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Conserved domains on  [gi|1720389696|ref|XP_030105543|]
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ankyrin repeat and SAM domain-containing protein 1A isoform X3 [Mus musculus]

Protein Classification

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 ...
 903-1048 1.88e-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: 1.88e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  903 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 982
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  983 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1048
Cdd:cd01274     81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-263 5.03e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 5.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   29 NVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPShtrvneqnaleir 108
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  109 elkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL--GAHPNL 186
Cdd:COG0666    113 -----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLeaGADVNA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  187 LScsTRKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:COG0666    182 RD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 674-740 3.31e-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: 133.96  E-value: 3.31e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  674 LEQSVGEWLESIGLQQYESKLLLNGFDDVRFLGSNVMEEQDLREIGISDPQHRRKLLQAARSLPKVK 740
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 ...
 745-809 1.71e-34

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: 125.88  E-value: 1.71e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVHLLGHRKRIIASLADR 809
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 ...
 903-1048 1.88e-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: 1.88e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  903 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 982
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  983 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1048
Cdd:cd01274     81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-263 5.03e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 5.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   29 NVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPShtrvneqnaleir 108
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  109 elkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL--GAHPNL 186
Cdd:COG0666    113 -----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLeaGADVNA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  187 LScsTRKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:COG0666    182 RD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 674-740 3.31e-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: 133.96  E-value: 3.31e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  674 LEQSVGEWLESIGLQQYESKLLLNGFDDVRFLGSNVMEEQDLREIGISDPQHRRKLLQAARSLPKVK 740
Cdd:cd09499      1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 915-1048 3.33e-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: 133.59  E-value: 3.33e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   915 ESCGYEANYLGSMLIKDLRGTESTQDACAKMRKS-TEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDP 993
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696   994 EDLCTFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQLALQAQKS 1048
Cdd:smart00462   82 DDLDVFGYIARDPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARSE 134
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 745-809 1.71e-34

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: 125.88  E-value: 1.71e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVHLLGHRKRIIASLADR 809
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
164-255 3.77e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 3.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  164 LDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLAARNGHKAVVQVLLDaGMDSNYQTEMGSALHEAALFGKTDVVQI 243
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1720389696  244 LLAAGIDVNIKD 255
Cdd:pfam12796   80 LLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 27-262 1.70e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 99.33  E-value: 1.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLH---HAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGD-AQIVRLLIQQGPShtrvneq 102
Cdd:PHA03095    37 GADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGAD------- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  103 naleirelkkygpfdpyINAKNNDNETALH--CAAQYGHTEVVKALLEELTDPTMRNNKFETPLDlaALYGR----LEVV 176
Cdd:PHA03095   110 -----------------VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELL 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  177 KLLLGAHPNLLSCSTRKHTPLHLAARNGH--KAVVQVLLDAGMDSNYQTEMG-SALHEAALFG--KTDVVQILLAAGIDV 251
Cdd:PHA03095   171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISI 250

                          250
                   ....*....|.
gi 1720389696  252 NIKDNRGLTAL 262
Cdd:PHA03095   251 NARNRYGQTPL 261
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 677-736 1.22e-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: 1.22e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   677 SVGEWLESIGLQQYESKLLLNGFDDVRFLgsNVMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLL--LLTSEEDLKELGITKLGHRKKILKAIQKL 65
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
919-1038 1.61e-14

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.63  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  919 YEANYLGSM-------LIKDLRgTESTQDA--CAKM------RKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEI 983
Cdd:pfam00640    1 FAVRYLGSVevpeeraPDKNTR-MQQAREAirRVKAakinkiRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  984 RNIS-CAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDvnLTYEIILTLGQAFEVA 1038
Cdd:pfam00640   80 VSISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 676-736 2.07e-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: 2.07e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  676 QSVGEWLESIGLQQYEsKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:pfam00536    6 EDVGEWLESIGLGQYI-DSFRAGYIDGDALLQ--LTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 745-806 1.17e-12

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: 63.83  E-value: 1.17e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFlSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 806
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAI 60
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 744-806 2.71e-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: 60.00  E-value: 2.71e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696   744 YDGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVkNLWELELVNVLKVHLLGHRKRIIASL 806
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL-LLTSEEDLKELGITKLGHRKKILKAI 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-262 1.66e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   73 PLHLAAWKGDAQIVRLLIQQgpSHTRVNEQNALeirelkkygpfdpyinaknndNETALHCAAQYGHTEVVKALLEEltD 152
Cdd:cd22192     20 PLLLAAKENDVQAIKKLLKC--PSCDLFQRGAL---------------------GETALHVAALYDNLEAAVVLMEA--A 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  153 PTMRNN-------KFETPLDLAALYGRLEVVKLLLGAHPNLLS---CST----RKHT-------PLHLAARNGHKAVVQV 211
Cdd:cd22192     75 PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpraTGTffrpGPKNliyygehPLSFAACVGNEEIVRL 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  212 LLDAGMDSNYQTEMG-SALHEAALFGKTDVV----QILLAAGIDVN------IKDNRGLTAL 262
Cdd:cd22192    155 LIEHGADIRAQDSLGnTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPF 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 37-65 5.02e-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: 41.42  E-value: 5.02e-05
                            10        20
                    ....*....|....*....|....*....
gi 1720389696    37 GYTPLHHAALNGHRDVVEVLLRNDALTNV 65
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 37-202 1.68e-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: 45.84  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   37 GYTPLHHAALNGHRDVVEVLLRNDALTNVA---------DSKGC-----YPLHLAAWKGDAQIVRLLIQQGPShtrVNEQ 102
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPAD---ILTA 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  103 NAL--EIRELKKygpfdpyINAKNNDNETALHCAAQyghtEVVKALLEELTDPT----MRNNKFETPLDLAALYGRLEVV 176
Cdd:TIGR00870  205 DSLgnTLLHLLV-------MENEFKAEYEELSCQMY----NFALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLF 273

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720389696  177 KLLLGahpnlLSCSTRKHT-----PLHLAAR 202
Cdd:TIGR00870  274 RLKLA-----IKYKQKKFVawpngQQLLSLY 299
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 903-1048 1.88e-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: 1.88e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  903 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 982
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  983 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1048
Cdd:cd01274     81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-263 5.03e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 5.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   29 NVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPShtrvneqnaleir 108
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  109 elkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL--GAHPNL 186
Cdd:COG0666    113 -----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLeaGADVNA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  187 LScsTRKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:COG0666    182 RD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-262 6.24e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.13  E-value: 6.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPShtrvneqnale 106
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD----------- 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  107 irelkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL--GAHP 184
Cdd:COG0666    146 -------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLeaGADV 212

