NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|941804980|ref|XP_014328368|]
View 

caskin-2 isoform X5 [Xiphophorus maculatus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-224 8.48e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVA 82
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   83 QLLLssnmvsallegERGND--SLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLL 159
Cdd:COG0666   137 KLLL-----------EAGADvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLL 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  160 LDAGINVNLRNTYNQTALDIVNQfttsTASRDIKQLLREASSSLQVRAVKDYWNLHDPTALNLRA 224
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAE----NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 489-559 1.01e-39

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: 141.28  E-value: 1.01e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  489 WLPDYIPSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRLCDLQR 559
Cdd:cd09498     1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 423-488 2.28e-39

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: 140.09  E-value: 2.28e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980  423 GKDSEAIYQWLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNIPE 488
Cdd:cd09497     1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 203-264 1.62e-38

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


:

Pssm-ID: 212996  Cd Length: 62  Bit Score: 137.80  E-value: 1.62e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  203 LQVRAVKDYWNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQRGTDRVGFFPPSVVEVL 264
Cdd:cd12063     1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 851-940 2.26e-31

Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. This region is predicted to be natively unstructured. Its function is not known.


:

Pssm-ID: 465308  Cd Length: 91  Bit Score: 118.37  E-value: 2.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   851 QNKRSQSLNRYALSDGEPDEDDDLPLPSssassVTMPPYATLSRRPGRA------SGPPRQVNRSHSFAVRSRHKGPPPP 924
Cdd:pfam16907    1 PKKRSQSLNRYALSDGEPEEEEEPPLGS-----GTLGSYATLTRRPGRSqlarlqPSPEKNVNRSQSFAVRARKKGPPPP 75

                           90
                   ....*....|....*.
gi 941804980   925 PPKRMSSVSGSPTRQH 940
Cdd:pfam16907   76 PPKRLSSVSSSTSSEL 91
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1353-1415 1.35e-26

C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. Part of this region is predicted to be in coiled-coil conformation. Its function is not known.


:

Pssm-ID: 465209  Cd Length: 61  Bit Score: 103.70  E-value: 1.35e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941804980  1353 QKRLEQTSTSLEAALKVVENELAHGSSVDGCSSSSsvKAAGNILDDIGNMFDDLADQLDAMLE 1415
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESQSSGSAEV--KSAGNILDDIGNMFDDLADQLDAMLD 61
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 325-365 1.47e-08

Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this region.CASK and Caskin1 are synaptic scaffolding proteins. The binding motif on human Caskin1 is EEIWVLRK. A similar motif is found on protein MINT1 and protein TIAM1, both shown to be able to bind to CASK though the motif. MINT1 and TIAM1 are not part of this family. This region is predicted to be natively unstructured.


:

Pssm-ID: 465190  Cd Length: 55  Bit Score: 52.36  E-value: 1.47e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 941804980   325 QDIWVLRSS-PTGDRNSVGSTGSVGSSRSAGSGQSSESGRKQ 365
Cdd:pfam16600    1 EEIWVLRKPgAGGDRSSVGSTGSVGSVRSSGSGQSSHALHAG 42
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-224 8.48e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVA 82
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   83 QLLLssnmvsallegERGND--SLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLL 159
Cdd:COG0666   137 KLLL-----------EAGADvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLL 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  160 LDAGINVNLRNTYNQTALDIVNQfttsTASRDIKQLLREASSSLQVRAVKDYWNLHDPTALNLRA 224
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAE----NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 489-559 1.01e-39

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: 141.28  E-value: 1.01e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  489 WLPDYIPSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRLCDLQR 559
Cdd:cd09498     1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 423-488 2.28e-39

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: 140.09  E-value: 2.28e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980  423 GKDSEAIYQWLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNIPE 488
Cdd:cd09497     1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 203-264 1.62e-38

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212996  Cd Length: 62  Bit Score: 137.80  E-value: 1.62e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  203 LQVRAVKDYWNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQRGTDRVGFFPPSVVEVL 264
Cdd:cd12063     1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 851-940 2.26e-31

Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. This region is predicted to be natively unstructured. Its function is not known.


Pssm-ID: 465308  Cd Length: 91  Bit Score: 118.37  E-value: 2.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   851 QNKRSQSLNRYALSDGEPDEDDDLPLPSssassVTMPPYATLSRRPGRA------SGPPRQVNRSHSFAVRSRHKGPPPP 924
Cdd:pfam16907    1 PKKRSQSLNRYALSDGEPEEEEEPPLGS-----GTLGSYATLTRRPGRSqlarlqPSPEKNVNRSQSFAVRARKKGPPPP 75

                           90
                   ....*....|....*.
gi 941804980   925 PPKRMSSVSGSPTRQH 940
Cdd:pfam16907   76 PPKRLSSVSSSTSSEL 91
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1353-1415 1.35e-26

C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. Part of this region is predicted to be in coiled-coil conformation. Its function is not known.


Pssm-ID: 465209  Cd Length: 61  Bit Score: 103.70  E-value: 1.35e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941804980  1353 QKRLEQTSTSLEAALKVVENELAHGSSVDGCSSSSsvKAAGNILDDIGNMFDDLADQLDAMLE 1415
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESQSSGSAEV--KSAGNILDDIGNMFDDLADQLDAMLD 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
70-170 8.01e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 8.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    70 LDLACEFGRLKVAQLLLssnmvsallEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKaGIDINRATKAGTALHEAAL 149
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL---------ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAAR 70

                           90       100
                   ....*....|....*....|.
gi 941804980   150 YGKTEVVRLLLDAGINVNLRN 170
Cdd:pfam12796   71 SGHLEIVKLLLEKGADINVKD 91
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 495-554 3.85e-16

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: 73.84  E-value: 3.85e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   495 PSDLGEWLSVIGLPQYqKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:pfam00536    5 VEDVGEWLESIGLGQY-IDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 422-484 1.29e-15

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: 72.30  E-value: 1.29e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941804980   422 EGKDSEAIYQWLCEFQLEQYTSNFiRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYiDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 495-556 7.06e-15

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: 70.40  E-value: 7.06e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980    495 PSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRLCD 556
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-221 2.78e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   75 EFGRLKVAQLLLSSN-----MVSALLEGerGNDsLDSPST---TPLHLAARNGHK-DVIKLLLKAGIDINRATKAG-TAL 144
Cdd:PHA03095   45 EYGKTPLHLYLHYSSekvkdIVRLLLEA--GAD-VNAPERcgfTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGrTPL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  145 HeAALYGK---TEVVRLLLDAGINVNLRNTYNQTALDIvnqFTTST-ASRDIKQLLREASSSlqVRAVKDYWNlhdpTAL 220
Cdd:PHA03095  122 H-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAV---LLKSRnANVELLRLLIDAGAD--VYAVDDRFR----SLL 191


                  .
gi 941804980  221 N 221
Cdd:PHA03095  192 H 192
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 422-484 1.18e-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: 61.54  E-value: 1.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941804980    422 EGKDSEAIYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:smart00454    2 SQWSPESVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 325-365 1.47e-08

Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this region.CASK and Caskin1 are synaptic scaffolding proteins. The binding motif on human Caskin1 is EEIWVLRK. A similar motif is found on protein MINT1 and protein TIAM1, both shown to be able to bind to CASK though the motif. MINT1 and TIAM1 are not part of this family. This region is predicted to be natively unstructured.


