  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLgsNVMEEQDLRDIGISDPQHRRKL 752
Cdd:cd09543     6 RTVAEWLESIKMQQYTEHFMAAGYNSIDKV--LQMTQEDIKHIGVRLPGHQKRI 57
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-759 1.43e-04

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 41.18  E-value: 1.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09551     8 SVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQ--MTSEDLLRIGVTLAGHQKKILNSIQSM 65
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 698-759 1.55e-04

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 40.66  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767939589  698 EQSVGEWLESIGLQQYESKLLLNGFDdvhflGSNVME-EQD-LRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09534     3 EEFVEEWLNELNCGQYLDIFEKNLIT-----GDLLLElDKEaLKELGITKVGDRIRLLRAIKSL 61
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-180 1.57e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.57e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767939589   148 DNETALHCAA-QYGHTEVVKVLLEELTDPTMRNN 180
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
99-156 1.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939589    99 LLRND-ALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrVNEQNNDNETALHCA 156
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-759 1.69e-04

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 41.00  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09554     5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQ--ISTEDLLRMGVTLAGHQKKILSSIQAM 62
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 701-755 2.04e-04

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 40.38  E-value: 2.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  701 VGEWLESIGLQQYESKLLLNGFD-DVHFLgsnvMEEQDLRDIGISDPQHRRKLLQA 755
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITgDVLVA----LDHEDLKEMGITSVGHRLTILKA 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 72-268 2.39e-04

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: 45.46  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589    72 NVNCVDSTGYTPLHHAAL-NGHKDVVEVLLRNDALTNVADSKgcypLHLAAwKGDAQIVRLLI-HQGPSHTR------VN 143
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAIS-LEYVDAVEAILlHLLAAFRKsgplelAN 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   144 EQNNDNE----TALHCAAQYGHTEVVKVLLEELTD-----------PTMRNNKF---ETPLDLAALYGRLEVVKMLLNAH 205
Cdd:TIGR00870  119 DQYTSEFtpgiTALHLAAHRQNYEIVKLLLERGASvparacgdffvKSQGVDSFyhgESPLNAAACLGSPSIVALLSEDP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   206 PNLLSCNTKKHTPLHLAA-----RNGHKAVVQ------VLLDAGMDS--------NYQTEmgSALHEAALFGKTDVVQIL 266
Cdd:TIGR00870  199 ADILTADSLGNTLLHLLVmenefKAEYEELSCqmynfaLSLLDKLRDskelevilNHQGL--TPLKLAAKEGRIVLFRLK 276


                   ..
gi 767939589   267 LA 268
Cdd:TIGR00870  277 LA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 80-110 2.41e-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: 2.41e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767939589    80 GYTPLHHAAL-NGHKDVVEVLLRNDALTNVAD 110
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 163-284 2.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  163 EVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLN--AHPNLlscNTKKH-TPLHLAARNGH-----KAVVQVL 234
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDngADINS---STKNNsTPLHYLSNIKYnltdvKEIVKLL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767939589  235 LDAGMDSNYQTEMG-SALHEAA--LFGKTDVVQILLAAGTDVNIKDNHGLTAL 284
Cdd:PHA03100   93 LEYGANVNAPDNNGiTPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLL 145
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 148-177 3.07e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.07e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 767939589    148 DNETALHCAAQYGHTEVVKVLLEELTDPTM 177
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 946-1041 3.11e-04

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: 41.85  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  946 YLGSMLIKDLRGTESTQDACAKMRKSTEhmKKIPtIILSI--TYKG-VKFIDASNKNVIAEHEIRNIS-CA---AQDPED 1018
Cdd:cd01211     8 YLGCAKVNAPRSETEALRIMAILREQSA--QPIK-VTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILfCArgpDGTSES 84