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  185 NLLscSTRKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:COG0666    213 NAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-263 9.26e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 9.26e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   38 YTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPshtrvneqnaleirelkkygpfd 117
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA----------------------- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  118 pYINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL--GAHPNLlsCSTRKHT 195
Cdd:COG0666     79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeaGADVNA--QDNDGNT 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  196 PLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:COG0666    156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-230 7.41e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 7.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   26 RGPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPShtrvneqnal 105
Cdd:COG0666    109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD---------- 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  106 eirelkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLGAHPN 185
Cdd:COG0666    179 --------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720389696  186 LLSCSTRKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMGSALH 230
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 674-740 3.31e-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: 133.96  E-value: 3.31e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  674 LEQSVGEWLESIGLQQYESKLLLNGFDDVRFLGSNVMEEQDLREIGISDPQHRRKLLQAARSLPKVK 740
Cdd:cd09499      1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 915-1048 3.33e-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: 133.59  E-value: 3.33e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   915 ESCGYEANYLGSMLIKDLRGTESTQDACAKMRKS-TEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDP 993
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696   994 EDLCTFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQLALQAQKS 1048
Cdd:smart00462   82 DDLDVFGYIARDPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARSE 134
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 745-809 1.71e-34

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: 125.88  E-value: 1.71e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVHLLGHRKRIIASLADR 809
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 917-1035 1.80e-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: 1.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  917 CGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPT-IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPED 995
Cdd:cd00934      1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGpVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1720389696  996 LCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAF 1035
Cdd:cd00934     81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-262 9.71e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 9.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  119 YINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLH 198
Cdd:COG0666     13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  199 LAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:COG0666     93 AAARNGDLEIVKLLLEAGADVNARDKDGeTPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
164-255 3.77e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 3.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  164 LDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLAARNGHKAVVQVLLDaGMDSNYQTEMGSALHEAALFGKTDVVQI 243
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1720389696  244 LLAAGIDVNIKD 255
Cdd:pfam12796   80 LLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 27-262 1.70e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 99.33  E-value: 1.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLH---HAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGD-AQIVRLLIQQGPShtrvneq 102
Cdd:PHA03095    37 GADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGAD------- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  103 naleirelkkygpfdpyINAKNNDNETALH--CAAQYGHTEVVKALLEELTDPTMRNNKFETPLDlaALYGR----LEVV 176
Cdd:PHA03095   110 -----------------VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELL 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  177 KLLLGAHPNLLSCSTRKHTPLHLAARNGH--KAVVQVLLDAGMDSNYQTEMG-SALHEAALFG--KTDVVQILLAAGIDV 251
Cdd:PHA03095   171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISI 250

                          250
                   ....*....|.
gi 1720389696  252 NIKDNRGLTAL 262
Cdd:PHA03095   251 NARNRYGQTPL 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
131-222 3.33e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  131 LHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLgAHPNlLSCSTRKHTPLHLAARNGHKAVVQ 210
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHAD-VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1720389696  211 VLLDAGMDSNYQ 222
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 27-221 1.09e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGH-----RDVVEVLLRNDALTNVADSKGCYPLHLAAWK--GDAQIVRLLIQQGPShtrv 99
Cdd:PHA03100    58 GADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN---- 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  100 neqnaleirelkkygpfdpyINAKNNDNETALHCAAQYGHTEV------------------VKALLEELTDPTMRNNKFE 161
Cdd:PHA03100   134 --------------------VNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGF 193

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  162 TPLDLAALYGRLEVVKLLL--GAHPNLlsCSTRKHTPLHLAARNGHKAVVQVLLDAGMDSNY 221
Cdd:PHA03100   194 TPLHYAVYNNNPEFVKYLLdlGANPNL--VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-185 6.02e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 6.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   26 RGPNVNCVDSTGYTPLHHAALN--GHRDVVEVLLRNDALTNVADSKGCYPLHLAAW--KGDAQIVRLLIQQGpshTRVNE 101
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG---VDINA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  102 QNALEIreLKKYGpFDpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLG 181
Cdd:PHA03100   172 KNRVNY--LLSYG-VP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                   ....
gi 1720389696  182 AHPN 185
Cdd:PHA03100   247 NGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-157 1.61e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   41 LHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQqgpsHTRVNEQnaleirelkkygpfdpyi 120
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLK------------------ 58

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720389696  121 naknNDNETALHCAAQYGHTEVVKALLEELTDPTMRN 157
Cdd:pfam12796   59 ----DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 907-1044 5.77e-19

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269971  Cd Length: 144  Bit Score: 84.64  E-value: 5.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  907 HQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMrKSTEHMK-----KIPTIILSITYKGVKFIDASNKNVIAEH 981
Cdd:cd01273      2 HPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKL-KFARQLKksegaKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696  982 EIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFstVDVNLTYEIILTLGQAFEVAYQLALQ 1044
Cdd:cd01273     81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVF--DSEKLAEEITLTIGQAFDLAYRRFLE 141
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 27-264 2.71e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.87  E-value: 2.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGpshtrvneqnale 106
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG------------- 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  107 irelkkygpfdPYINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRlEVVKLLLGaHPNL 186
Cdd:PHA02874   181 -----------AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASI 247

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  187 LSCSTRKHTPLHLAArnghkavvqvlldagmdsNYQTEMgsalheaalfgktDVVQILLAAGIDVNIKDNRGLTALDT 264
Cdd:PHA02874   248 NDQDIDGSTPLHHAI------------------NPPCDI-------------DIIDILLYHKADISIKDNKGENPIDT 294
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 671-730 8.97e-16

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: 72.55  E-value: 8.97e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  671 SRTLEQSVGEWLESIGLQQYESKLLLNGFDDVRFLGSnVMEEqDLREIGISDPQHRRKLL 730
Cdd:cd09491      1 SLSWPKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSD-ITEE-DLEEAGVTNPAHKRRLL 58
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 44-282 1.78e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 1.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   44 AALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQG------------PSHTRVNEQNALEIRELK 111
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaipdvkypdiesELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  112 KYGPF-DPYINAKNNdneTALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLG--AHPNLLS 188
Cdd:PHA02875    89 DLGKFaDDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDhkACLDIED 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  189 CStrKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG--SALHEAALFGKTDVVQILLAAGIDVNIK---DNRGLTALD 263
Cdd:PHA02875   166 CC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADCNIMfmiEGEECTILD 243

                          250       260
                   ....*....|....*....|
gi 1720389696  264 TVRDLPSQ-KSQQIAALIED 282
Cdd:PHA02875   244 MICNMCTNlESEAIDALIAD 263
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 677-736 1.22e-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: 1.22e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   677 SVGEWLESIGLQQYESKLLLNGFDDVRFLgsNVMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLL--LLTSEEDLKELGITKLGHRKKILKAIQKL 65
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
919-1038 1.61e-14