Pssm-ID: 465190  Cd Length: 55  Bit Score: 52.36  E-value: 1.47e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 941804980   325 QDIWVLRSS-PTGDRNSVGSTGSVGSSRSAGSGQSSESGRKQ 365
Cdd:pfam16600    1 EEIWVLRKPgAGGDRSSVGSTGSVGSVRSSGSGQSSHALHAG 42
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 204-262 5.87e-08

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 50.61  E-value: 5.87e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980    204 QVRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGhihdsQRGTDRVGFFPPSVVE 262
Cdd:smart00326    4 QVRALYDY-TAQDPDELSFKKGDIITVLEKSDDGWWKG-----RLGRGKEGLFPSNYVE 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-179 1.52e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRgaasvnAPSHD-------GQIPLHLSAQYGHYEVSEMLLQhqSNPCLMNKAkktpldlace 75
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLK------CPSCDlfqrgalGETALHVAALYDNLEAAVVLME--AAPELVNEP---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   76 fgrlkvaqlllssnMVSALLEGErgndsldspstTPLHLAARNGHKDVIKLLLKAGIDINRATKAGTA------------ 143
Cdd:cd22192    82 --------------MTSDLYQGE-----------TALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyyg 136

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 941804980  144 ---LHEAALYGKTEVVRLLLDAGINVNLRNTYNQTALDI 179
Cdd:cd22192   137 ehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-135 2.02e-07

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: 48.35  E-value: 2.02e-07
                            10        20
                    ....*....|....*....|....*.
gi 941804980    110 TPLHLAARNGHKDVIKLLLKAGIDIN 135
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADIN 29
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 205-264 4.44e-05

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 42.20  E-value: 4.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   205 VRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVEVL 264
Cdd:pfam07653    2 GRVIFDY-VGTDKNGLTLKKGDVVKVLGKDNDGWWEGETG------GRVGLVPSTAVEEI 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-224 8.48e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVA 82
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   83 QLLLssnmvsallegERGND--SLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLL 159
Cdd:COG0666   137 KLLL-----------EAGADvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLL 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  160 LDAGINVNLRNTYNQTALDIVNQfttsTASRDIKQLLREASSSLQVRAVKDYWNLHDPTALNLRA 224
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAE----NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 489-559 1.01e-39

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: 141.28  E-value: 1.01e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  489 WLPDYIPSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRLCDLQR 559
Cdd:cd09498     1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 423-488 2.28e-39

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: 140.09  E-value: 2.28e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980  423 GKDSEAIYQWLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNIPE 488
Cdd:cd09497     1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 203-264 1.62e-38

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212996  Cd Length: 62  Bit Score: 137.80  E-value: 1.62e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  203 LQVRAVKDYWNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQRGTDRVGFFPPSVVEVL 264
Cdd:cd12063     1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SH3_Caskin cd11880
Src Homology 3 domain of CASK interacting protein; Caskin proteins are multidomain adaptor ...
 203-263 8.18e-37

Src Homology 3 domain of CASK interacting protein; Caskin proteins are multidomain adaptor proteins that contain six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. There are two Caskin proteins called Caskin1 and Caskin2. Caskin1 binds to the multidomain scaffolding protein CASK through the CaM domain in competition with Munc-interacting protein 1 (Mint1). CASK participates in one of two evolutionarily conserved tripartite complexes containing either Mint1 and Velis or Caskin1 and Velis. Caskin1 may play a role in infantile myoclonic epilepsy. There is not much known about Caskin2; despite sharing a domain architecture with Caskin1, Caskin2 does not bind CASK. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212813  Cd Length: 61  Bit Score: 132.68  E-value: 8.18e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  203 LQVRAVKDYWNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQRGTDRVGFFPPSVVEV 263
Cdd:cd11880     1 LQVRATKDYWNNHDLTALNVRAGDIITVLEQHPDGRWKGHIHDNQTGNDRVGYFPPSLVEV 61
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 851-940 2.26e-31

Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. This region is predicted to be natively unstructured. Its function is not known.


Pssm-ID: 465308  Cd Length: 91  Bit Score: 118.37  E-value: 2.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   851 QNKRSQSLNRYALSDGEPDEDDDLPLPSssassVTMPPYATLSRRPGRA------SGPPRQVNRSHSFAVRSRHKGPPPP 924
Cdd:pfam16907    1 PKKRSQSLNRYALSDGEPEEEEEPPLGS-----GTLGSYATLTRRPGRSqlarlqPSPEKNVNRSQSFAVRARKKGPPPP 75

                           90
                   ....*....|....*.
gi 941804980   925 PPKRMSSVSGSPTRQH 940
Cdd:pfam16907   76 PPKRLSSVSSSTSSEL 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-177 1.74e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 1.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVA 82
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   83 QLLLssnmvsallegERGND--SLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLL 159
Cdd:COG0666   203 KLLL-----------EAGADvnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLL 271

                         170
                  ....*....|....*...
gi 941804980  160 LDAGINVNLRNTYNQTAL 177
Cdd:COG0666   272 LLALLLLAAALLDLLTLL 289
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1353-1415 1.35e-26

C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. Part of this region is predicted to be in coiled-coil conformation. Its function is not known.


Pssm-ID: 465209  Cd Length: 61  Bit Score: 103.70  E-value: 1.35e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941804980  1353 QKRLEQTSTSLEAALKVVENELAHGSSVDGCSSSSsvKAAGNILDDIGNMFDDLADQLDAMLE 1415
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESQSSGSAEV--KSAGNILDDIGNMFDDLADQLDAMLD 61
SH3_Caskin1 cd12062
Src Homology 3 domain of CASK interacting protein 1; Caskin1 is a multidomain adaptor protein ...
 203-264 2.15e-24

Src Homology 3 domain of CASK interacting protein 1; Caskin1 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It is expressed at high levels in the brain and is localized in presynaptic regions. It binds to the multidomain scaffolding protein CASK through the CaMK domain in competition with Munc-interacting protein 1 (Mint1). CASK participates in one of two evolutionarily conserved tripartite complexes containing either Mint1 and Velis or Caskin1 and Velis. Caskin1 may play a role in infantile myoclonic epilepsy. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212995  Cd Length: 62  Bit Score: 97.38  E-value: 2.15e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  203 LQVRAVKDYWNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQRGTDRVGFFPPSVVEVL 264
Cdd:cd12062     1 LQVRALKDYCNNYDLTSLNIKAGDVITVLEQHPDGRWKGCIHDNRTGNDRVGYFPSSLVEAI 62
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-177 1.83e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   61 LMNKAKKTPLDLACEFGRLKVAQLLLSSNMVSALLEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKA 140
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 941804980  141 G-TALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:COG0666   120 GeTPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
70-170 8.01e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 8.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    70 LDLACEFGRLKVAQLLLssnmvsallEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKaGIDINRATKAGTALHEAAL 149
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL---------ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAAR 70