                          90       100
                  ....*....|....*....|...
gi 767939589 1019 LCtFAYITKDLQTSHHYCHVFST 1041
Cdd:cd01211    85 DC-FAFTWSHGETAIFQCHVFRC 106
Ank_4 pfam13637
Ankyrin repeats (many copies);
249-285 3.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 3.29e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 767939589   249 SALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALD 285
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 699-759 3.86e-04

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 39.61  E-value: 3.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLGsnvMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09506     8 DDVGDWLESLNLGEHRERFMDNEIDGSHLPN---LDKEDLTELGVTRVGHRMNIERALKKL 65
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-246 3.94e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.94e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767939589   216 HTPLHLAA-RNGHKAVVQVLLDAGMDSNYQTE 246
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 249-278 4.57e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 4.57e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767939589   249 SALHEAAL-FGKTDVVQILLAAGTDVNIKDN 278
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-242 5.49e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 5.49e-04
                           10        20
                   ....*....|....*....|....*.
gi 767939589   217 TPLHLAARNGHKAVVQVLLDAGMDSN 242
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 80-226 7.47e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 43.64  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   80 GYTPLHHAALNGHKDVVEVLLRNDALTNVADS----------KGCY----PLHLAAWKGDAQIVRLLIHQGPSHTRVNEQ 145
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggPGFYfgelPLSLAACTNQLDIVKFLLENPHSPADISAR 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  146 NNDNETALHCaaqyghtevvkvlLEELTDPTMRNNKFETpldlaALYGRLEVVKMLLNAHPNLLS-CNTKKHTPLHLAAR 224
Cdd:cd22196   174 DSMGNTVLHA-------------LVEVADNTPENTKFVT-----KMYNEILILGAKIRPLLKLEEiTNKKGLTPLKLAAK 235


                  ..
gi 767939589  225 NG 226
Cdd:cd22196   236 TG 237
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 699-753 7.63e-04

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 38.83  E-value: 7.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  699 QSVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLL 753
Cdd:cd09542     5 RSVSEWLESIRMKRYILHFRSAGLDTMECVLE--LTAEDLTQMGITLPGHQKRIL 57
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 774-826 8.15e-04

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 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 SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-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: 188898  Cd Length: 67  Bit Score: 38.82  E-value: 8.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNlwelelvNVLKVQLL--------GHRKRII 826
Cdd:cd09499     4 SVGQWLESIGLPQYESKLLLNGFDDVDFLGS-------GVMEDQDLkeigitdeQHRQIIL 57
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 703-759 8.30e-04

SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization.


Pssm-ID: 188940  Cd Length: 60  Bit Score: 38.82  E-value: 8.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767939589  703 EWLESIGLQQYESKLLLNGFDDVHFLGSNVMeeQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09541     5 EWLEEAGLQHYYPAFAAGGVTSIEALAQLTM--QDYASLGVQDMEDKQKLFRLIQTL 59
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 772-831 9.34e-04

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 38.66  E-value: 9.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  772 PPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVQLLGHRKRIIASLAD 831
Cdd:cd09491     5 PKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEA-GVTNPAHKRRLLDSLQD 63
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 72-244 1.00e-03

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: 43.33  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   72 NVNCVDS--TGYTPLHHAALNGHKDVVEVLLRNDALTNVADSK-------------GCYPLHLAAWKGDAQIVRLLIHQG 136
Cdd:cd21882    63 NAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  137 PSHTRVNEQNNDNETALHcaaqyghtevvkvLLEELTDPTMRNNKFETPL-DLAALYGRlevvkmllNAHPNL---LSCN 212
Cdd:cd21882   143 AQPAALEAQDSLGNTVLH-------------ALVLQADNTPENSAFVCQMyNLLLSYGA--------HLDPTQqleEIPN 201

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767939589  213 TKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQ 244
Cdd:cd21882   202 HQGLTPLKLAAVEGKIVMFQHILQREFSGPYQ 233
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 777-830 1.02e-03