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.63  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  919 YEANYLGSM-------LIKDLRgTESTQDA--CAKM------RKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEI 983
Cdd:pfam00640    1 FAVRYLGSVevpeeraPDKNTR-MQQAREAirRVKAakinkiRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  984 RNIS-CAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDvnLTYEIILTLGQAFEVA 1038
Cdd:pfam00640   80 VSISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 919-1040 1.95e-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: 1.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  919 YEANYLGSMLIKDLRGTESTQDACAKMRksteHMKKIPT-IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDLC 997
Cdd:cd13161      4 FEAKYLGSVPVKEPKGNDVVMAAVKRLK----DLKLKPKpVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720389696  998 TFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQ 1040
Cdd:cd13161     80 LFAFISHDPRLGRITCHVFRCKRGA--QEICDTIAEAFKAAAE 120
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 919-1036 1.87e-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: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  919 YEANYLGSMLIKDLRGTESTQDACA---KMRKSTEhmKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNIS-CAAqDPE 994
Cdd:cd13159      5 FYLKYLGSTLVEKPKGEGATAEAVKtiiAMAKASG--KKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISyCTA-DAN 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720389696  995 DLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFE 1036
Cdd:cd13159     82 HDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 676-736 2.07e-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: 2.07e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  676 QSVGEWLESIGLQQYEsKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:pfam00536    6 EDVGEWLESIGLGQYI-DSFRAGYIDGDALLQ--LTEDDLLKLGVTLLGHRKKILYAIQRL 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-100 2.25e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 2.25e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696   24 MWRGPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNvaDSKGCYPLHLAAWKGDAQIVRLLIQQGPSHTRVN 100
Cdd:pfam12796   17 LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 745-806 1.17e-12

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: 63.83  E-value: 1.17e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFlSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 806
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAI 60
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 40-262 1.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   40 PLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWK----GDAQIVRLLIQQGPSHTRVNEQNALEIREL----- 110
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKDAFNNRNVeifki 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  111 -------KKYGPFDPYINAKNNDNETalhcaaqygHTEVVKALLEELTDPTMRN-NKFETPLDLAALYGRLEVVKLLL-- 180
Cdd:PHA02878   120 iltnrykNIQTIDLVYIDKKSKDDII---------EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLsy 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  181 GAHPNLLSCSTRkhTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMGSA-LHEAALFGKT-DVVQILLAAGIDVNIKDN-R 257
Cdd:PHA02878   191 GANVNIPDKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTpLHISVGYCKDyDILKLLLEHGVDVNAKSYiL 268


                   ....*
gi 1720389696  258 GLTAL 262
Cdd:PHA02878   269 GLTAL 273
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
676-736 2.28e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 63.06  E-value: 2.28e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLgsNVMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:pfam07647    7 ESVADWLRSIGLEQYTDNFRDQGITGAELL--LRLTLEDLKRLGITSVGHRRKILKKIQEL 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
141-262 4.50e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 4.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  141 EVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLAARNGHKAVVQVLLDAGMDSN 220
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720389696  221 YQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:COG0666     82 AKDDGGnTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 119-262 4.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 4.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  119 YINAKNNDNETALHCAAQYGHT-----EVVKALLEELTDPTMRNNKFETPLDLAALY--GRLEVVKLLLGAHPNLLSCST 191
Cdd:PHA03100    60 DINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696  192 RKHTPLHLAARNGH--KAVVQVLLDAGMDSNyqtemgsalheaalfgKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:PHA03100   140 DGENLLHLYLESNKidLKILKLLIDKGVDIN----------------AKNRVNYLLSYGVPINIKDVYGFTPL 196
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 677-734 1.03e-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: 60.72  E-value: 1.03e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLgsnVMEEQDLREIGISDPQHRRKLLQAAR 734
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALL---LLTDEDLKELGITSPGHRKKILRAIQ 55
PHA03095 PHA03095
ankyrin-like protein; Provisional
 141-263 2.55e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 2.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  141 EVVKALLEELTDPTMRNNKFETPLDLAALYG---RLEVVKLLLGAHPNLLSCSTRKHTPLHLAARNGHKA-VVQVLLDAG 216
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  217 MDSNYQTEMG-SALHeAALFGK---TDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:PHA03095   108 ADVNAKDKVGrTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLA 157
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 744-806 2.71e-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: 60.00  E-value: 2.71e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696   744 YDGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVkNLWELELVNVLKVHLLGHRKRIIASL 806
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL-LLTSEEDLKELGITKLGHRKKILKAI 62
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 903-1020 3.13e-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: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  903 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTehmKKIPTIILSITYKGVKFIDASNKNVIAEHE 982
Cdd:cd01268      1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASR---KKPVRAVLWVSGDGLRVVDEKTKGLIVDQT 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720389696  983 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVD 1020
Cdd:cd01268     78 IEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVK 115
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 921-1039 1.00e-10

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: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  921 ANYLGSMLIKDLrgteSTQDACAKMRKSTEHMKKIPT----IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDl 996
Cdd:cd13157      6 AQYIGSFPVSGL----DVADRADSVRKQLESLKESGSrgrpVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH- 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720389696  997 CTFAYITKDLQ--TSHHYCHVFSTVDVNLTYEIILTLGQAFEVAY 1039
Cdd:cd13157     81 AQFAFVARNPGgpTNRQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-180 1.03e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.03e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  129 TALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL 180
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_SASH-like cd09493
SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like ...
 676-735 1.73e-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: 57.51  E-value: 1.73e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLgsNVMEEQDLREIGISDPQHRRKLLQAARS 735
Cdd:cd09493      3 KTVEELLERINLQEHTSTLLLNGYETLEDF--KDLKESHLNELNITDPEHRAKLLTAAEL 60
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 27-180 3.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 3.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWK-GDAQIVRLLIQQGpshTRVNEQNAl 105
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG---VDVNAKSY- 266

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  106 eIRELkkygpfdpyinaknndneTALHCAAQygHTEVVKALLEELTDPTMRNNKFETPLDLAAL-YGRLEVVKLLL 180
Cdd:PHA02878   267 -ILGL------------------TALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-264 9.74e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 9.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  107 IRELKKYGPFDPYINAKNNDNETALHCAAQYGH---TEVVKALLEELTDPTMRNNKFETPLDLAALYG-RLEVVKLLLGA 182
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  183 HPNLLSCSTRKHTPLH--LAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHeaALFGKTDV----VQILLAAGIDVNIKD 255
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGmTPLA--VLLKSRNAnvelLRLLIDAGADVYAVD 184