                           90       100
                   ....*....|....*....|.
gi 941804980   150 YGKTEVVRLLLDAGINVNLRN 170
Cdd:pfam12796   71 SGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-136 2.92e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 2.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    37 LHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQLLLSSNMVSALLEGErgndsldspstTPLHLAA 116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR-----------TALHYAA 69

                           90       100
                   ....*....|....*....|
gi 941804980   117 RNGHKDVIKLLLKAGIDINR 136
Cdd:pfam12796   70 RSGHLEIVKLLLEKGADINV 89
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 495-554 3.85e-16

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: 73.84  E-value: 3.85e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   495 PSDLGEWLSVIGLPQYqKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:pfam00536    5 VEDVGEWLESIGLGQY-IDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 422-484 1.29e-15

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: 72.30  E-value: 1.29e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941804980   422 EGKDSEAIYQWLCEFQLEQYTSNFiRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYiDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 495-556 7.06e-15

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: 70.40  E-value: 7.06e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980    495 PSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRLCD 556
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 495-552 7.94e-15

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


Pssm-ID: 188890  Cd Length: 63  Bit Score: 70.24  E-value: 7.94e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  495 PSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVK 552
Cdd:cd09491     5 PKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQ 62
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
495-554 1.61e-13

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 66.52  E-value: 1.61e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   495 PSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:pfam07647    6 LESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-177 2.35e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.29  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   61 LMNKAKKTPLDLACEFGRLKVAQLLLSSNMVSALLEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKA 140
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 941804980  141 G-TALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:COG0666    87 GnTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 431-484 2.47e-13

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: 65.71  E-value: 2.47e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  431 QWLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09488     7 EWLESIKMGRYKENFTAAGYtSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 429-483 4.93e-13

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: 64.95  E-value: 4.93e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  429 IYQWLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISK 483
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-221 2.78e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   75 EFGRLKVAQLLLSSN-----MVSALLEGerGNDsLDSPST---TPLHLAARNGHK-DVIKLLLKAGIDINRATKAG-TAL 144
Cdd:PHA03095   45 EYGKTPLHLYLHYSSekvkdIVRLLLEA--GAD-VNAPERcgfTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGrTPL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  145 HeAALYGK---TEVVRLLLDAGINVNLRNTYNQTALDIvnqFTTST-ASRDIKQLLREASSSlqVRAVKDYWNlhdpTAL 220
Cdd:PHA03095  122 H-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAV---LLKSRnANVELLRLLIDAGAD--VYAVDDRFR----SLL 191


                  .
gi 941804980  221 N 221
Cdd:PHA03095  192 H 192
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 3-198 3.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSV-LLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKV 81
Cdd:PHA02875   71 ELHDAVEEGDVKAVeELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   82 AQLLLSSNmvsALLEGErgndslDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG--TALHEAALYGKTEVVRLL 159
Cdd:PHA02875  151 IELLIDHK---ACLDIE------DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLF 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 941804980  160 LDAGINVNLRNTY---NQTALDIVNQFTTSTASRDIKQLLRE 198
Cdd:PHA02875  222 IKRGADCNIMFMIegeECTILDMICNMCTNLESEAIDALIAD 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 3-180 3.54e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHY-----EVSEMLLQHQSNPCLMNKAKKTPLDLAcefg 77
Cdd:PHA03100   38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA---- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   78 rlkVAQLLLSSNMVSALLEgeRGND--SLDSPSTTPLHLAARNGHKD--VIKLLLKAGIDINRATK-------------- 139
Cdd:PHA03100  114 ---ISKKSNSYSIVEYLLD--NGANvnIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRvnyllsygvpinik 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 941804980  140 ---AGTALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTALDIV 180
Cdd:PHA03100  189 dvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 497-553 6.82e-12

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: 61.49  E-value: 6.82e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  497 DLGEWLSVIGLPQYQKRLCDNgYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKR 553
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKN-EIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
422-484 8.55e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 8.55e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941804980   422 EGKDSEAIYQWLCEFQLEQYTSNFIRAGYDVPT-ISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:pfam07647    2 ESWSLESVADWLRSIGLEQYTDNFRDQGITGAElLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 17-180 1.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   17 LLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVaqlllssnmVSALLE 96
Cdd:PHA02878  152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPI---------VHILLE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   97 GERGNDSLDSPSTTPLHLA-ARNGHKDVIKLLLKAGIDIN-RATKAG-TALHEAAlygKTE-VVRLLLDAGINVNLRNTY 172
Cdd:PHA02878  223 NGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNaKSYILGlTALHSSI---KSErKLKLLLEYGADINSLNSY 299


                  ....*...
gi 941804980  173 NQTALDIV 180
Cdd:PHA02878  300 KLTPLSSA 307
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 422-484 1.18e-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: 61.54  E-value: 1.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941804980    422 EGKDSEAIYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:smart00454    2 SQWSPESVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 5.98e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 5.98e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 941804980   109 TTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLLL 160
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 499-554 1.15e-10

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: 58.46  E-value: 1.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  499 GEWLSVIGLPQYQKRLCDNGYDSI-----AIVKDitwEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09499     6 GQWLESIGLPQYESKLLLNGFDDVdflgsGVMED---QDLKEIGITDEQHRQIILQAARSL 63
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 5-105 1.40e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    5 HYAAwQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQL 84
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90       100
                  ....*....|....*....|.
gi 941804980   85 LLSSNMVSALLEGERGNDSLD 105
Cdd:PTZ00322  167 LSRHSQCHFELGANAKPDSFT 187
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 500-554 1.52e-10

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: 58.23  E-value: 1.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  500 EWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09527     7 DWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDLDAIGVMNPAHRKRILEAVRRL 61
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 498-554 3.31e-10

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: 56.85  E-value: 3.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  498 LGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09488     5 VGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 426-484 6.45e-10

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: 56.30  E-value: 6.45e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  426 SEAIYQWLCEFQLEQYTSNFIRAGYDVPTISR-MTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09527     2 SNIVYDWLRTLQLEQYAEKFVDNGYDDLEVCKqIGDPDLDAIGVMNPAHRKRILEAVRRL 61
PHA03095 PHA03095
ankyrin-like protein; Provisional
 3-177 1.07e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVL-LLLRGAASVNAPSHDGQIPLH--LSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGR- 78
Cdd:PHA03095   86 PLHLYLYNATTLDVIkLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNa 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   79 -LKVAQLLL--------------------------SSNMVSALLEGERGNDSLDSPSTTPLHLAARNGHKDVIKL--LLK 129
Cdd:PHA03095  166 nVELLRLLIdagadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLI 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 941804980  130 AGIDINRATKAG-TALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:PHA03095  246 AGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 498-554 1.26e-09