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 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 apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 38.39  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939589  777 SWLDSLGLQDYVHSFLSSGYssidtvkNLWEL-----ELVNVLKVQLLGHRKRIIASLA 830
Cdd:cd09497     9 DWLREFGLEEYTPNFIKAGY-------DLPTIsrmtpEDLTAIGITKPGHRKKLKSEIA 60
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 700-753 1.32e-03

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: 38.05  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVH-FLGSNvmeEQDLRDIGISDPQHRRKLL 753
Cdd:cd09490     5 DIAEWLASIHLEQYLDLFREHGYVTATdCQGIN---DSRLKQIGISPTGHRRRIL 56
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 700-758 2.08e-03

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 37.54  E-value: 2.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  700 SVGEWLESIGLQQYESKLLLNGFDDVHFLGSnvMEEQDLRDIGISDPQHRRKLL---QAARS 758
Cdd:cd09550     4 SVDDWLDSIKMGRYKDHFAAGGYSSLGMVMR--MNIEDIRRLGITLMGHQKKILtsiQVMRA 63
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 72-202 3.65e-03

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: 41.32  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589   72 NVNCVDS--TGYTPLHHAALNGHKDVVEVLLRNDALTNVA---------DSKGCY-----PLHLAAWKGDAQIVRLLIHQ 135
Cdd:cd22193    66 NAEYTDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpkYQGEGFyfgelPLSLAACTNQPDIVQYLLEN 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939589  136 GPSHTRVNEQNNDNETALHCAAQYG-----HTEVVKVLLEELT------DPT-----MRNNKFETPLDLAALYGRLEVVK 199
Cdd:cd22193   146 EHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRMYDMILirgaklCPTveleeIRNNDGLTPLQLAAKMGKIEILK 225


                  ...
gi 767939589  200 MLL 202
Cdd:cd22193   226 YIL 228
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 774-829 3.91e-03

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 37.15  E-value: 3.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939589  774 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVQLLGHRKRIIASL 829
Cdd:cd09549     9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLS-LGITSLEHQELLLAGI 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-208 4.54e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.54e-03
                            10        20
                    ....*....|....*....|....*
gi 767939589    184 TPLDLAALYGRLEVVKMLLNAHPNL 208
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-147 4.66e-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: 35.73  E-value: 4.66e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 767939589   112 KGCYPLHLAAWK-GDAQIVRLLIHQGPShtrVNEQNN 147
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD---VNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-170 5.53e-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: 35.31  E-value: 5.53e-03
                           10        20
                   ....*....|....*....|...
gi 767939589   148 DNETALHCAAQYGHTEVVKVLLE 170
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLE 23
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 698-759 5.85e-03

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 36.53  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939589  698 EQSVGEWLESIGLQQYESKLLLNGFDDVHFLgsNVMEEQDLRDIGISDPQHRRKLLQAARSL 759
Cdd:cd09505     7 EEDVCTWLRSIGLEQYVEVFRANNIDGKELL--NLTKESLSKDLKIESLGHRNKILRKIEEL 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 220-289 5.89e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939589  220 HLAArNGHKAVVQVLLDAGMDSNYQTEMGSA-LHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALDTVRE 289
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 112-138 6.86e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 6.86e-03
                            10        20
                    ....*....|....*....|....*..
gi 767939589    112 KGCYPLHLAAWKGDAQIVRLLIHQGPS 138
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 777-829 9.37e-03

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 36.06  E-value: 9.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767939589  777 SWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVQLLGHRKRIIASL 829
Cdd:cd09555    11 AWLSAIGLECYQDNFSKFGLCTFSDVAQL-SLEDLPALGITLAGHQKKLLHHI 62
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 183-208 9.69e-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: 34.93  E-value: 9.69e-03
                           10        20
                   ....*....|....*....|....*.
gi 767939589   183 ETPLDLAALYGRLEVVKMLLNAHPNL 208
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADI 28
 
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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