                   ....*....
gi 1720389696  256 NRGLTALDT 264
Cdd:PHA03095   185 DRFRSLLHH 193
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 746-803 1.16e-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: 55.38  E-value: 1.16e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  746 GVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNL-WE-LElvnVLKVHLLGHRKRII 803
Cdd:cd09498      4 DYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLtWEdLQ---DIGITKLGHQKKLM 60
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 27-252 1.66e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGH-RDVVEVLLRNDALTNVADSKGCYPLHLAAWKG-DAQIVRLLIQQGPShtrVNEQNA 104
Cdd:PHA02876   263 GFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGAD---VNAADR 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  105 LEIRELKKYGPFDPYinaknndnetalhcaaqyghTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLGAHP 184
Cdd:PHA02876   340 LYITPLHQASTLDRN--------------------KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  185 NLLSCSTRKHTPLHLA--ARNGHKAVvQVLLDAGMDSNYQTE-MGSALHEAALFG-KTDVVQILLAAGIDVN 252
Cdd:PHA02876   400 DIEALSQKIGTALHFAlcGTNPYMSV-KTLIDRGANVNSKNKdLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 27-202 1.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVD-STGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGpshtrvneqnal 105
Cdd:PHA02878   157 GADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG------------ 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  106 eirelkkygpfdPYINAKNNDNETALHCAAQY-GHTEVVKALLEELTDPtmrnNKFETPLDLAALYGRL---EVVKLLL- 180
Cdd:PHA02878   225 ------------ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDV----NAKSYILGLTALHSSIkseRKLKLLLe 288

                          170       180
                   ....*....|....*....|...
gi 1720389696  181 -GAHPNLLscSTRKHTPLHLAAR 202
Cdd:PHA02878   289 yGADINSL--NSYKLTPLSSAVK 309
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 957-1044 1.78e-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: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  957 TIILSITYKGVKFIDASNKNVIAEHEIRNISCAA-QDPEDLCTFAYITKDlQTSHHYCHVFSTVDvNLTYEIILTLGQAF 1035
Cdd:cd01209     84 NISLTISTDGLNLVTPDTGQIIANHHMQSISFASgGDPDTYDYVAYVAKD-PVNQRACHVLECGD-GLAQDVIATIGQAF 161


                   ....*....
gi 1720389696 1036 EVAYQLALQ 1044
Cdd:cd01209    162 ELRFKQYLK 170
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 745-806 1.87e-09

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: 54.84  E-value: 1.87e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 806
Cdd:cd09543      1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNSIDKVLQM-TQEDIKHIGVRLPGHQKRIAYSI 61
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 748-806 2.33e-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: 2.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  748 SPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 806
Cdd:cd09488      1 AFRSVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTR-LGVTLVGHQKKILNSI 58
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 678-736 2.36e-09

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: 54.37  E-value: 2.36e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  678 VGEWLESIGLQQYESKLLLNGFDDVRFlgSNVMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09527      5 VYDWLRTLQLEQYAEKFVDNGYDDLEV--CKQIGDPDLDAIGVMNPAHRKRILEAVRRL 61
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-77 2.68e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.68e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720389696   29 NVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLA 77
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_SAMSN1 cd09561
SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as ...
 672-736 6.17e-09

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: 53.33  E-value: 6.17e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  672 RTLEQSVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09561      2 RPKPKTLQELLERIHLQEYTSTLLLNGYETLEDLKD--LKESHLIELNITDPEDRARLLSAAENL 64
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-90 1.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720389696   37 GYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLI 90
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-262 1.66e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   73 PLHLAAWKGDAQIVRLLIQQgpSHTRVNEQNALeirelkkygpfdpyinaknndNETALHCAAQYGHTEVVKALLEEltD 152
Cdd:cd22192     20 PLLLAAKENDVQAIKKLLKC--PSCDLFQRGAL---------------------GETALHVAALYDNLEAAVVLMEA--A 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  153 PTMRNN-------KFETPLDLAALYGRLEVVKLLLGAHPNLLS---CST----RKHT-------PLHLAARNGHKAVVQV 211
Cdd:cd22192     75 PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpraTGTffrpGPKNliyygehPLSFAACVGNEEIVRL 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  212 LLDAGMDSNYQTEMG-SALHEAALFGKTDVV----QILLAAGIDVN------IKDNRGLTAL 262
Cdd:cd22192    155 LIEHGADIRAQDSLGnTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPF 216
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
744-808 2.69e-08

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 51.50  E-value: 2.69e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  744 YDGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASLAD 808
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRL-TLEDLKRLGITSVGHRRKILKKIQE 64
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 99-256 3.01e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   99 VNEQNALEIRELKKYGPFDPYINAKNN-DNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGR----- 172
Cdd:PHA03100     6 VLTKSRIIKVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdv 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  173 LEVVKLLL--GAHPNllSCSTRKHTPLHLAARN--GHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFG--KTDVVQILL 245
Cdd:PHA03100    86 KEIVKLLLeyGANVN--APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGeNLLHLYLESNkiDLKILKLLI 163

                          170
                   ....*....|.
gi 1720389696  246 AAGIDVNIKDN 256
Cdd:PHA03100   164 DKGVDINAKNR 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-167 3.63e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 3.63e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  110 LKKYGPFDPyiNAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLA 167
Cdd:pfam13857    1 LLEHGPIDL--NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-213 4.59e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.59e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  162 TPLDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLAARNGHKAVVQVLL 213
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-255 4.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   22 MSMWRGPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQqgpSHTRVNE 101
Cdd:PHA02876   163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID---NRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  102 Q-----NALEIRELK----------KYGPFDPY---------------------------INAKNNDNETALHCAAQYGH 139
Cdd:PHA02876   240 NdlsllKAIRNEDLEtslllydagfSVNSIDDCkntplhhasqapslsrlvpkllergadVNAKNIKGETPLYLMAKNGY 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  140 -TEVVKALLEELTDPTMRNNKFETPLDLAALYGRLE--VVKLL-LGAHPNLLSCSTRkhTPLHLAARNGHKAVVQVLLDA 215
Cdd:PHA02876   320 dTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdiVITLLeLGANVNARDYCDK--TPIHYAAVRNNVVIINTLLDY 397

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1720389696  216 GMD-SNYQTEMGSALHeAALFGKTDV--VQILLAAGIDVNIKD 255
Cdd:PHA02876   398 GADiEALSQKIGTALH-FALCGTNPYmsVKTLIDRGANVNSKN 439
SAM_SASH1_repeat2 cd09492
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ...
 677-736 6.73e-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: 6.73e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09492      9 SVSDWLVSIGLPMYSPPLLEAGFSTLSRVSS--LSETCLREAGITEERHIRKLLSAARLV 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
195-245 7.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 7.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  195 TPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILL 245
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 21-260 7.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 7.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   21 PMSMWRGPNVNCVDSTGYTPLHHAALNGH-RDVVEVLLRNDALTNVADSKGCYPLHLAA-WKGDAQIVRLLIQQGPShtr 98
Cdd:PHA02876   291 PKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGAN--- 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   99 vneqnaleirelkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLaALYGR--LEVV 176
Cdd:PHA02876   368 ---------------------VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTnpYMSV 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  177 KLLLGAHPNLLSCSTRKHTPLHLAARNGHKA-VVQVLLDAGMDSNYQTEMGSALHEAALfGKTDVVQILLAAGIDvnIKD 255
Cdd:PHA02876   426 KTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIAL-EYHGIVNILLHYGAE--LRD 502