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: 55.71  E-value: 1.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  498 LGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09546     6 VGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEM 62
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 31-177 1.73e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   31 HDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQLLLSSNMVSallegergNDSLDSPSTT 110
Cdd:PHA02875   33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA--------DDVFYKDGMT 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  111 PLHLAARNGHKDVIKLLLKAGIDIN-RATKAGTALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:PHA02875  105 PLHLATILKKLDIMKLLIARGADPDiPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 491-554 2.29e-09

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: 55.04  E-value: 2.29e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  491 PDYIP-SDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09553     1 PDYTTfTTVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDM 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 3-225 3.58e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHY---AAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYE-VSEMLLQHQSNPCLMNKAKKTPLD--LACEF 76
Cdd:PHA03095   50 PLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHvyLSGFN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   77 GRLKVAQLLLssnmvsallegERGND--SLDSPSTTPLH--LAARNGHKDVIKLLLKAGIDInRATKA--GTALHEAALY 150
Cdd:PHA03095  130 INPKVIRLLL-----------RKGADvnALDLYGMTPLAvlLKSRNANVELLRLLIDAGADV-YAVDDrfRSLLHHHLQS 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  151 GKT--EVVRLLLDAGINVNLRNTYNQTALDIVNQFTTSTASrDIKQLLrEASSSLQVRavkdywNLHDPTALNLRAG 225
Cdd:PHA03095  198 FKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRS-LVLPLL-IAGISINAR------NRYGQTPLHYAAV 266
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-179 4.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 4.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAwQGKSDSVLL--LLRGAASVNAPSHDGQIPLHLSAQYGH-YEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRL 79
Cdd:PHA02876  276 PLHHAS-QAPSLSRLVpkLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   80 KvaqlllssNMVSALLEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINR-ATKAGTALHeAALYG------- 151
Cdd:PHA02876  355 K--------DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAlSQKIGTALH-FALCGtnpymsv 425

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  152 -----------------------------KTEVVRLLLDAGINVNLRNTYNQTALDI 179
Cdd:PHA02876  426 ktlidrganvnsknkdlstplhyackkncKLDVIEMLLDNGADVNAINIQNQYPLLI 482
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 491-554 6.65e-09

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: 53.50  E-value: 6.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  491 PDYIP-SDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09551     1 PDFTAfTSVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSM 65
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-135 7.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 7.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    1 MRPLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLK 80
Cdd:PHA02875  103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980   81 VAQLLLSSnmvsalleGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDIN 135
Cdd:PHA02875  183 ICKMLLDS--------GANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 500-554 9.14e-09

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


Pssm-ID: 188954  Cd Length: 69  Bit Score: 53.39  E-value: 9.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  500 EWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09555    11 AWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLL 65
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-177 1.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNP-----CLMNKAKKTPLDLA---- 73
Cdd:PHA02876  181 PIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNInkndlSLLKAIRNEDLETSllly 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   74 -----------CEFGRLKVAQLLLS-SNMVSALLegERGND--SLDSPSTTPLHLAARNGH-KDVIKLLLKAGIDINRAT 138
Cdd:PHA02876  261 dagfsvnsiddCKNTPLHHASQAPSlSRLVPKLL--ERGADvnAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 941804980  139 KA-GTALHEAALYGK-TEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:PHA02876  339 RLyITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPI 379
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 325-365 1.47e-08

Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this region.CASK and Caskin1 are synaptic scaffolding proteins. The binding motif on human Caskin1 is EEIWVLRK. A similar motif is found on protein MINT1 and protein TIAM1, both shown to be able to bind to CASK though the motif. MINT1 and TIAM1 are not part of this family. This region is predicted to be natively unstructured.


Pssm-ID: 465190  Cd Length: 55  Bit Score: 52.36  E-value: 1.47e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 941804980   325 QDIWVLRSS-PTGDRNSVGSTGSVGSSRSAGSGQSSESGRKQ 365
Cdd:pfam16600    1 EEIWVLRKPgAGGDRSSVGSTGSVGSVRSSGSGQSSHALHAG 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 3-167 1.70e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLqhQSNPC---LMNKAKKTPLDLACEFGRL 79
Cdd:PHA02875   38 PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL--DLGKFaddVFYKDGMTPLHLATILKKL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   80 KVAQLLLSsnmvsallegeRGNDSlDSPST---TPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEV 155
Cdd:PHA02875  116 DIMKLLIA-----------RGADP-DIPNTdkfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGcTPLIIAMAKGDIAI 183

                         170
                  ....*....|..
gi 941804980  156 VRLLLDAGINVN 167
Cdd:PHA02875  184 CKMLLDSGANID 195
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 3-135 2.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNpcLMNKAKK--TPLDLACEFGRlK 80
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH--IMNKCKNgfTPLHNAIIHNR-S 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980   81 VAQLLLSSNMVsallegergNDSlDSPSTTPLHLAARNG-HKDVIKLLLKAGIDIN 135
Cdd:PHA02874  237 AIELLINNASI---------NDQ-DIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-135 2.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACefGRLK-- 80
Cdd:PHA02878  171 ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdy 248

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   81 -VAQLLLssnmvsallegERGNDsLDSPST----TPLHLAARNghKDVIKLLLKAGIDIN 135
Cdd:PHA02878  249 dILKLLL-----------EHGVD-VNAKSYilglTALHSSIKS--ERKLKLLLEYGADIN 294
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 2.64e-08

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: 51.96  E-value: 2.64e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980  432 WLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNI 486
Cdd:cd09551    12 WLSAIKMSQYRDNFLSSGFtSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMRV 67
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 204-257 2.88e-08

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 51.31  E-value: 2.88e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 941804980  204 QVRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSqrgtdRVGFFP 257
Cdd:cd00174     1 YARALYDY-EAQDDDELSFKKGDIITVLEKDDDGWWEGELNGG-----REGLFP 48
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 432-485 3.09e-08

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: 51.91  E-value: 3.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  432 WLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEISKLN 485
Cdd:cd09498    13 WLSLLGLPQYHKVLVENGYDsIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLK 67
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 422-481 3.24e-08

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


Pssm-ID: 188942  Cd Length: 70  Bit Score: 51.76  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  422 EGKDSEAIYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEI 481
Cdd:cd09543     1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNsIDKVLQMTQEDIKHIGVRLPGHQKRIAYSI 61
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 491-552 3.29e-08

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: 51.93  E-value: 3.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941804980  491 PDYIP-SDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVK 552
Cdd:cd09552     1 PDYTSfSTVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQ 63
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 205-259 3.68e-08

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 51.13  E-value: 3.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  205 VRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQRGTDRvGFFPPS 259
Cdd:cd11883     2 VVALYDF-TPKSKNQLSFKAGDIIYVLNKDPSGWWDGVIISSSGKVKR-GWFPSN 54
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 428-486 3.98e-08

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: 51.43  E-value: 3.98e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  428 AIYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNI 486
Cdd:cd09547     5 TVSDWLDSIKMGQYKNNFMAAGFTtLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 496-554 4.73e-08

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: 51.02  E-value: 4.73e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  496 SDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09554     4 GSVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAM 62
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 204-262 5.87e-08