                   ....*
gi 1720389696  256 NRGLT 260
Cdd:PHA02876   503 SRVLH 507
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-147 1.26e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   34 DSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQ---------QGPSHTRVNEQNA 104
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfasisdphaAGDLLCTAAKRND 634

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720389696  105 LE-IRELKKYGpFDpyINAKNNDNETALHCAAQYGHTEVVKALL 147
Cdd:PLN03192   635 LTaMKELLKQG-LN--VDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_5 pfam13857
Ankyrin repeats (many copies);
212-263 2.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  212 LLDAG-MDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 919-1012 2.74e-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: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  919 YEANYLGSMLIKDLRGTESTQDACAKM----RKSTEHMKKIptiILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPE 994
Cdd:cd01215     18 FKAKLIGIDEVPAARGDKMCQDAMMKLkgavKAAGEHKQRI---WLNISLEGIKILDEKTGALLHHHPVHKISFIARDTT 94

                           90
                   ....*....|....*...
gi 1720389696  995 DLCTFAYITKdLQTSHHY 1012
Cdd:cd01215     95 DNRAFGYVCG-LDGGHRF 111
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 751-808 2.84e-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: 2.84e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  751 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASLAD 808
Cdd:cd09546      5 SVGEWLEAIKMGRYTEIFMENGYSSMDAVAQV-TLEDLRRLGVTLVGHQKKIMNSIQE 61
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 751-806 3.16e-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: 48.34  E-value: 3.16e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  751 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 806
Cdd:cd09547      5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRM-TIDDIRRIGVTLIGHQRRIVSSI 59
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-255 3.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   52 VVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGpSHTRVNEQNALEIREL----KKYGPFDPYINAKNNDN 127
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECavdsKNIDTIKAIIDNRSNIN 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  128 ETALHCAAQYGHTEVVKALLeeLTDPTMRNNKFE----TPLDLAALYGRL-EVVKLLLGAHPNLLSCSTRKHTPLHLAAR 202
Cdd:PHA02876   239 KNDLSLLKAIRNEDLETSLL--LYDAGFSVNSIDdcknTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  203 NGHKAV-VQVLLDAGMDSNYQTEM-GSALHEAALFGK-TDVVQILLAAGIDVNIKD 255
Cdd:PHA02876   317 NGYDTEnIRTLIMLGADVNAADRLyITPLHQASTLDRnKDIVITLLELGANVNARD 372
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 677-736 4.24e-07

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


Pssm-ID: 188897  Cd Length: 71  Bit Score: 48.45  E-value: 4.24e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSNVMEeqDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09498      9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWE--DLQDIGITKLGHQKKLMLAIKKL 66
SAM_SASH1_repeat1 cd09559
SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins ...
 676-736 5.92e-07

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: 47.71  E-value: 5.92e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLgsNVMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09559      4 KSVEDLLDRINLKEHMPTFLFNGYEDLDTF--KLLEEEDLDELNIRDPEHRAVLLTAVELL 62
SAM_SASH3 cd09560
SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) ...
 672-736 7.67e-07

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: 47.39  E-value: 7.67e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  672 RTLEQSVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09560      2 RPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKE--LRETHLNELNIMDPQHRAKLLTAAELL 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 75-181 1.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   75 HLAAwKGDAQIVRLLIQQGPshtrvneqnaleirelkkygpfDPyiNAKNNDNETALHCAAQYGHTEVVKALLEELTDPT 154
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGA----------------------DP--NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT 142

                           90       100
                   ....*....|....*....|....*..
gi 1720389696  155 MRNNKFETPLDLAALYGRLEVVKLLLG 181
Cdd:PTZ00322   143 LLDKDGKTPLELAEENGFREVVQLLSR 169
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 919-1049 1.52e-06

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


Pssm-ID: 269968  Cd Length: 179  Bit Score: 49.59  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  919 YEANYLGSMLIKdlRGTeSTQDACAKMR------KSTEHMKKIPTIILSITykGVKFI-----------DASNKNVIAEH 981
Cdd:cd01270     31 FQAKYIGSLEVP--RPS-SRVEIVAAMRriryefKAKNIKKKKVTITVSVD--GVKVVlrkkkkkkgwtWDESKLLLMQH 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389696  982 EIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKSR 1049
Cdd:cd01270    106 PIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEVCHKLSLQHMQGN 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 27-96 2.39e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.39e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPSH 96
Cdd:PTZ00322   105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 943-1040 6.09e-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: 6.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  943 AKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIA-------EHEIRNIS-CAAQdPEDLCTFAYITK--DLQTSHhy 1012
Cdd:cd01212     32 ATARRLTVHLRPPQSCILEISDRGLKMVDRSKPNKKDgkpcihyFYSLKNISfCGFH-PRNSRYFGFITKhpLLQRFA-- 108

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720389696 1013 CHVF----STVDVNltyEIIltlGQAFEVAYQ 1040
Cdd:cd01212    109 CHVFvsqeSTRPVA---ESV---GRAFQRFYQ 134
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 114-260 6.34e-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: 50.53  E-value: 6.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  114 GPFDPYINA----KNNDNETALHCAAQYGHTEVVKALLEELTD-----------PTMRNNKF---ETPLDLAALYGRLEV 175
Cdd:cd22194    124 GILDRFINAeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvffnPKYKHEGFyfgETPLALAACTNQPEI 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  176 VKLLL-GAHPNLLSCSTRKHTPLHlaarnghkAVVQVLLDAGMDSNYQTEMG---------------------SALHEAA 233
Cdd:cd22194    204 VQLLMeKESTDITSQDSRGNTVLH--------ALVTVAEDSKTQNDFVKRMYdmillksenknletirnneglTPLQLAA 275

                          170       180
                   ....*....|....*....|....*..
gi 1720389696  234 LFGKTDVVQILLaaGIDVNIKDNRGLT 260
Cdd:cd22194    276 KMGKAEILKYIL--SREIKEKPNRSLS 300
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-147 6.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 6.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696   73 PLHLAAWKGDAQIVRLLIQQGPShtrvneqnaleirelkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKALL 147
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGAD------------------------INAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 678-736 9.54e-06

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: 44.33  E-value: 9.54e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  678 VGEWLESIGLQQYESKLLLNgfdDVRflGSNVM--EEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09507     10 VGAWLESLQLGEYRDIFARN---DIR--GSELLhlERRDLKDLGITKVGHVKRILQAIKDL 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
27-57 1.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.02e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1720389696   27 GPNVNCVDSTGYTPLHHAALNGHRDVVEVLL 57
Cdd:pfam13637   24 GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-180 1.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   26 RGPNVNCVDSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKgDAQIVRLLIQQGPshtrvneqnal 105
Cdd:PHA02874   179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNAS----------- 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  106 eirelkkygpfdpyINAKNNDNETALHCAAQYG-HTEVVKALLEELTDPTMRNNKFETPLDLAALY-GRLEVVKLLL 180
Cdd:PHA02874   247 --------------INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 145-285 1.10e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  145 ALLEEL----TDPTMRNNKFETPLDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLAARNGHKAVVQVLLDAGMDSN 220
Cdd:PLN03192   539 ALLEELlkakLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  221 YQTEmGSALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL---------DTVRDLPSQKSQQIAALIEDHMT 285
Cdd:PLN03192   619 PHAA-GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALqvamaedhvDMVRLLIMNGADVDKANTDDDFS 691
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-736 1.25e-05

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: 44.08  E-value: 1.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09549      9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVAR--MTAQDVLSLGITSLEHQELLLAGIQAL 66
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 677-730 1.43e-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: 43.76  E-value: 1.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGF---DDVRFlgsnvMEEQDLREIGISDPQHRRKLL 730
Cdd:cd09488      4 SVGEWLESIKMGRYKENFTAAGYtslDAVAQ-----MTAEDLTRLGVTLVGHQKKIL 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-93 1.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.71e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696   28 PNVNCVDSTgyTPLHHAALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQG 93
Cdd:PHA02875   128 PDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-736 1.76e-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: 43.79  E-value: 1.76e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09545      5 SVDDWLQAIKMERYKDNFTAAGYTTLEAVVH--MNQDDLARIGISAIAHQNKILSSVQGM 62
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 745-808 1.80e-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: 43.87  E-value: 1.80e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASLAD 808
Cdd:cd09553      2 DYTTFTTVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRI-GVTLAGHQKKILSSIQD 64
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 918-1035 1.86e-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: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  918 GYEANYLGSMLIKDLRGTESTQDACAKMRKStEHMKKIP-TIILSITykGVKFIDASNKNVIAEHEIRNISCAAQDPEDL 996
Cdd:cd13168      2 LYKALYLGQVEVGEDGGVEQIESAAIIVVLE-SDLTPKEvLLELGEI--GVTVWDKSTSEVLFKHSFPEISSCGRRVDDP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720389696  997 CTFAYITKDLQTS---HHYCHVFSTVDVNLTYEIILTLGQAF 1035
Cdd:cd13168     79 NYFAYIAGDTPCSlakHFVCYVFEAADEEEAETILQGIAQGF 120
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 746-806 1.89e-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: 43.46  E-value: 1.89e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696  746 GVSPTSVPSWLDSLGLQDYVHSFLSSGyssIDTVKNLWEL--ELVNVLKVHLLGHRKRIIASL 806
Cdd:cd09542      1 GIPYRSVSEWLESIRMKRYILHFRSAG---LDTMECVLELtaEDLTQMGITLPGHQKRILCSI 60
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-262 2.16e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 2.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720389696  229 LHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-736 2.23e-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: 43.34  E-value: 2.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09547      5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSR--MTIDDIRRIGVTLIGHQRRIVSSIQTL 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-213 2.40e-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: 48.47  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   37 GYTPLHHAALNGHRDVVEVLLRND-ALTNVADS----KGCYPLHLAAWKGDAQIVRLLIQQGPShtrVNEQNA------L 105
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGAD---VVSPRAtgtffrP 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  106 EIRELKKYGpfdpyinaknndnETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVK------LL 179
Cdd:cd22192    128 GPKNLIYYG-------------EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydliLS 194

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720389696  180 LGAHPNLLSCSTRKH----TPLHLAARNGHKAVVQVLL 213
Cdd:cd22192    195 YDKEDDLQPLDLVPNnqglTPFKLAAKEGNIVMFQHLV 232
SAM_SARM1-like_repeat2 cd09502
SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like ...
 680-734 2.64e-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: 43.05  E-value: 2.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  680 EWLESIG--LQQYESKLLLNGFDdvRFLGSNVMEEQDLREIGISDPQHRRKLLQAAR 734
Cdd:cd09502     12 NWLQSLGpeYSQYTYQMLNAGID--RNSLPSLTEDQLLEDCGITNGIHRLRILNAIK 66
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 748-806 2.64e-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: 2.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  748 SPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 806
Cdd:cd09550      1 SCLSVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRM-NIEDIRRLGITLMGHQKKILTSI 58
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 37-61 2.85e-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: 41.86  E-value: 2.85e-05
                           10        20
                   ....*....|....*....|....*
gi 1720389696   37 GYTPLHHAALNGHRDVVEVLLRNDA 61
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGA 26
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 751-806 2.95e-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: 42.93  E-value: 2.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  751 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 806
Cdd:cd09554      5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLR-MGVTLAGHQKKILSSI 59
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 680-731 3.47e-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: 42.63  E-value: 3.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720389696  680 EWLESIGLQQYESKLLLNGFDdvrfLGS-NVMEEQDLREIGISDPQHRRKLLQ 731
Cdd:cd09497      9 DWLREFGLEEYTPNFIKAGYD----LPTiSRMTPEDLTAIGITKPGHRKKLKS 57
Ank_4 pfam13637
Ankyrin repeats (many copies);
227-263 4.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.07e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1720389696  227 SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 263
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 750-806 4.74e-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: 42.33  E-value: 4.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  750 TSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASL 806
Cdd:cd09551      7 TSVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRI-GVTLAGHQKKILNSI 62
PHA03095 PHA03095
ankyrin-like protein; Provisional
 27-186 4.85e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 4.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   27 GPNVNCVDSTGYTPLH-HAA-LNGHRDVVEVLLRNDALTNVADSKGCYPLH--LAAWKGDAQIVRLLIQQG--PSHTRVN 100
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGadVYAVDDR 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  101 EQNALE------------IRELKKYGPF--------------------------DPYI------NAKNNDNETALHCAAQ 136
Cdd:PHA03095   187 FRSLLHhhlqsfkprariVRELIRAGCDpaatdmlgntplhsmatgssckrslvLPLLiagisiNARNRYGQTPLHYAAV 266

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720389696  137 YGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLGAHPNL 186
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 37-65 5.02e-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: 41.42  E-value: 5.02e-05
                            10        20
                    ....*....|....*....|....*....
gi 1720389696    37 GYTPLHHAALNGHRDVVEVLLRNDALTNV 65
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 675-736 5.50e-05