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 50.61  E-value: 5.87e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980    204 QVRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGhihdsQRGTDRVGFFPPSVVE 262
Cdd:smart00326    4 QVRALYDY-TAQDPDELSFKKGDIITVLEKSDDGWWKG-----RLGRGKEGLFPSNYVE 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-180 8.63e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 8.63e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980   127 LLKAG-IDINRATKAG-TALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTALDIV 180
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 4-210 1.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    4 LHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQ 83
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   84 LLLsSNMVSALLEGERGndsldspsTTPLHLAARNgHKDVIKLLLKAGIDINRATKAGTALHEAALYG-KTEVVRLLLDA 162
Cdd:PHA02874  208 LLI-DHGNHIMNKCKNG--------FTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 941804980  163 GINVNLRNTYNQTALDIVNQFTTSTASrdIKQLLREASSSLQVRAVKD 210
Cdd:PHA02874  278 KADISIKDNKGENPIDTAFKYINKDPV--IKDIIANAVLIKEADKLKD 323
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-179 1.52e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRgaasvnAPSHD-------GQIPLHLSAQYGHYEVSEMLLQhqSNPCLMNKAkktpldlace 75
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLK------CPSCDlfqrgalGETALHVAALYDNLEAAVVLME--AAPELVNEP---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   76 fgrlkvaqlllssnMVSALLEGErgndsldspstTPLHLAARNGHKDVIKLLLKAGIDINRATKAGTA------------ 143
Cdd:cd22192    82 --------------MTSDLYQGE-----------TALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyyg 136

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 941804980  144 ---LHEAALYGKTEVVRLLLDAGINVNLRNTYNQTALDI 179
Cdd:cd22192   137 ehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-135 2.02e-07

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: 48.35  E-value: 2.02e-07
                            10        20
                    ....*....|....*....|....*.
gi 941804980    110 TPLHLAARNGHKDVIKLLLKAGIDIN 135
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADIN 29
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 431-481 2.03e-07

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: 49.64  E-value: 2.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 941804980  431 QWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEI 481
Cdd:cd09548    12 EWLEAIKMERYKDNFTAAGYNsLESVARMTIEDVMSLGITLVGHQKKIMSSI 63
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 428-481 2.21e-07

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: 49.23  E-value: 2.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  428 AIYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEI 481
Cdd:cd09542     6 SVSEWLESIRMKRYILHFRSAGLDtMECVLELTAEDLTQMGITLPGHQKRILCSI 60
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 497-554 2.84e-07

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: 48.47  E-value: 2.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  497 DLGEWLSVIGLPQYQKRLCDNGYDSIAIVKdITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09533     1 DVADWLSSLGLPQYEDQFIENGITGDVLVA-LDHEDLKEMGITSVGHRLTILKAVYEL 57
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 3-135 2.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQ--GKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHY--EVSEMLLQHQSNPCLMNKAK------------ 66
Cdd:PHA03100  109 PLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRVNyllsygvpinik 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980   67 ----KTPLDLACEFGRLKVAQLLL----SSNMVSallegERGNdsldspstTPLHLAARNGHKDVIKLLLKAGIDIN 135
Cdd:PHA03100  189 dvygFTPLHYAVYNNNPEFVKYLLdlgaNPNLVN-----KYGD--------TPLHIAILNNNKEIFKLLLNNGPSIK 252
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-174 3.69e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQ--HQSNPclmnkakKTPLDLACefgrlk 80
Cdd:PLN03192  561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDP-------HAAGDLLC------ 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   81 vaqlllssnmvsallegergndsldspsttplhLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLL 159
Cdd:PLN03192  628 ---------------------------------TAAKRNDLTAMKELLKQGLNVDSEDHQGaTALQVAMAEDHVDMVRLL 674

                         170
                  ....*....|....*
gi 941804980  160 LDAGINVNLRNTYNQ 174
Cdd:PLN03192  675 IMNGADVDKANTDDD 689
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 495-550 4.14e-07

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: 48.46  E-value: 4.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  495 PSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDItWE-DLQEI-GITKLGHQKKlMLA 550
Cdd:cd09500     5 PASVSEWLDSIGLGDYIETFLKHGYTSMERVKRI-WEvELTNVlEINKLGHRKR-ILA 60
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 4.27e-07

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: 48.49  E-value: 4.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980  432 WLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNI 486
Cdd:cd09553    12 WLDAIKMGRYKENFVSAGFaSFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRL 67
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 427-486 4.27e-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: 48.39  E-value: 4.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  427 EAIYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNI 486
Cdd:cd09546     4 RSVGEWLEAIKMGRYTEIFMENGYSsMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMRV 64
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 498-548 4.44e-07

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: 48.49  E-value: 4.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 941804980  498 LGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLM 548
Cdd:cd09548    10 VGEWLEAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIM 60
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 498-552 4.48e-07

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: 48.32  E-value: 4.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  498 LGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVK 552
Cdd:cd09550     5 VDDWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQ 59
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 36-177 7.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   36 PLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQLLL--------------SSNMVSALLEGERGN 101
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciEKDMIKTILDCGIDV 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  102 DSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAGT-ALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:PHA02874  118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCyPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 430-486 7.94e-07

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


Pssm-ID: 188954  Cd Length: 69  Bit Score: 47.62  E-value: 7.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  430 YQWLCEFQLEQYTSNFIRAG---YDVptISRMTPEDLTAIGVTKPGHRKKISSEISKLNI 486
Cdd:cd09555    10 QAWLSAIGLECYQDNFSKFGlctFSD--VAQLSLEDLPALGITLAGHQKKLLHHIQLLQQ 67
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-484 8.49e-07

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: 47.64  E-value: 8.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 941804980  432 WLCEFQLEQYTSNFIRAGYDVP-TISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09545     9 WLQAIKMERYKDNFTAAGYTTLeAVVHMNQDDLARIGISAIAHQNKILSSVQGM 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-139 1.01e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 46.51  E-value: 1.01e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 941804980   110 TPLHLAA-RNGHKDVIKLLLKAGIDINRATK 139
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 431-488 1.74e-06

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: 46.78  E-value: 1.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  431 QWLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLNIPE 488
Cdd:cd09554     8 EWLRAIKMERYEDSFLQAGFtTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMGIQN 66
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 498-554 2.01e-06

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: 46.87  E-value: 2.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  498 LGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09545     6 VDDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQGM 62
Ank_4 pfam13637
Ankyrin repeats (many copies);
68-128 2.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 2.02e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980    68 TPLDLACEFGRLKVAQLLLSSnmvsalleGERGNDSlDSPSTTPLHLAARNGHKDVIKLLL 128
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--------GADINAV-DGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-135 2.36e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 45.33  E-value: 2.36e-06
                           10        20
                   ....*....|....*....|....*.
gi 941804980   110 TPLHLAARNGHKDVIKLLLKAGIDIN 135
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 431-487 2.54e-06

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: 46.14  E-value: 2.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  431 QWLCEFQLEQYTSNFIRAGYD-VPTISR--MTPEDLTAIGVTKPGHRKKISSEISKLNIP 487
Cdd:cd09499     7 QWLESIGLPQYESKLLLNGFDdVDFLGSgvMEDQDLKEIGITDEQHRQIILQAARSLPKK 66
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 498-554 4.85e-06