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: 42.20  E-value: 5.50e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  675 EQSVGEWLESIGLQQYESKLLLNGFDdvrflGSNVME-EQD-LREIGISDPQHRRKLLQAARSL 736
Cdd:cd09534      3 EEFVEEWLNELNCGQYLDIFEKNLIT-----GDLLLElDKEaLKELGITKVGDRIRLLRAIKSL 61
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 745-806 6.13e-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: 42.30  E-value: 6.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASL 806
Cdd:cd09552      2 DYTSFSTVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRV-GVTLAGHQKKILNSI 62
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 676-735 6.43e-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: 41.83  E-value: 6.43e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLGsnvMEEQDL-REIGISDPQHRRKLLQAARS 735
Cdd:cd09563      7 EQVCDWLAELGLGQYVDECRRWVKSGQTLLK---ASPQELeKELGIKHPLHRKKLQLALQA 64
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 676-736 6.65e-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: 41.84  E-value: 6.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09546      4 RSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQ--VTLEDLRRLGVTLVGHQKKIMNSIQEM 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 126-158 7.76e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 7.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720389696  126 DNETALHCAA-QYGHTEVVKALLEELTDPTMRNN 158
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-736 8.39e-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: 8.39e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09551      8 SVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQ--MTSEDLLRIGVTLAGHQKKILNSIQSM 65
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 127-262 8.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 8.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  127 NETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLL--GAHPNLLSCSTRkhTPLHLAARNG 204
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMkhGAIPDVKYPDIE--SELHDAVEEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  205 HKAVVQVLLDAGM---DSNYQTEMgSALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:PHA02875    80 DVKAVEELLDLGKfadDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
PTB_X11 cd01208
X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is ...
 921-1045 9.08e-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: 44.20  E-value: 9.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  921 ANYLGSMLIKdlrgTESTQDACAKMRKSTEHMKKIPT----------IILSITYKGVKFIDASNKNVIAEHEIRNISCAA 990
Cdd:cd01208     12 ANYLGSTQLL----SERNPSKNVRMAQAQEAVSRVKApegesqpsteVDLFISTERIKVLNADTQETMMDHALRTISYIA 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  991 -----------------QDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLtyeIILTLGQAFEVAYQLALQA 1045
Cdd:cd01208     88 dignivvlmarrrmprsSSQECVETTPPSQEGKRQYKMICHVFESEDAQL---IAQSIGQAFSVAYQEFLRA 156
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-736 9.13e-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: 41.77  E-value: 9.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09554      5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQ--ISTEDLLRMGVTLAGHQKKILSSIQAM 62
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 749-802 9.72e-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: 9.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  749 PTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELvNVLKVHLLGHRKRI 802
Cdd:cd09527      2 SNIVYDWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDL-DAIGVMNPAHRKRI 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 194-221 1.06e-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: 1.06e-04
                            10        20
                    ....*....|....*....|....*...
gi 1720389696   194 HTPLHLAARNGHKAVVQVLLDAGMDSNY 221
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 745-806 1.21e-04

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: 41.55  E-value: 1.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  745 DGVSPTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 806
Cdd:cd09548      3 DFTSFCSVGEWLEAIKMERYKDNFTAAGYNSLESVARM-TIEDVMSLGITLVGHQKKIMSSI 63
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 676-729 1.34e-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: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLgsNVMEEQDLREIGISDPQHRRKL 729
Cdd:cd09543      6 RTVAEWLESIKMQQYTEHFMAAGYNSIDKV--LQMTQEDIKHIGVRLPGHQKRI 57
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 680-736 1.34e-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: 40.74  E-value: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  680 EWLESIGLQQYESKLLLNGFDDVRFLGSNVMeeQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09541      5 EWLEEAGLQHYYPAFAAGGVTSIEALAQLTM--QDYASLGVQDMEDKQKLFRLIQTL 59
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 678-732 1.53e-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: 40.76  E-value: 1.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  678 VGEWLESIGLQQYESKLLLNGFD-DVRFLgsnvMEEQDLREIGISDPQHRRKLLQA 732
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITgDVLVA----LDHEDLKEMGITSVGHRLTILKA 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 37-67 1.65e-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: 1.65e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720389696   37 GYTPLHHAAL-NGHRDVVEVLLRNDALTNVAD 67
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 37-202 1.68e-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: 45.84  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   37 GYTPLHHAALNGHRDVVEVLLRNDALTNVA---------DSKGC-----YPLHLAAWKGDAQIVRLLIQQGPShtrVNEQ 102
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPAD---ILTA 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  103 NAL--EIRELKKygpfdpyINAKNNDNETALHCAAQyghtEVVKALLEELTDPT----MRNNKFETPLDLAALYGRLEVV 176
Cdd:TIGR00870  205 DSLgnTLLHLLV-------MENEFKAEYEELSCQMY----NFALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLF 273

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720389696  177 KLLLGahpnlLSCSTRKHT-----PLHLAAR 202
Cdd:TIGR00870  274 RLKLA-----IKYKQKKFVawpngQQLLSLY 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-200 1.80e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720389696  152 DPTMRNNKFETPLDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLA 200
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 119-258 1.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  119 YINAKNNDNETALHCAAQYGHTEVVKALLEELTDPTMRNNKFETPLDLAALYGRLEVVKLLLgahPNLLSCSTrkhtplh 198
Cdd:PHA02874    27 CINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI---DNGVDTSI------- 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389696  199 LAARNGHKAVVQVLLDAGMDSNYQT-EMGSALHEAALFGKTDVVQILLAAGIDVNIKDNRG 258
Cdd:PHA02874    97 LPIPCIEKDMIKTILDCGIDVNIKDaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-256 1.86e-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: 1.86e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1720389696  227 SALHEAAL-FGKTDVVQILLAAGIDVNIKDN 256
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 194-224 2.15e-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: 2.15e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720389696  194 HTPLHLAA-RNGHKAVVQVLLDAGMDSNYQTE 224
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 126-155 2.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.25e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1720389696   126 DNETALHCAAQYGHTEVVKALLEELTDPTM 155
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 923-1018 3.41e-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: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  923 YLGSMLIKDLRGTESTQDACAKMRKSTEhmKKIPtIILSI--TYKG-VKFIDASNKNVIAEHEIRNIS-CA---AQDPED 995
Cdd:cd01211      8 YLGCAKVNAPRSETEALRIMAILREQSA--QPIK-VTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILfCArgpDGTSES 84

                           90       100
                   ....*....|....*....|...
gi 1720389696  996 LCtFAYITKDLQTSHHYCHVFST 1018
Cdd:cd01211     85 DC-FAFTWSHGETAIFQCHVFRC 106
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 676-730 3.56e-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: 39.99  E-value: 3.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  676 QSVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLL 730
Cdd:cd09542      5 RSVSEWLESIRMKRYILHFRSAGLDTMECVLE--LTAEDLTQMGITLPGHQKRIL 57
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-736 3.77e-04

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: 40.02  E-value: 3.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09553      8 TVGDWLDAIKMGRYKENFVSAGFASFDLVAQ--MTAEDLLRIGVTLAGHQKKILSSIQDM 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 195-220 5.52e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 5.52e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720389696  195 TPLHLAARNGHKAVVQVLLDAGMDSN 220
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 677-730 6.65e-04

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: 39.20  E-value: 6.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVR-FLGSNvmeEQDLREIGISDPQHRRKLL 730
Cdd:cd09490      5 DIAEWLASIHLEQYLDLFREHGYVTATdCQGIN---DSRLKQIGISPTGHRRRIL 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 44-227 9.38e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 9.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   44 AALNGHRDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIQQGPShtrvneqnaleirelkkygpfdpyINAK 123
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN------------------------VHIR 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  124 NNDNETALHCAAQYGHTEVVKAL--LEELTDPTMRNNKfetpLDLAALYGRLEVVKLLLGAHPNLLSCSTRKHTPLHLAA 201
Cdd:PLN03192   588 DANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                          170       180
                   ....*....|....*....|....*....
gi 1720389696  202 RNGHKAVVQVLLDAGMD---SNYQTEMGS 227
Cdd:PLN03192   664 AEDHVDMVRLLIMNGADvdkANTDDDFSP 692
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 749-803 1.09e-03

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: 38.43  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  749 PTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKN--LWELELVNVlKVHLLGHRKRII 803
Cdd:cd09499      2 VQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSgvMEDQDLKEI-GITDEQHRQIIL 57
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 677-735 1.09e-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: 38.69  E-value: 1.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389696  677 SVGEWLESIGLQQYESKLLLNGFDDVRFLGSnvMEEQDLREIGISDPQHRRKLL---QAARS 735
Cdd:cd09550      4 SVDDWLDSIKMGRYKDHFAAGGYSSLGMVMR--MNIEDIRRLGITLMGHQKKILtsiQVMRA 63
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 750-806 1.19e-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: 38.43  E-value: 1.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389696  750 TSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELvNVLKVHLLGHRKRIIASL 806
Cdd:cd09490      4 LDIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRL-KQIGISPTGHRRRILKQL 59
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 754-807 1.45e-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: 38.01  E-value: 1.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  754 SWLDSLGLQDYVHSFLSSGYssidtvkNLWEL-----ELVNVLKVHLLGHRKRIIASLA 807
Cdd:cd09497      9 DWLREFGLEEYTPNFIKAGY-------DLPTIsrmtpEDLTAIGITKPGHRKKLKSEIA 60
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 29-246 1.60e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   29 NVNCVDSTGYTPLHHAAL-NGHRDVVEVLLRNDALTNVADSKgcypLHLAAwKGDAQIVRLLIQqgPSHTRVNEQNALEI 107
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAIS-LEYVDAVEAILL--HLLAAFRKSGPLEL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  108 relkkygPFDPYINAKNNDnETALHCAAQYGHTEVVKALLEELTD-----------PTMRNNKF---ETPLDLAALYGRL 173
Cdd:TIGR00870  117 -------ANDQYTSEFTPG-ITALHLAAHRQNYEIVKLLLERGASvparacgdffvKSQGVDSFyhgESPLNAAACLGSP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  174 EVVKLLLGAHPNLLSCSTRKHTPLHLAA-----RNGHKAVVQ------VLLDAGMDS--------NYQTEmgSALHEAAL 234
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEELSCqmynfaLSLLDKLRDskelevilNHQGL--TPLKLAAK 266

                          250
                   ....*....|..
gi 1720389696  235 FGKTDVVQILLA 246
Cdd:TIGR00870  267 EGRIVLFRLKLA 278
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 200-262 1.69e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720389696  200 AARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 262
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 69-103 2.19e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 2.19e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720389696   69 KGCYPLHLAAWK-GDAQIVRLLIQQGPShtrVNEQN 103
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD---VNARD 33
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 749-808 2.39e-03

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: 37.50  E-value: 2.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  749 PTSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASLAD 808
Cdd:cd09491      5 PKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEA-GVTNPAHKRRLLDSLQD 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 69-95 2.53e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.53e-03
                            10        20
                    ....*....|....*....|....*..
gi 1720389696    69 KGCYPLHLAAWKGDAQIVRLLIQQGPS 95
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 208-308 4.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  208 VVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALDTVRDlpSQKSQQIAALIEDhmtg 286
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCiTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD--SKNIDTIKAIIDN---- 233

                           90       100
                   ....*....|....*....|..
gi 1720389696  287 kRSvkEVDRTSTAQLPLLSNTD 308
Cdd:PHA02876   234 -RS--NINKNDLSLLKAIRNED 252
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 126-148 4.43e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 4.43e-03
                           10        20
                   ....*....|....*....|...
gi 1720389696  126 DNETALHCAAQYGHTEVVKALLE 148
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLE 23
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 676-736 4.49e-03

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: 36.91  E-value: 4.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696  676 QSVGEWLESIGLQQYESKlllngFDDVRFLGSNV--MEEQDLREIGISDPQHRRKLLQAARSL 736
Cdd:cd09506      8 DDVGDWLESLNLGEHRER-----FMDNEIDGSHLpnLDKEDLTELGVTRVGHRMNIERALKKL 65
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 176-245 4.79e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 4.79e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389696  176 VKLLL--GAHPNLLSCSTRkhTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMG-SALHEAALFGKTDVVQILL 245
Cdd:PTZ00322    98 ARILLtgGADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGkTPLELAEENGFREVVQLLS 168
PHA02791 PHA02791
ankyrin-like protein; Provisional
 34-225 5.67e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696   34 DSTGYTPLHHAALNGHRDVVEVLLRNDALTNVADSKgcYPLHLAAWKGDAQIVRLLIQQGPSHTRVNEQnaleirelkky 113
Cdd:PHA02791    27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDK----------- 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389696  114 gpfdpyinaknndNETALHCAAQYGHTEVVKALLEELTDPTMRNNK-FETPLDLAALYGRLEVVKLLLGAHPN------L 186
Cdd:PHA02791    94 -------------GNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFYHAVMLNDVSIVSYFLSEIPStfdlaiL 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720389696  187 LSCstrkhtpLHLAARNGHKAVVQVLLDAGMDSNYQTEM 225
Cdd:PHA02791   161 LSC-------IHITIKNGHVDMMILLLDYMTSTNTNNSL 192
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 751-806 6.00e-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: 36.77  E-value: 6.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389696  751 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 806
Cdd:cd09549      9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLS-LGITSLEHQELLLAGI 63
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-253 7.47e-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: 7.47e-03
                           10        20
                   ....*....|....*....|....*..
gi 1720389696  227 SALHEAALFGKTDVVQILLAAGIDVNI 253
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 680-738 7.57e-03

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 36.12  E-value: 7.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389696  680 EWLESIGLQQYESKLLLNGFDDVRFLgsnVMEEQDLREIGISDPQHRRKLLQAARSLPK 738
Cdd:cd09520      9 ELLAKLGLEKYIDLFAQQEIDLQTFL---TLTDQDLKELGITAFGARRKMLLAISELNK 64
 
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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