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: 45.26  E-value: 4.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  498 LGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09547     6 VSDWLDSIKMGQYKNNFMAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTL 62
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 500-552 5.08e-06

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: 45.38  E-value: 5.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 941804980  500 EWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVK 552
Cdd:cd09542     9 EWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 61
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 431-481 5.16e-06

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: 45.38  E-value: 5.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 941804980  431 QWLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEI 481
Cdd:cd09552    11 EWLDAIKMGQYKESFANAGFtSFDVVSQMTMEDILRVGVTLAGHQKKILNSI 62
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 4-85 5.62e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.95  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    4 LHYAAWQGKSD---SVLLLLRGAASVNAP-SHDGQIPLHLSAQYGHYEVSEMLLQH-QSNPCLMNKAKKTPLDLACEFGR 78
Cdd:PHA02736   59 VHIVSNPDKADpqeKLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHD 138


                  ....*..
gi 941804980   79 LKVAQLL 85
Cdd:PHA02736  139 AKMMNIL 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
1-53 7.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 7.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 941804980     1 MRPLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLL 53
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-63 7.58e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 7.58e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980     3 PLHYAAWQGKSDSVLLLLRGAAsVNAPSHdGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMN 63
Cdd:pfam12796   33 ALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SH3_Stac_1 cd11833
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ...
 220-261 1.08e-05

First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins; Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212767 [Multi-domain]  Cd Length: 53  Bit Score: 44.03  E-value: 1.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 941804980  220 LNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVV 261
Cdd:cd11833    16 LEMRPGDKITLLDDSNEDWWKGKIE------DRVGFFPANFV 51
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 438-485 1.12e-05

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: 44.21  E-value: 1.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 941804980  438 LEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLN 485
Cdd:cd09520    16 LEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELN 63
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 142-170 1.41e-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: 43.05  E-value: 1.41e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 941804980   142 TALHEAAL-YGKTEVVRLLLDAGINVNLRN 170
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 500-547 1.42e-05

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: 44.44  E-value: 1.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 941804980  500 EWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKL 547
Cdd:cd09543    10 EWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKHIGVRLPGHQKRI 57
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 496-554 1.42e-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: 1.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  496 SDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09549     8 GSVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQAL 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
36-86 1.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 941804980    36 PLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQLLL 86
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-180 1.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.53e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 941804980   142 TALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTALDIV 180
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 497-554 1.63e-05

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: 43.85  E-value: 1.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  497 DLGEWLSVIGLPQYQKRLCDNGYDSiAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09506     9 DVGDWLESLNLGEHRERFMDNEIDG-SHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-211 1.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980    3 PLHYAAWQGKSDSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKtpLDLACEFGRLKVA 82
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA--IKDAFNNRNVEIF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   83 QLLLSSNmvsalLEGERGND--SLDSPSTTPLHLAarnghkDVIKLLLKAGIDINRATK--AGTALHEAALYGKTEVVRL 158
Cdd:PHA02878  118 KIILTNR-----YKNIQTIDlvYIDKKSKDDIIEA------EITKLLLSYGADINMKDRhkGNTALHYATENKDQRLTEL 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  159 LLDAGINVNLRNTYNQTAL---------DIVNQFTTSTASRDIKQLLREASSSLQVRAVKDY 211
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLhhavkhynkPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 431-484 1.95e-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: 43.70  E-value: 1.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 941804980  431 QWLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09549    12 EWLEALDLCRYKDNFAAAGYgSLEAVARMTAQDVLSLGITSLEHQELLLAGIQAL 66
SH3_CRK_C cd11759
C-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
 213-263 2.65e-05

C-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The C-terminal SH3 domain of CRK has not been shown to bind any target protein; it acts as a negative regulator of CRK function by stabilizing a structure that inhibits the access by target proteins to the N-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212693 [Multi-domain]  Cd Length: 57  Bit Score: 43.24  E-value: 2.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 941804980  213 NLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVEV 263
Cdd:cd11759    13 NAYDKTALALEVGDLVKVTKINVSGQWEGELN------GKVGHFPFTHVEL 57
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 433-484 2.99e-05

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 43.05  E-value: 2.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 941804980  433 LCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09523    12 LNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQEL 63
SAM_SASH1_repeat2 cd09492
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ...
 496-552 3.00e-05

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: 43.27  E-value: 3.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  496 SDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVK 552
Cdd:cd09492     8 SSVSDWLVSIGLPMYSPPLLEAGFSTLSRVSSLSETCLREAGITEERHIRKLLSAAR 64
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 205-264 4.44e-05

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 42.20  E-value: 4.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   205 VRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVEVL 264
Cdd:pfam07653    2 GRVIFDY-VGTDKNGLTLKKGDVVKVLGKDNDGWWEGETG------GRVGLVPSTAVEEI 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 87-159 5.34e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 5.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941804980   87 SSNMVSALLEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDIN-RATKAGTALHEAALYGKTEVVRLL 159
Cdd:PLN03192  537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHiRDANGNTALWNAISAKHHKIFRIL 610
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-172 5.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   14 DSVLLLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQLLLsSNMVSA 93
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   94 LLEGERGNdsldspstTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEVVRLLLDAGINVNLRNTY 172
Cdd:PHA02874  184 NVKDNNGE--------SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGfTPLHNAIIHNRSAIELLINNASINDQDIDGS 255
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 485-554 6.25e-05

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 42.40  E-value: 6.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  485 NIPEWLPDyipsDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKdITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09507     1 PVTNWTTE----EVGAWLESLQLGEYRDIFARNDIRGSELLH-LERRDLKDLGITKVGHVKRILQAIKDL 65
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 205-261 6.61e-05

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212884  Cd Length: 53  Bit Score: 41.71  E-value: 6.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  205 VRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIhdsqrgTDRVGFFPPSVV 261
Cdd:cd11951     2 VQAQYDF-SAEDPSQLSFRRGDIIEVLDCPDPNWWRGRI------SGRVGFFPRNYV 51
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 79-160 7.44e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   79 LKVAQLLLSSNMVSA--LLEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEAALYGKTEV 155
Cdd:PTZ00322   84 VELCQLAASGDAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGkTPLELAEENGFREV 163


                  ....*
gi 941804980  156 VRLLL 160
Cdd:PTZ00322  164 VQLLS 168
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 429-477 8.31e-05

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: 41.90  E-value: 8.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 941804980  429 IYQWLCEFQLEQYTSNFIRAGYDVPTISR-MTPEDLTAIGVTKPGHRKKI 477
Cdd:cd09490     6 IAEWLASIHLEQYLDLFREHGYVTATDCQgINDSRLKQIGISPTGHRRRI 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-207 9.36e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  107 PSTTPLHLAAR-NGHKDVIKLLLKAGIDI-NRATKAGTALHEAALYGKTEVVRLLLDAGIN-VNLRNTYN----QTALDI 179
Cdd:cd22192    16 ISESPLLLAAKeNDVQAIKKLLKCPSCDLfQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHI 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 941804980  180 --VNQFTTStasrdIKQLLREASSSLQVRA 207
Cdd:cd22192    96 avVNQNLNL-----VRELIARGADVVSPRA 120
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 495-554 1.00e-04

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


Pssm-ID: 188933  Cd Length: 62  Bit Score: 41.43  E-value: 1.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  495 PSDLGEWLSVIGLPQYQKRLCDNGYDSiAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09534     3 EEFVEEWLNELNCGQYLDIFEKNLITG-DLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 496-554 1.02e-04

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 41.85  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  496 SDLGEWLSVIGLPQYQKRLCD-NGYDSIAIVKdITWEDLQE--IGITKLGHQKKLMLAVKRL 554
Cdd:cd09515     7 EDVAKWLKKEGFSKYVDLLCNkHRIDGKVLLS-LTEEDLRSppLEIKVLGDIKRLWLAIRKL 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
 122-177 1.27e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941804980  122 DVIKLLLKAGIDIN-RATKAGTALHeaaLYGKT------EVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:PHA03095   28 EEVRRLLAAGADVNfRGEYGKTPLH---LYLHYssekvkDIVRLLLEAGADVNAPERCGFTPL 87
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 426-484 1.28e-04

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: 41.24  E-value: 1.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941804980  426 SEAIYQWLCEFQLEQYTSNFIR---AGYDVPTISRmtpEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09507     7 TEEVGAWLESLQLGEYRDIFARndiRGSELLHLER---RDLKDLGITKVGHVKRILQAIKDL 65
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 432-484 1.28e-04

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 41.54  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 941804980  432 WLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09506    13 WLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 422-477 1.29e-04

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: 41.52  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  422 EGKDSEAIYQWLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAI-GVTKPGHRKKI 477
Cdd:cd09500     1 DGNSPASVSEWLDSIGLGDYIETFLKHGYtSMERVKRIWEVELTNVlEINKLGHRKRI 58
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-147 1.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980    94 LLE-GERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAG-TALHEA 147
Cdd:pfam13857    1 LLEhGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGlTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
18-73 1.80e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980    18 LLLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLA 73
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 142-168 1.93e-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: 39.88  E-value: 1.93e-04
                            10        20
                    ....*....|....*....|....*..
gi 941804980    142 TALHEAALYGKTEVVRLLLDAGINVNL 168
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 204-263 1.95e-04

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 40.39  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  204 QVRAVKDYwNLHDPTALNLRAGDLIMVLEQHS-DGRWKGHihdSQRGtdRVGFFPPSVVEV 263
Cdd:cd11763     1 KVRALYDF-DSQPSGELSLRAGEVLTITRQDVgDGWLEGR---NSRG--EVGLFPSSYVEI 55
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-481 2.15e-04

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: 40.62  E-value: 2.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 941804980  432 WLCEFQLEQYTSNFIRAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISSEI 481
Cdd:cd09550     8 WLDSIKMGRYKDHFAAGGYsSLGMVMRMNIEDIRRLGITLMGHQKKILTSI 58
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-177 2.43e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 2.43e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 941804980   144 LHEAALYGKTEVVRLLLDAGINVNLRNTYNQTAL 177
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 204-263 2.80e-04

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 39.92  E-value: 2.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  204 QVRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVEV 263
Cdd:cd11805     1 RVQALYDF-NPQEPGELEFRRGDIITVLDSSDPDWWKGELR------GRVGIFPANYVQP 53
SH3_9 pfam14604
Variant SH3 domain;
207-262 4.09e-04

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 39.52  E-value: 4.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980   207 AVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGhihdsQRGTdRVGFFPPSVVE 262
Cdd:pfam14604    1 ALYPY-EPKDDDELSLQRGDVITVIEESEDGWWEG-----INTG-RTGLVPANYVE 49
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 496-554 4.21e-04

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: 39.97  E-value: 4.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  496 SDLGEWLSVIGLPQYQKRLCDNGYDsIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09520     5 SDLPELLAKLGLEKYIDLFAQQEID-LQTFLTLTDQDLKELGITAFGARRKMLLAISEL 62
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 220-262 5.54e-04

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 39.17  E-value: 5.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 941804980  220 LNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVE 262
Cdd:cd11766    16 LSLRKGDRVLVLEKSSDGWWRGECN------GQVGWFPSNYVT 52
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 142-167 6.98e-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: 6.98e-04
                           10        20
                   ....*....|....*....|....*.
gi 941804980   142 TALHEAALYGKTEVVRLLLDAGINVN 167
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 429-477 7.59e-04

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


Pssm-ID: 188890  Cd Length: 63  Bit Score: 39.04  E-value: 7.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 941804980  429 IYQWLCEFQLEQYTSNFIRAGYD-VPTISRMTPEDLTAIGVTKPGHRKKI 477
Cdd:cd09491     8 VSEWLMNLGLQQYEEGLMHNGWDsLEFLSDITEEDLEEAGVTNPAHKRRL 57
SAM_SASH-like cd09493
SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like ...
 495-552 1.01e-03

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: 38.64  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  495 PSDLGEWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGITKLGHQKKLMLAVK 552
Cdd:cd09493     2 PKTVEELLERINLQEHTSTLLLNGYETLEDFKDLKESHLNELNITDPEHRAKLLTAAE 59
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 79-177 1.05e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   79 LKVAQLLLSSNmvsalleGERGNDSLDSPSTTplhlAARNGHKDVIKLLLKAGIDINRA-TKAGTALHEAALYGKTEVVR 157
Cdd:PLN03192  507 LNVGDLLGDNG-------GEHDDPNMASNLLT----VASTGNAALLEELLKAKLDPDIGdSKGRTPLHIAASKGYEDCVL 575

                          90       100
                  ....*....|....*....|
gi 941804980  158 LLLDAGINVNLRNTYNQTAL 177
Cdd:PLN03192  576 VLLKHACNVHIRDANGNTAL 595
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 206-257 1.53e-03

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 37.57  E-value: 1.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 941804980   206 RAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGhihdsQRGTDRVGFFP 257
Cdd:pfam00018    1 VALYDY-TAQEPDELSFKKGDIIIVLEKSEDGWWKG-----RNKGGKEGLIP 46
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 32-64 1.59e-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: 37.27  E-value: 1.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 941804980    32 DGQIPLHLSA-QYGHYEVSEMLLQHQSNPCLMNK 64
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 486-557 1.68e-03

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 38.43  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 941804980  486 IPEWLPDyipsDLGEWLSviGLP----QYQKRLCDNGYDSIAIVkDITWEDLQEIGITKLGHQKKLMLAVKRLCDL 557
Cdd:cd09511     1 VAKWSPK----QVTDWLK--GLDdclqQYIYTFEREKVTGEQLL-NLSPQDLENLGVTKIGHQELILEAVELLCAL 69
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 425-485 1.88e-03

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: 37.96  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941804980  425 DSEAIYQWLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKLN 485
Cdd:cd09534     2 DEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 495-554 2.08e-03

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.


Pssm-ID: 188918  Cd Length: 64  Bit Score: 37.86  E-value: 2.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  495 PSDLGEWLSVIGLPQYQKRLCDNGYDsIAIVKDITWEDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09519     4 PKDLSELLEQIGCSKYLPIFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 62
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 220-263 2.17e-03

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 37.71  E-value: 2.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 941804980  220 LNLRAGDLIMVLEQHSDGRWKGhihdSQRGTdrVGFFPPSVVEV 263
Cdd:cd11823    16 LSLQPGDIIEVHEKQDDGWWLG----ELNGK--KGIFPATYVEE 53
SH3_Stac2_C cd11985
C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); ...
 220-262 2.47e-03

C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac2 contains a single SH3 domain at the C-terminus unlike Stac1 and Stac3, which contain two C-terminal SH3 domains. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212918  Cd Length: 53  Bit Score: 37.23  E-value: 2.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 941804980  220 LNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVE 262
Cdd:cd11985    16 LPLQPGDRVMVVDDSNEDWWKGKSG------DRVGFFPANFVQ 52
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 428-484 2.66e-03

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 37.69  E-value: 2.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 941804980  428 AIYQWLCEFQLEQYTSNFIRAGYDVPTISRMTPEDLTAIGVTKPGHRKKISSEISKL 484
Cdd:cd09524     7 SISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERL 63
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-213 3.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   94 LLEGERGNDSLDSPSTTPLHLAARNGHKDVIKLLLKAGIDINRATKAGTALHEAALYGKT-EVVRLLLDAginvnlRNTY 172
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNiDTIKAIIDN------RSNI 237

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 941804980  173 NQTALDIVNqfttSTASRDIKQLLREASSSLQVRAVKDYWN 213
Cdd:PHA02876  238 NKNDLSLLK----AIRNEDLETSLLLYDAGFSVNSIDDCKN 274
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 116-208 3.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.65  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  116 ARNGHKDVIKLLLKAGIDINRATKAGTALheaALYGK-----TEVVRLLLDAGINVNLRNtYNQTALDIV--NQFTTSTA 188
Cdd:PHA02989   11 SDTVDKNALEFLLRTGFDVNEEYRGNSIL---LLYLKrkdvkIKIVKLLIDNGADVNYKG-YIETPLCAVlrNREITSNK 86

                          90       100
                  ....*....|....*....|
gi 941804980  189 SRDIKQLLREASSSLQVRAV 208
Cdd:PHA02989   87 IKKIVKLLLKFGADINLKTF 106
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 430-476 3.70e-03

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: 37.28  E-value: 3.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 941804980  430 YQWLCEFQLEQYTSNFIRAGYDVP-TISRMTPEDLTAIGVTKPGHRKK 476
Cdd:cd09541     4 YEWLEEAGLQHYYPAFAAGGVTSIeALAQLTMQDYASLGVQDMEDKQK 51
SAM_tumor-p63,p73 cd09503
SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 ...
 500-539 4.27e-03

SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188902  Cd Length: 65  Bit Score: 36.91  E-value: 4.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 941804980  500 EWLSVIGLPQYQKRLCDNGYDSIAIVKDITWEDLQEIGIT 539
Cdd:cd09503     9 SWLTKLGCSNYIDNFHQQGLLSIFQLDEFTLEDLAAMKIP 48
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 101-168 4.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 4.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  101 NDSLDSpSTTPLHLAARNGHKDVIKLLLKAGIDINRA-TKAGTALHEAALYGKTEVVRLLLDAGINVNL 168
Cdd:PHA02874   29 NISVDE-TTTPLIDAIRSGDAKIVELFIKHGADINHInTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 204-262 4.30e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 36.73  E-value: 4.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  204 QVRAVKDYWNLhDPTALNLRAGDLIMVLEQHSDGRWKGHIHdsqrgtDRVGFFPPSVVE 262
Cdd:cd11950     1 QVRALYDFEAL-EDDELGFNSGDVIEVLDSSNPSWWKGRLH------GKLGLFPANYVA 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 113-210 4.38e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980  113 HLAArNGHKDVIKLLLKAGIDIN-RATKAGTALHEAALYGKTEVVRLLLDAGINVNLRNTYNQTALDIVNQfttsTASRD 191
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNcRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE----NGFRE 162

                          90       100
                  ....*....|....*....|..
gi 941804980  192 IKQLL---REASSSLQVRAVKD 210
Cdd:PTZ00322  163 VVQLLsrhSQCHFELGANAKPD 184
SH3_MLK1-3 cd12059
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ...
 207-261 4.39e-03

Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212992 [Multi-domain]  Cd Length: 58  Bit Score: 36.67  E-value: 4.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941804980  207 AVKDYwnlhDPTA---LNLRAGDLIMVLEQHS-----DGRWKGHIHdsqrgtDRVGFFPPSVV 261
Cdd:cd12059     4 AVFDY----EASAedeLTLRRGDRVEVLSKDSavsgdEGWWTGKIN------DRVGIFPSNYV 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 19-196 4.64e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   19 LLRGAASVNAPSHDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLMNKAKKTPLDLACEFGRLKVAQLLLssnmvsALLEGE 98
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINL------LVQYGA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941804980   99 RGNDSLDSPSTTPLhLAARNGHKDVIKLLLKAGID---INRATKAGTALHEAALYGKTEVVRLLLDAGINVNLRNTYNQT 175
Cdd:PHA02946  132 KINNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNT 210

                         170       180
                  ....*....|....*....|.
gi 941804980  176 ALDIVNQFTTSTAsrDIKQLL 196
Cdd:PHA02946  211 PLHIVCSKTVKNV--DIINLL 229
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 526-554 4.65e-03

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 36.88  E-value: 4.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 941804980  526 KDITW--------EDLQEIGITKLGHQKKLMLAVKRL 554
Cdd:cd09521    27 HDVTFsqllkmteEDLEKIGITQPGDQKKILDAIKEV 63
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
 204-261 6.15e-03

Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212754 [Multi-domain]  Cd Length: 54  Bit Score: 36.29  E-value: 6.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 941804980  204 QVRAVKDYWNLHDpTALNLRAGDLIMVLEQHSDGRWKGhihDSQRGTdrvGFFPPSVV 261
Cdd:cd11820     2 KVRALYDFEAAED-NELTFKAGEIITVLDDSDPNWWKG---SNHRGE---GLFPANFV 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 32-59 6.62e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 6.62e-03
                            10        20
                    ....*....|....*....|....*...
gi 941804980     32 DGQIPLHLSAQYGHYEVSEMLLQHQSNP 59
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 204-262 8.86e-03

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 35.85  E-value: 8.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 941804980  204 QVRAVKDYwNLHDPTALNLRAGDLIMVLEQHSDGRWKGHIHDSQrgtdrvGFFPPSVVE 262
Cdd:cd11827     1 QCKALYAY-DAQDTDELSFNEGDIIEILKEDPSGWWTGRLRGKE------GLFPGNYVE 52
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH