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Conserved domains on  [gi|1720364136|ref|XP_030101415|]
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caskin-2 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 152-213 1.97e-42

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: 148.58  E-value: 1.97e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  152 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESQRGTDRVGYFPPGIVEVV 213
Cdd:cd12063      1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 421-491 1.88e-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: 140.12  E-value: 1.88e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  421 WLPNYIPVDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLAELRR 491
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 ...
 355-420 3.84e-36

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: 130.84  E-value: 3.84e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  355 GKDAQAIHNWLSEFQLEGYTAHFLQAGYDVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSIAE 420
Cdd:cd09497      1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-170 8.38e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 8.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:COG0666    105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   81 IEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVNQfttsQASREIKQLLREASGILKVRALKD 159
Cdd:COG0666    177 ADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE----NGNLEIVKLLLEAGADLNAKDKDG 252

                          170
                   ....*....|.
gi 1720364136  160 FWNLHDPTALN 170
Cdd:COG0666    253 LTALLLAAAAG 263
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1012-1069 8.29e-24

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: 95.22  E-value: 8.29e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136 1012 QQRLEQTSSSLEAALRAAEKSIGTEERDGP---TGTSTKHILDDISTMFDALADQLDAMLD 1069
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESQSSgsaEVKSAGNILDDIGNMFDDLADQLDAMLD 61
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 665-749 7.72e-19

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: 82.16  E-value: 7.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  665 SHSLSRPGPAEGEAEGEAEGPVGS-ALGSYATLTRRPGRSTLARTSPSltPTRGTPRSQSFALRARRKGPPPPPPKRLSS 743
Cdd:pfam16907    5 SQSLNRYALSDGEPEEEEEPPLGSgTLGSYATLTRRPGRSQLARLQPS--PEKNVNRSQSFAVRARKKGPPPPPPKRLSS 82


                   ....*.
gi 1720364136  744 VSGSTE 749
Cdd:pfam16907   83 VSSSTS 88
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 529-975 1.02e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  529 PRLLTF-QGSElspELQAAMAGGGSEPLP-----------LPPAR---SPSQESIGARSRGSGHSQEQPVPQPSVGDPSA 593
Cdd:PHA03247  2531 PRMLTWiRGLE---ELASDDAGDPPPPLPpaappaapdrsVPPPRpapRPSEPAVTSRARRPDAPPQSARPRAPVDDRGD 2607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  594 PQeRNLPEGTERPSKLCSPLPGQGPAPYVFMCPQNLPSSPAPGPPPGVPRAfsylagspaapPDPPRPKRRSHSLSRPGP 673
Cdd:PHA03247  2608 PR-GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA-----------PGRVSRPRRARRLGRAAQ 2675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  674 AEGEAEGEAEGPVGSALGSYATLTRRPgrstlartSPSLTPtRGTPRSQSFALRARrkgppppppkrLSSVSGSTEPPSL 753
Cdd:PHA03247  2676 ASSPPQRPRRRAARPTVGSLTSLADPP--------PPPPTP-EPAPHALVSATPLP-----------PGPAAARQASPAL 2735

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  754 DGTSGPKEGATGPrrrtlSEPTGPSESPGPSAPTGPVSDTEEEpGPEGTPPSRGSSGEGLPFAEEGNlTIKQRPKPAGPP 833
Cdd:PHA03247  2736 PAAPAPPAVPAGP-----ATPGGPARPARPPTTAGPPAPAPPA-APAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPP 2808

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  834 PRETPVPPGLDFNLTESD------TVKRRPKCKEREPLQTALLAFGVVGSDTPGPSNPlSTQAPCDPPSASSNPPQRSEP 907
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGplppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRP-PSRSPAAKPAAPARPPVRRLA 2887

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  908 SVLPSQGTSASSLSSVTQSPGHPGPSAGPALANSTGSKPNVET----EPPAPPAALLKVPGAGTAPKPVSVA 975
Cdd:PHA03247  2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQppppPPPRPQPPLAPTTDPAGAGEPSGAV 2959
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 266-299 7.32e-06

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: 44.27  E-value: 7.32e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720364136  266 AGDRNSVGSEGSVGSIRSAGSGQSSEGTNGHGTG 299
Cdd:pfam16600   12 GGDRSSVGSTGSVGSVRSSGSGQSSHALHAGSEG 45
 
Name Accession Description Interval E-value
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 152-213 1.97e-42

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: 148.58  E-value: 1.97e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  152 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESQRGTDRVGYFPPGIVEVV 213
Cdd:cd12063      1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 421-491 1.88e-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: 140.12  E-value: 1.88e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  421 WLPNYIPVDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLAELRR 491
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 ...
 355-420 3.84e-36

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: 130.84  E-value: 3.84e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  355 GKDAQAIHNWLSEFQLEGYTAHFLQAGYDVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSIAE 420
Cdd:cd09497      1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-170 8.38e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 8.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:COG0666    105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   81 IEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVNQfttsQASREIKQLLREASGILKVRALKD 159
Cdd:COG0666    177 ADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE----NGNLEIVKLLLEAGADLNAKDKDG 252

                          170
                   ....*....|.
gi 1720364136  160 FWNLHDPTALN 170
Cdd:COG0666    253 LTALLLAAAAG 263
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1012-1069 8.29e-24

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: 95.22  E-value: 8.29e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136 1012 QQRLEQTSSSLEAALRAAEKSIGTEERDGP---TGTSTKHILDDISTMFDALADQLDAMLD 1069
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESQSSgsaEVKSAGNILDDIGNMFDDLADQLDAMLD 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-119 5.22e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 5.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   20 LDLACEFGRLKVAQLLLNshlcvallEGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKaGIEINRQTKTGTALHEAALY 99
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE--------NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARS 71

                           90       100
                   ....*....|....*....|
gi 1720364136  100 GKTEVVRLLLEGGVDVNIRN 119
Cdd:pfam12796   72 GHLEIVKLLLEKGADINVKD 91
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 665-749 7.72e-19

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: 82.16  E-value: 7.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  665 SHSLSRPGPAEGEAEGEAEGPVGS-ALGSYATLTRRPGRSTLARTSPSltPTRGTPRSQSFALRARRKGPPPPPPKRLSS 743
Cdd:pfam16907    5 SQSLNRYALSDGEPEEEEEPPLGSgTLGSYATLTRRPGRSQLARLQPS--PEKNVNRSQSFAVRARKKGPPPPPPKRLSS 82


                   ....*.
gi 1720364136  744 VSGSTE 749
Cdd:pfam16907   83 VSSSTS 88
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 429-486 4.45e-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: 73.46  E-value: 4.45e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  429 DLLEWLCALGLPQYHKQLvSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:pfam00536    7 DVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 354-416 4.07e-14

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: 68.06  E-value: 4.07e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  354 EGKDAQAIHNWLSEFQLEGYTAHFlQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYiDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 429-488 3.33e-12

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: 62.70  E-value: 3.33e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   429 DLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLAE 488
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 361-416 1.48e-10

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: 58.08  E-value: 1.48e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136   361 IHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:smart00454    9 VADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 529-975 1.02e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  529 PRLLTF-QGSElspELQAAMAGGGSEPLP-----------LPPAR---SPSQESIGARSRGSGHSQEQPVPQPSVGDPSA 593
Cdd:PHA03247  2531 PRMLTWiRGLE---ELASDDAGDPPPPLPpaappaapdrsVPPPRpapRPSEPAVTSRARRPDAPPQSARPRAPVDDRGD 2607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  594 PQeRNLPEGTERPSKLCSPLPGQGPAPYVFMCPQNLPSSPAPGPPPGVPRAfsylagspaapPDPPRPKRRSHSLSRPGP 673
Cdd:PHA03247  2608 PR-GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA-----------PGRVSRPRRARRLGRAAQ 2675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  674 AEGEAEGEAEGPVGSALGSYATLTRRPgrstlartSPSLTPtRGTPRSQSFALRARrkgppppppkrLSSVSGSTEPPSL 753
Cdd:PHA03247  2676 ASSPPQRPRRRAARPTVGSLTSLADPP--------PPPPTP-EPAPHALVSATPLP-----------PGPAAARQASPAL 2735

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  754 DGTSGPKEGATGPrrrtlSEPTGPSESPGPSAPTGPVSDTEEEpGPEGTPPSRGSSGEGLPFAEEGNlTIKQRPKPAGPP 833
Cdd:PHA03247  2736 PAAPAPPAVPAGP-----ATPGGPARPARPPTTAGPPAPAPPA-APAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPP 2808

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  834 PRETPVPPGLDFNLTESD------TVKRRPKCKEREPLQTALLAFGVVGSDTPGPSNPlSTQAPCDPPSASSNPPQRSEP 907
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGplppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRP-PSRSPAAKPAAPARPPVRRLA 2887

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  908 SVLPSQGTSASSLSSVTQSPGHPGPSAGPALANSTGSKPNVET----EPPAPPAALLKVPGAGTAPKPVSVA 975
Cdd:PHA03247  2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQppppPPPRPQPPLAPTTDPAGAGEPSGAV 2959
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 153-211 1.21e-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: 52.16  E-value: 1.21e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136   153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGhihesQRGTDRVGYFPPGIVE 211
Cdd:smart00326    4 QVRALYDY-TAQDPDELSFKKGDIITVLEKSDDGWWKG-----RLGRGKEGLFPSNYVE 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-147 2.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNSHLCVALlegeaKDPCDpnyTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:PHA02875   120 LLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI-----EDCCG---CTPLIIAMAKGDIAICKMLLDSG 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136   81 IEINRQTKTG--TALHEAALYGKTEVVRLLLEGGVDVNIRNTY---NQTALDIVNQFTTSQASREIKQLLRE 147
Cdd:PHA02875   192 ANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADCNIMFMIegeECTILDMICNMCTNLESEAIDALIAD 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-128 2.44e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLL-------NSHLCVALLEGEakdpcdpnytTPLHLAAKNGHREVI 73
Cdd:cd22192     36 LLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaapelvNEPMTSDLYQGE----------TALHIAVVNQNLNLV 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   74 RQLLKAGIEINRQTKTGTA---------------LHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDI 128
Cdd:cd22192    106 RELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 153-213 4.13e-06

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: 44.89  E-value: 4.13e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHEsqrgtdRVGYFPPGIVEVV 213
Cdd:pfam07653    1 YGRVIFDY-VGTDKNGLTLKKGDVVKVLGKDNDGWWEGETGG------RVGLVPSTAVEEI 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-84 6.38e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 6.38e-06
                            10        20
                    ....*....|....*....|....*.
gi 1720364136    59 TPLHLAAKNGHREVIRQLLKAGIEIN 84
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADIN 29
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 266-299 7.32e-06

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: 44.27  E-value: 7.32e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720364136  266 AGDRNSVGSEGSVGSIRSAGSGQSSEGTNGHGTG 299
Cdd:pfam16600   12 GGDRSSVGSTGSVGSVRSSGSGQSSHALHAGSEG 45
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 687-966 6.87e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  687 GSALGSYATLTRRPGRSTLARTSPSLTPTRGTPRSQSFAlrarrkGPPPPPPKRLSSVSGSTeppSLDGTSGPKEGATGP 766
Cdd:pfam17823  105 GAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFS------APRAAACRANASAAPRA---AIAAASAPHAASPAP 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  767 RRRTLSEPTGPSESPGPSAPTGPVSDTEEEPGPeGTPPSRGSSGEGLP-----FAEEGNLTIKQRPKPAGPPPRETPVPP 841
Cdd:pfam17823  176 RTAASSTTAASSTTAASSAPTTAASSAPATLTP-ARGISTAATATGHPaagtaLAAVGNSSPAAGTVTAAVGTVTPAALA 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  842 GLD----------FNLTESDTVKRRPKCKEREPLQT-ALLAFGVVGSDTPGPSNPLSTQAPCDPPSASSNPPQRS---EP 907
Cdd:pfam17823  255 TLAaaagtvasaaGTINMGDPHARRLSPAKHMPSDTmARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNttlEP 334

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  908 SVLPSQGTSASSLSSVTQSPGHPgPSAGPALANSTGSKPNVE-TEPPAPPAALLKVPGAG 966
Cdd:pfam17823  335 NTPKSVASTNLAVVTTTKAQAKE-PSASPVPVLHTSMIPEVEaTSPTTQPSPLLPTQGAA 393
PHA03309 PHA03309
transcriptional regulator ICP4; Provisional
 688-806 7.84e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 165564 [Multi-domain]  Cd Length: 2033  Bit Score: 43.69  E-value: 7.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  688 SALGSYATLTRRPGRSTLARTSPSLTPTRGTPRSQSFALRARRKGPPPPPPKRLSSVSGSTEPPSLDGTS---GPKEGAT 764
Cdd:PHA03309  1823 SSSSSSSSPSSRPSRSATPSLSPSPSPPRRAPVDRSRSGRRRERDRPSANPFRWAPRQRSRADHSPDGTApgdAPLNLED 1902

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720364136  765 GP-RRRTLSEPTGPSESPGPSAPTGPVSDTEEEpgpEGTPPSR 806
Cdd:PHA03309  1903 GPgRGRPIWTPSSATTLPSRSGPEDSVDETETE---DSAPPAR 1942
 
Name Accession Description Interval E-value
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 152-213 1.97e-42

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: 148.58  E-value: 1.97e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  152 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESQRGTDRVGYFPPGIVEVV 213
Cdd:cd12063      1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 421-491 1.88e-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: 140.12  E-value: 1.88e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  421 WLPNYIPVDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLAELRR 491
Cdd:cd09498      1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
SH3_Caskin cd11880
Src Homology 3 domain of CASK interacting protein; Caskin proteins are multidomain adaptor ...
 152-212 4.15e-39

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: 138.84  E-value: 4.15e-39
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  152 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESQRGTDRVGYFPPGIVEV 212
Cdd:cd11880      1 LQVRATKDYWNNHDLTALNVRAGDIITVLEQHPDGRWKGHIHDNQTGNDRVGYFPPSLVEV 61
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 355-420 3.84e-36

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: 130.84  E-value: 3.84e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  355 GKDAQAIHNWLSEFQLEGYTAHFLQAGYDVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSIAE 420
Cdd:cd09497      1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-170 8.38e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 8.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:COG0666    105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   81 IEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVNQfttsQASREIKQLLREASGILKVRALKD 159
Cdd:COG0666    177 ADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE----NGNLEIVKLLLEAGADLNAKDKDG 252

                          170
                   ....*....|.
gi 1720364136  160 FWNLHDPTALN 170
Cdd:COG0666    253 LTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-183 8.03e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 8.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:COG0666     72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--------GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   81 IEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVnqftTSQASREIKQLLREASGILKVRALKD 159
Cdd:COG0666    144 ADVNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA----AENGHLEIVKLLLEAGADVNAKDNDG 219

                          170       180
                   ....*....|....*....|....
gi 1720364136  160 FWNLHDptALNVRAGDVITVLEQH 183
Cdd:COG0666    220 KTALDL--AAENGNLEIVKLLLEA 241
SH3_Caskin1 cd12062
Src Homology 3 domain of CASK interacting protein 1; Caskin1 is a multidomain adaptor protein ...
 152-213 1.54e-25

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: 100.46  E-value: 1.54e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  152 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESQRGTDRVGYFPPGIVEVV 213
Cdd:cd12062      1 LQVRALKDYCNNYDLTSLNIKAGDVITVLEQHPDGRWKGCIHDNRTGNDRVGYFPSSLVEAI 62
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1012-1069 8.29e-24

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: 95.22  E-value: 8.29e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136 1012 QQRLEQTSSSLEAALRAAEKSIGTEERDGP---TGTSTKHILDDISTMFDALADQLDAMLD 1069
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESQSSgsaEVKSAGNILDDIGNMFDDLADQLDAMLD 61
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-159 8.65e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 8.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:COG0666    138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA--------GADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   81 IEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVNQFTTSQASREIKQLLREASGILKVRALKD 159
Cdd:COG0666    210 ADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-119 5.22e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 5.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   20 LDLACEFGRLKVAQLLLNshlcvallEGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKaGIEINRQTKTGTALHEAALY 99
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE--------NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARS 71

                           90       100
                   ....*....|....*....|
gi 1720364136  100 GKTEVVRLLLEGGVDVNIRN 119
Cdd:pfam12796   72 GHLEIVKLLLEKGADINVKD 91
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 665-749 7.72e-19

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: 82.16  E-value: 7.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  665 SHSLSRPGPAEGEAEGEAEGPVGS-ALGSYATLTRRPGRSTLARTSPSltPTRGTPRSQSFALRARRKGPPPPPPKRLSS 743
Cdd:pfam16907    5 SQSLNRYALSDGEPEEEEEPPLGSgTLGSYATLTRRPGRSQLARLQPS--PEKNVNRSQSFAVRARKKGPPPPPPKRLSS 82


                   ....*.
gi 1720364136  744 VSGSTE 749
Cdd:pfam16907   83 VSSSTS 88
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 429-486 4.45e-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: 73.46  E-value: 4.45e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  429 DLLEWLCALGLPQYHKQLvSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:pfam00536    7 DVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 354-416 4.07e-14

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: 68.06  E-value: 4.07e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  354 EGKDAQAIHNWLSEFQLEGYTAHFlQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYiDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2-86 6.92e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 6.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    2 LLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNsHLCVAllegeakdpCDPNYTTPLHLAAKNGHREVIRQLLKAGI 81
Cdd:pfam12796   16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN---------LKDNGRTALHYAARSGHLEIVKLLLEKGA 85


                   ....*
gi 1720364136   82 EINRQ 86
Cdd:pfam12796   86 DINVK 90
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 429-485 2.86e-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: 62.26  E-value: 2.86e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136  429 DLLEWLCALGLPQYHKQLVSSgYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKR 485
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKN-EIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-148 3.28e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 3.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   13 NKLKKTPLDLACEFGRLKVAQLLLNSHLCVALLEGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAGIEINRQTKTG-T 91
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGnT 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136   92 ALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVnqftTSQASREIKQLLREA 148
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA----AYNGNLEIVKLLLEA 142
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 429-488 3.33e-12

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: 62.70  E-value: 3.33e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   429 DLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLAE 488
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 432-486 5.79e-12

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: 61.48  E-value: 5.79e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09488      7 EWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 364-413 6.83e-12

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: 61.48  E-value: 6.83e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  364 WLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEI 413
Cdd:cd09488      8 WLESIKMGRYKENFTAAGYtSLDAVAQMTAEDLTRLGVTLVGHQKKILNSI 58
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
429-486 8.92e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 58.43  E-value: 8.92e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  429 DLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 361-416 1.48e-10

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: 58.08  E-value: 1.48e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136   361 IHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:smart00454    9 VADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
354-416 1.86e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 57.66  E-value: 1.86e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  354 EGKDAQAIHNWLSEFQLEGYTAHFLQAGYDVPT-ISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:pfam07647    2 ESWSLESVADWLRSIGLEQYTDNFRDQGITGAElLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 363-413 2.35e-10

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: 56.86  E-value: 2.35e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  363 NWLSEFQLEGYTAHFLQAGYDVPTISRMTPEDLTAIGVTKPGHRKKIASEI 413
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-109 1.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.14e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720364136   57 YTTPLHLAAKNGHREVIRQLLKAGIEINRQTKTG-TALHEAALYGKTEVVRLLL 109
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 354-416 2.37e-09

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


Pssm-ID: 188942  Cd Length: 70  Bit Score: 54.46  E-value: 2.37e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  354 EGKDAQAIHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09543      1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNsIDKVLQMTQEDIKHIGVRLPGHQKRIAYSILGL 64
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 153-206 3.88e-09

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: 53.24  E-value: 3.88e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESqrgtdRVGYFP 206
Cdd:cd00174      1 YARALYDY-EAQDDDELSFKKGDIITVLEKDDDGWWEGELNGG-----REGLFP 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
76-129 6.64e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 6.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136   76 LLKAG-IEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIV 129
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 7.54e-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: 53.12  E-value: 7.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09551     11 DWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSM 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 529-975 1.02e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  529 PRLLTF-QGSElspELQAAMAGGGSEPLP-----------LPPAR---SPSQESIGARSRGSGHSQEQPVPQPSVGDPSA 593
Cdd:PHA03247  2531 PRMLTWiRGLE---ELASDDAGDPPPPLPpaappaapdrsVPPPRpapRPSEPAVTSRARRPDAPPQSARPRAPVDDRGD 2607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  594 PQeRNLPEGTERPSKLCSPLPGQGPAPYVFMCPQNLPSSPAPGPPPGVPRAfsylagspaapPDPPRPKRRSHSLSRPGP 673
Cdd:PHA03247  2608 PR-GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA-----------PGRVSRPRRARRLGRAAQ 2675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  674 AEGEAEGEAEGPVGSALGSYATLTRRPgrstlartSPSLTPtRGTPRSQSFALRARrkgppppppkrLSSVSGSTEPPSL 753
Cdd:PHA03247  2676 ASSPPQRPRRRAARPTVGSLTSLADPP--------PPPPTP-EPAPHALVSATPLP-----------PGPAAARQASPAL 2735

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  754 DGTSGPKEGATGPrrrtlSEPTGPSESPGPSAPTGPVSDTEEEpGPEGTPPSRGSSGEGLPFAEEGNlTIKQRPKPAGPP 833
Cdd:PHA03247  2736 PAAPAPPAVPAGP-----ATPGGPARPARPPTTAGPPAPAPPA-APAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPP 2808

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  834 PRETPVPPGLDFNLTESD------TVKRRPKCKEREPLQTALLAFGVVGSDTPGPSNPlSTQAPCDPPSASSNPPQRSEP 907
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGplppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRP-PSRSPAAKPAAPARPPVRRLA 2887

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  908 SVLPSQGTSASSLSSVTQSPGHPGPSAGPALANSTGSKPNVET----EPPAPPAALLKVPGAGTAPKPVSVA 975
Cdd:PHA03247  2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQppppPPPRPQPPLAPTTDPAGAGEPSGAV 2959
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 154-207 1.06e-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: 52.28  E-value: 1.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  154 VRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHESQRGTDRvGYFPP 207
Cdd:cd11883      2 VVALYDF-TPKSKNQLSFKAGDIIYVLNKDPSGWWDGVIISSSGKVKR-GWFPS 53
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 1.17e-08

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: 52.63  E-value: 1.17e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09546      8 EWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEM 62
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 153-211 1.21e-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: 52.16  E-value: 1.21e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136   153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGhihesQRGTDRVGYFPPGIVE 211
Cdd:smart00326    4 QVRALYDY-TAQDPDELSFKKGDIITVLEKSDDGWWKG-----RLGRGKEGLFPSNYVE 56
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 427-484 1.53e-08

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: 52.14  E-value: 1.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  427 PVDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVK 484
Cdd:cd09491      5 PKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQ 62
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-147 2.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNSHLCVALlegeaKDPCDpnyTTPLHLAAKNGHREVIRQLLKAG 80
Cdd:PHA02875   120 LLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI-----EDCCG---CTPLIIAMAKGDIAICKMLLDSG 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136   81 IEINRQTKTG--TALHEAALYGKTEVVRLLLEGGVDVNIRNTY---NQTALDIVNQFTTSQASREIKQLLRE 147
Cdd:PHA02875   192 ANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADCNIMFMIegeECTILDMICNMCTNLESEAIDALIAD 263
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 430-486 2.54e-08

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: 51.49  E-value: 2.54e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136  430 LLEWLCALGLPQYHKQLVSSGYDsMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09497      7 IFDWLREFGLEEYTPNFIKAGYD-LPTISRMTPEDLTAIGITKPGHRKKLKSEIAQL 62
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 3.06e-08

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: 51.57  E-value: 3.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09553     11 DWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDM 65
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 360-416 3.14e-08

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


Pssm-ID: 188926  Cd Length: 63  Bit Score: 51.29  E-value: 3.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  360 AIHNWLSEFQLEGYTAHFLQAGYDVPTISR-MTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09527      4 IVYDWLRTLQLEQYAEKFVDNGYDDLEVCKqIGDPDLDAIGVMNPAHRKRILEAVRRL 61
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 364-420 3.60e-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: 3.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  364 WLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSIAE 420
Cdd:cd09554      9 WLRAIKMERYEDSFLQAGFtTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMGIQN 66
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 359-418 4.31e-08

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: 51.09  E-value: 4.31e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  359 QAIHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSI 418
Cdd:cd09546      4 RSVGEWLEAIKMGRYTEIFMENGYSsMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMRV 64
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 360-418 4.89e-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: 50.81  E-value: 4.89e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  360 AIHNWLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSI 418
Cdd:cd09551      8 SVEDWLSAIKMSQYRDNFLSSGFtSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMRV 67
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 432-488 6.54e-08

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


Pssm-ID: 188926  Cd Length: 63  Bit Score: 50.14  E-value: 6.54e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLAE 488
Cdd:cd09527      7 DWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDLDAIGVMNPAHRKRILEAVRRLKE 63
PHA03095 PHA03095
ankyrin-like protein; Provisional
 6-128 7.69e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 7.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    6 QSNPCL--VNKLKKTPLDLAC--EFGRLKVAQLLLNSHLCV-----ALLEGEA----KDPCDpnyTTPLHLAAKNGHRE- 71
Cdd:PHA03095    22 ASNVTVeeVRRLLAAGADVNFrgEYGKTPLHLYLHYSSEKVkdivrLLLEAGAdvnaPERCG---FTPLHLYLYNATTLd 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136   72 VIRQLLKAGIEINRQTKTG-TALHeAALYGK---TEVVRLLLEGGVDVNIRNTYNQTALDI 128
Cdd:PHA03095    99 VIKLLIKAGADVNAKDKVGrTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAV 158
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 359-413 1.12e-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: 49.62  E-value: 1.12e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  359 QAIHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEI 413
Cdd:cd09542      5 RSVSEWLESIRMKRYILHFRSAGLDtMECVLELTAEDLTQMGITLPGHQKRILCSI 60
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 362-418 1.59e-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: 49.54  E-value: 1.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  362 HNWLSEFQLEGYTAHFLQAG---YDVptISRMTPEDLTAIGVTKPGHRKKIASEIAQLSI 418
Cdd:cd09555     10 QAWLSAIGLECYQDNFSKFGlctFSD--VAQLSLEDLPALGITLAGHQKKLLHHIQLLQQ 67
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 364-409 3.47e-07

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


Pssm-ID: 188897  Cd Length: 71  Bit Score: 48.45  E-value: 3.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720364136  364 WLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKI 409
Cdd:cd09498     13 WLSLLGLPQYHKVLVENGYDsIDFVTDLTWEDLQDIGITKLGHQKKL 59
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 432-480 1.30e-06

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: 46.53  E-value: 1.30e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLtWE-ELQEI-GVNKLGHQKKLM 480
Cdd:cd09500     10 EWLDSIGLGDYIETFLKHGYTSMERVKRI-WEvELTNVlEINKLGHRKRIL 59
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 1.50e-06

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: 46.46  E-value: 1.50e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09555     11 AWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLL 65
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 361-418 1.87e-06

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


Pssm-ID: 188952  Cd Length: 69  Bit Score: 46.56  E-value: 1.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136  361 IHNWLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSI 418
Cdd:cd09553      9 VGDWLDAIKMGRYKENFVSAGFaSFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRL 67
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 432-484 1.90e-06

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: 46.37  E-value: 1.90e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKL---MLGVK 484
Cdd:cd09543     10 EWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKHIGVRLPGHQKRIaysILGLK 65
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 153-212 1.91e-06

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: 45.70  E-value: 1.91e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHesqrgtDRVGYFPPGIVEV 212
Cdd:cd11805      1 RVQALYDF-NPQEPGELEFRRGDIITVLDSSDPDWWKGELR------GRVGIFPANYVQP 53
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 360-418 2.15e-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: 46.03  E-value: 2.15e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  360 AIHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLSI 418
Cdd:cd09547      5 TVSDWLDSIKMGQYKNNFMAAGFTtLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-480 2.42e-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: 46.15  E-value: 2.42e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLM 480
Cdd:cd09552     11 EWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRVGVTLAGHQKKIL 59
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-128 2.44e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLL-------NSHLCVALLEGEakdpcdpnytTPLHLAAKNGHREVI 73
Cdd:cd22192     36 LLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaapelvNEPMTSDLYQGE----------TALHIAVVNQNLNLV 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   74 RQLLKAGIEINRQTKTGTA---------------LHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDI 128
Cdd:cd22192    106 RELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 364-417 2.59e-06

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: 46.17  E-value: 2.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  364 WLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLS 417
Cdd:cd09548     13 WLEAIKMERYKDNFTAAGYNsLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMR 67
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-484 2.63e-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: 45.77  E-value: 2.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVK 484
Cdd:cd09542      9 EWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 61
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-484 3.22e-06

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: 45.63  E-value: 3.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVK 484
Cdd:cd09550      7 DWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQ 59
Ank_4 pfam13637
Ankyrin repeats (many copies);
18-77 3.73e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.73e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   18 TPLDLACEFGRLKVAQLLLNSHLCVallegeakDPCDPNYTTPLHLAAKNGHREVIRQLL 77
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADI--------NAVDGNGETALHFAASNGNVEVLKLLL 54
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 153-213 4.13e-06

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: 44.89  E-value: 4.13e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHEsqrgtdRVGYFPPGIVEVV 213
Cdd:pfam07653    1 YGRVIFDY-VGTDKNGLTLKKGDVVKVLGKDNDGWWEGETGG------RVGLVPSTAVEEI 54
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-480 4.44e-06

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: 45.40  E-value: 4.44e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLM 480
Cdd:cd09548     12 EWLEAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIM 60
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 360-416 4.66e-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: 45.33  E-value: 4.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  360 AIHNWLSEFQLEGYTAHFLQAGYDVP-TISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09545      5 SVDDWLQAIKMERYKDNFTAAGYTTLeAVVHMNQDDLARIGISAIAHQNKILSSVQGM 62
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 5.76e-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: 44.86  E-value: 5.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09554      8 EWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAM 62
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-84 6.38e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 6.38e-06
                            10        20
                    ....*....|....*....|....*.
gi 1720364136    59 TPLHLAAKNGHREVIRQLLKAGIEIN 84
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADIN 29
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 432-486 6.82e-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: 44.60  E-value: 6.82e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSM-----GLVADltwEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09499      7 QWLESIGLPQYESKLLLNGFDDVdflgsGVMED---QDLKEIGITDEQHRQIILQAARSL 63
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-119 6.98e-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: 43.82  E-value: 6.98e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720364136   91 TALHEAAL-YGKTEVVRLLLEGGVDVNIRN 119
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 266-299 7.32e-06

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: 44.27  E-value: 7.32e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720364136  266 AGDRNSVGSEGSVGSIRSAGSGQSSEGTNGHGTG 299
Cdd:pfam16600   12 GGDRSSVGSTGSVGSVRSSGSGQSSHALHAGSEG 45
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 429-475 8.14e-06

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: 44.23  E-value: 8.14e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720364136  429 DLLEWLCALGLPQYHKQLVSSGYDSMGLVAdLTWEELQEIGVNKLGH 475
Cdd:cd09533      1 DVADWLSSLGLPQYEDQFIENGITGDVLVA-LDHEDLKEMGITSVGH 46
SH3_CRK_C cd11759
C-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
 162-212 8.16e-06

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: 44.01  E-value: 8.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  162 NLHDPTALNVRAGDVITVLEQHPDGRWKGHIHesqrgtDRVGYFPPGIVEV 212
Cdd:cd11759     13 NAYDKTALALEVGDLVKVTKINVSGQWEGELN------GKVGHFPFTHVEL 57
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-129 9.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.85e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1720364136   91 TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIV 129
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 428-486 1.33e-05

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


Pssm-ID: 188946  Cd Length: 64  Bit Score: 43.72  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136  428 VDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09547      4 VTVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTL 62
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-179 1.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   18 TPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAK------------NG-----------HREVIR 74
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKH--------GADINHINTKIPHPLLTAIKigahdiikllidNGvdtsilpipciEKDMIK 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   75 QLLKAGIEIN-RQTKTGTALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIvnqfTTSQASREIKQLLREASGILK 153
Cdd:PHA02874   109 TILDCGIDVNiKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI----AIKHNFFDIIKLLLEKGAYAN 184

                          170       180
                   ....*....|....*....|....*.
gi 1720364136  154 VRAlkdfWNLHDPTALNVRAGDVITV 179
Cdd:PHA02874   185 VKD----NNGESPLHNAAEYGDYACI 206
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 360-416 1.69e-05

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


Pssm-ID: 188949  Cd Length: 65  Bit Score: 43.70  E-value: 1.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  360 AIHNWLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEI----AQL 416
Cdd:cd09550      4 SVDDWLDSIKMGRYKDHFAAGGYsSLGMVMRMNIEDIRRLGITLMGHQKKILTSIqvmrAQL 65
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 358-416 1.82e-05

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: 43.44  E-value: 1.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  358 AQAIHNWLSEFQLEGYTAHFLQAGYD-VPTISR--MTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09499      2 VQSVGQWLESIGLPQYESKLLLNGFDdVDFLGSgvMEDQDLKEIGITDEQHRQIILQAARSL 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-171 2.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   59 TPLHLAAKNGHREVIRQLLKAGIEINRQTKTGTA-LHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVnqfTTSQA 137
Cdd:PHA02878   170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSpLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS---VGYCK 246

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720364136  138 SREIKQLLRE-------ASGILKVRALKDfwNLHDPTALNV 171
Cdd:PHA02878   247 DYDILKLLLEhgvdvnaKSYILGLTALHS--SIKSERKLKL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
93-126 2.16e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 2.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720364136   93 LHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTAL 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 357-417 2.19e-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: 43.08  E-value: 2.19e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  357 DAQAIHNWLSEFQLEGYTAHFLQAGYDVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLS 417
Cdd:cd09506      6 TVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKLL 66
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 153-212 2.38e-05

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: 42.70  E-value: 2.38e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHP-DGRWKGhihESQRGtdRVGYFPPGIVEV 212
Cdd:cd11763      1 KVRALYDF-DSQPSGELSLRAGEVLTITRQDVgDGWLEG---RNSRG--EVGLFPSSYVEI 55
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 361-419 2.41e-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: 43.05  E-value: 2.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  361 IHNWLSEFQLEGYTAHFLQAGYDVPTISR-MTPEDLTAIGVTKPGHRKKIaseIAQLSIA 419
Cdd:cd09490      6 IAEWLASIHLEQYLDLFREHGYVTATDCQgINDSRLKQIGISPTGHRRRI---LKQLPII 62
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 155-206 2.66e-05

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: 42.19  E-value: 2.66e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  155 RALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGhihesQRGTDRVGYFP 206
Cdd:pfam00018    1 VALYDY-TAQEPDELSFKKGDIIIVLEKSEDGWWKG-----RNKGGKEGLIP 46
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-129 2.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNShlcvalleGEAKDPCDPNYTTPLHLAAKN-GHREVIRQLLKA 79
Cdd:PHA02878   186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN--------GASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720364136   80 GIEINRQT--KTGTALHEAAlygKTE-VVRLLLEGGVDVNIRNTYNQTALDIV 129
Cdd:PHA02878   258 GVDVNAKSyiLGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-88 2.95e-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: 41.89  E-value: 2.95e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1720364136   59 TPLHLAA-KNGHREVIRQLLKAGIEINRQTK 88
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 428-486 4.11e-05

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


Pssm-ID: 188944  Cd Length: 71  Bit Score: 42.63  E-value: 4.11e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136  428 VDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09545      4 ASVDDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQGM 62
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 428-487 4.12e-05

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: 42.31  E-value: 4.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  428 VDLLEWLCALGLPQYHkQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRLA 487
Cdd:cd09524      6 FSISQFLSSLGLEHLR-EIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLI 64
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-117 4.86e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 4.86e-05
                           10        20
                   ....*....|....*....|....*..
gi 1720364136   91 TALHEAALYGKTEVVRLLLEGGVDVNI 117
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 432-486 5.19e-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: 42.16  E-value: 5.19e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09549     12 EWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQAL 66
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-84 5.31e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 5.31e-05
                           10        20
                   ....*....|....*....|....*.
gi 1720364136   59 TPLHLAAKNGHREVIRQLLKAGIEIN 84
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 365-417 5.62e-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: 41.90  E-value: 5.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720364136  365 LSEFQLEGYTAHFLQAGYDVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQLS 417
Cdd:cd09520     11 LAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELN 63
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-129 5.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLA--CEFGRLKVAQLLLNSHlcvallegeAK-DPCDPNYTTPLHLAAKNGHR--EVIRQ 75
Cdd:PHA03100    91 LLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNG---------ANvNIKNSDGENLLHLYLESNKIdlKILKL 161

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136   76 LLKAGIEINRQTKTG-----------------TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIV 129
Cdd:PHA03100   162 LIDKGVDINAKNRVNyllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
 153-210 7.21e-05

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: 41.30  E-value: 7.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  153 KVRALKDFWNLHDpTALNVRAGDVITVLEQHPDGRWKGhihESQRGTdrvGYFPPGIV 210
Cdd:cd11820      2 KVRALYDFEAAED-NELTFKAGEIITVLDDSDPNWWKG---SNHRGE---GLFPANFV 52
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 361-413 8.60e-05

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


Pssm-ID: 188951  Cd Length: 71  Bit Score: 41.92  E-value: 8.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  361 IHNWLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEI 413
Cdd:cd09552      9 VDEWLDAIKMGQYKESFANAGFtSFDVVSQMTMEDILRVGVTLAGHQKKILNSI 62
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 13-126 1.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   13 NKLKKTPLDLACEFGRlkvaqlllNSHLCVALLE----GEAKDPCDpnyTTPLHLAAKNGHREVIRQLLKAGIEINRQT- 87
Cdd:PHA02876   338 DRLYITPLHQASTLDR--------NKDIVITLLElganVNARDYCD---KTPIHYAAVRNNVVIINTLLDYGADIEALSq 406

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720364136   88 KTGTALHeAALYGKTEV--VRLLLEGGVDVNIRNTYNQTAL 126
Cdd:PHA02876   407 KIGTALH-FALCGTNPYmsVKTLIDRGANVNSKNKDLSTPL 446
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 61-123 1.15e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 1.15e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364136   61 LHLAAKNGHREVIRQLLKAGIEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQ 123
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGaTALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
SH3_Stac_1 cd11833
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ...
 169-210 1.15e-04

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: 40.95  E-value: 1.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720364136  169 LNVRAGDVITVLEQHPDGRWKGHIHesqrgtDRVGYFPPGIV 210
Cdd:cd11833     16 LEMRPGDKITLLDDSNEDWWKGKIE------DRVGFFPANFV 51
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 747-1048 1.29e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  747 STEPPSLDGTSGPKEGATGPRRRTLSEPTGPSESPGPSAPTGpvSDTEEEPGPEGTPPSRGSSGEGLPFAEEGNLTIKQR 826
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREG--SPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  827 PKPAGPPPRETPVPPGLDFNLTESDTVkrrpkckerEPLQTALLAfGVVGSDTPGPSNPLSTQAP-CDPPSASSNPPQRS 905
Cdd:PHA03307   141 VGSPGPPPAASPPAAGASPAAVASDAA---------SSRQAALPL-SSPEETARAPSSPPAEPPPsTPPAAASPRPPRRS 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  906 EPSVLPSQGTSASSLSSvtQSPGHPGPSAGPALANSTGSKPNVETEPPAPPAALLKVPGAGTAPkpvsvactqlafsgpk 985
Cdd:PHA03307   211 SPISASASSPAPAPGRS--AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA---------------- 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364136  986 lAPRLGPRPVPPPRPENTGPVCPGRAQQRLEQTSSSLEAALRAAEKSIGTEERDGPTGTSTKH 1048
Cdd:PHA03307   273 -SGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE 334
SAM_SASH1_repeat2 cd09492
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ...
 432-480 1.47e-04

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: 40.96  E-value: 1.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720364136  432 EWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLM 480
Cdd:cd09492     12 DWLVSIGLPMYSPPLLEAGFSTLSRVSSLSETCLREAGITEERHIRKLL 60
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
 153-210 1.59e-04

Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. 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. 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: 212896 [Multi-domain]  Cd Length: 57  Bit Score: 40.39  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  153 KVRALKDFWNLHDpTALNVRAGDVITVLEQHPDGRWKGhihESQRGtdrVGYFPPGIV 210
Cdd:cd11963      3 KVRALYDFEAVED-NELTFKHGEIIIVLDDSDANWWKG---ENHRG---VGLFPSNFV 53
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
 153-210 1.73e-04

Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. 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. 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: 212897 [Multi-domain]  Cd Length: 55  Bit Score: 40.32  E-value: 1.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  153 KVRALKDFWNLHDpTALNVRAGDVITVLEQHPDGRWKGHIHESqrgtdrVGYFPPGIV 210
Cdd:cd11964      2 KVRAIYDFEAAED-NELTFKAGDIITILDDSDPNWWKGETPQG------TGLFPSNFV 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-82 1.74e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFGRLKVAQLLLNSHLCVALLEGEAKdpcdpnytTPLHLAAKNGHREVIRQLLKAG 80
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--------TPLELAEENGFREVVQLLSRHS 171


                   ..
gi 1720364136   81 IE 82
Cdd:PTZ00322   172 QC 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-126 2.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   12 VNKLKKTPLDLACEFGRLkvaqlllnSHLCVALLE-GEAKDPCDPNYTTPLHLAAKNGH-REVIRQLLKAGIEINRQTKT 89
Cdd:PHA02876   269 IDDCKNTPLHHASQAPSL--------SRLVPKLLErGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRL 340

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720364136   90 -GTALHEAALYGK-TEVVRLLLEGGVDVNIRNTYNQTAL 126
Cdd:PHA02876   341 yITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPI 379
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 169-211 2.27e-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: 39.94  E-value: 2.27e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1720364136  169 LNVRAGDVITVLEQHPDGRWKGHIHEsqrgtdRVGYFPPGIVE 211
Cdd:cd11766     16 LSLRKGDRVLVLEKSSDGWWRGECNG------QVGWFPSNYVT 52
SH3_9 pfam14604
Variant SH3 domain;
156-211 3.40e-04

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 39.14  E-value: 3.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  156 ALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGhihesQRGTdRVGYFPPGIVE 211
Cdd:pfam14604    1 ALYPY-EPKDDDELSLQRGDVITVIEESEDGWWEG-----INTG-RTGLVPANYVE 49
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 154-206 3.86e-04

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: 39.40  E-value: 3.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720364136  154 VRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIhesqrgTDRVGYFP 206
Cdd:cd11951      2 VQAQYDF-SAEDPSQLSFRRGDIIEVLDCPDPNWWRGRI------SGRVGFFP 47
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-146 4.02e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   16 KKTPLDLACEFG-RLKVAQLLLNSHLCVallegEAKDPCDpnyTTPLH--LAAKNGHREVIRQLLKAGIEINRQTKTG-T 91
Cdd:PHA03095    83 GFTPLHLYLYNAtTLDVIKLLIKAGADV-----NAKDKVG---RTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGmT 154

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136   92 ALHeaALYGKT----EVVRLLLEGGVDVNIRNTYNQTALDIVNQFTTSQAsREIKQLLR 146
Cdd:PHA03095   155 PLA--VLLKSRnanvELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRA-RIVRELIR 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 91-117 4.51e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.51e-04
                            10        20
                    ....*....|....*....|....*..
gi 1720364136    91 TALHEAALYGKTEVVRLLLEGGVDVNI 117
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_SARM1-like_repeat2 cd09502
SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like ...
 356-413 4.52e-04

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


Pssm-ID: 188901  Cd Length: 70  Bit Score: 39.58  E-value: 4.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  356 KDAQAIHNWLSEF--QLEGYTAHFLQAGYDVPTISRMTPEDLTA-IGVTKPGHRKKIASEI 413
Cdd:cd09502      5 CDTTNLHNWLQSLgpEYSQYTYQMLNAGIDRNSLPSLTEDQLLEdCGITNGIHRLRILNAI 65
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 364-416 4.68e-04

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: 39.46  E-value: 4.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720364136  364 WLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09549     13 WLEALDLCRYKDNFAAAGYgSLEAVARMTAQDVLSLGITSLEHQELLLAGIQAL 66
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 361-415 5.07e-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: 39.43  E-value: 5.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  361 IHNWLSEFQLEGYTAHFLQAGYD-VPTISRMTPEDLTAIGVTKPGHRKKIASEIAQ 415
Cdd:cd09491      8 VSEWLMNLGLQQYEEGLMHNGWDsLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQD 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 59-156 5.61e-04

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: 43.85  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   59 TPLHLAAKNGHREVIRQLLK-AGIEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVD-VNIRNTYN----QTALDI--V 129
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGeTALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIavV 98

                           90       100
                   ....*....|....*....|....*..
gi 1720364136  130 NQFTTSqasreIKQLLREASGILKVRA 156
Cdd:cd22192     99 NQNLNL-----VRELIARGADVVSPRA 120
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 687-966 6.87e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  687 GSALGSYATLTRRPGRSTLARTSPSLTPTRGTPRSQSFAlrarrkGPPPPPPKRLSSVSGSTeppSLDGTSGPKEGATGP 766
Cdd:pfam17823  105 GAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFS------APRAAACRANASAAPRA---AIAAASAPHAASPAP 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  767 RRRTLSEPTGPSESPGPSAPTGPVSDTEEEPGPeGTPPSRGSSGEGLP-----FAEEGNLTIKQRPKPAGPPPRETPVPP 841
Cdd:pfam17823  176 RTAASSTTAASSTTAASSAPTTAASSAPATLTP-ARGISTAATATGHPaagtaLAAVGNSSPAAGTVTAAVGTVTPAALA 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  842 GLD----------FNLTESDTVKRRPKCKEREPLQT-ALLAFGVVGSDTPGPSNPLSTQAPCDPPSASSNPPQRS---EP 907
Cdd:pfam17823  255 TLAaaagtvasaaGTINMGDPHARRLSPAKHMPSDTmARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNttlEP 334

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  908 SVLPSQGTSASSLSSVTQSPGHPgPSAGPALANSTGSKPNVE-TEPPAPPAALLKVPGAG 966
Cdd:pfam17823  335 NTPKSVASTNLAVVTTTKAQAKE-PSASPVPVLHTSMIPEVEaTSPTTQPSPLLPTQGAA 393
PHA03309 PHA03309
transcriptional regulator ICP4; Provisional
 688-806 7.84e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 165564 [Multi-domain]  Cd Length: 2033  Bit Score: 43.69  E-value: 7.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  688 SALGSYATLTRRPGRSTLARTSPSLTPTRGTPRSQSFALRARRKGPPPPPPKRLSSVSGSTEPPSLDGTS---GPKEGAT 764
Cdd:PHA03309  1823 SSSSSSSSPSSRPSRSATPSLSPSPSPPRRAPVDRSRSGRRRERDRPSANPFRWAPRQRSRADHSPDGTApgdAPLNLED 1902

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720364136  765 GP-RRRTLSEPTGPSESPGPSAPTGPVSDTEEEpgpEGTPPSR 806
Cdd:PHA03309  1903 GPgRGRPIWTPSSATTLPSRSGPEDSVDETETE---DSAPPAR 1942
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 354-411 8.50e-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: 38.83  E-value: 8.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364136  354 EGKDAQAIHNWLSEFQLEGYTAHFLQAGY-DVPTISRMTPEDLTAI-GVTKPGHRKKI-AS 411
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYtSMERVKRIWEVELTNVlEINKLGHRKRIlAS 61
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 428-485 8.71e-04

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


Pssm-ID: 188889  Cd Length: 63  Bit Score: 38.43  E-value: 8.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  428 VDLLEWLCALGLPQYHKQLVSSGYDSMGLVADLTWEELQEIGVNKLGHQKKLMLGVKR 485
Cdd:cd09490      4 LDIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRLKQIGISPTGHRRRILKQLPI 61
PHA03378 PHA03378
EBNA-3B; Provisional
 541-927 9.03e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  541 PELQAAMAGGGSEPLPLPPARSPSQESIgaRSRGSGHSQEQ-PVPQPSVgDPSAPQERNLPEGTERPSKLCSPLPgqgPA 619
Cdd:PHA03378   558 PVHDQLLPAPGLGPLQIQPLTSPTTSQL--ASSAPSYAQTPwPVPHPSQ-TPEPPTTQSHIPETSAPRQWPMPLR---PI 631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  620 PYVFMCPQNLPsspapgpppgvpraFSYLAGSPAAPPDPPRPKRRSHSLSRPGPAEGEAEGEAEGPvgSALGSYATLTRR 699
Cdd:PHA03378   632 PMRPLRMQPIT--------------FNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANT--MLPIQWAPGTMQ 695

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  700 PGRSTLARTSPSLTPTRGTPRSQSFALRARRKGPPPPPPKRLSSVSGSTEPPS-LDGTSGPKEGATGPRRRTLSEPTGPS 778
Cdd:PHA03378   696 PPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAaAPGRARPPAAAPGRARPPAAAPGAPT 775

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  779 ESPGPSAPTGPVSDTEEEPGPEGTPpsrgssgEGLPFAeegnlTIKQRPKPAGPPPRETPVPPGLdfnltESDTVKR-RP 857
Cdd:PHA03378   776 PQPPPQAPPAPQQRPRGAPTPQPPP-------QAGPTS-----MQLMPRAAPGQQGPTKQILRQL-----LTGGVKRgRP 838

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136  858 KCKerEPLQTALLAFGVVGSDTPGPSNPLSTQAPCDPPSAssnppqrSEPSVLPSQGTS--ASSLSSVTQSP 927
Cdd:PHA03378   839 SLK--KPAALERQAAAGPTPSPGSGTSDKIVQAPVFYPPV-------LQPIQVMRQLGSvrAAAASTVTQAP 901
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 508-808 1.08e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  508 RGPELMAIEGLENGEGPTTAGPRLltfQGSELSPELQAAMAGGGSEPLPLPPARSPSQESIGARSRGSGHSQEQPVPQPS 587
Cdd:PHA03307   147 PPAASPPAAGASPAAVASDAASSR---QAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPA 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  588 VGDPSAPQERNLPEGTERPSKLCSPLPGQGPAPYVFMCPQNLPSSPAPGPPPGVPRAFSYLAGSPAAPPDPPRPKRRSHS 667
Cdd:PHA03307   224 PGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  668 LSRPGPAEGEAEGEAEGPVGSALGSyaTLTRRPGRSTLA-RTSPSLTPTRGTPR-SQSFALRARRKGPPPPPPKRLSSVS 745
Cdd:PHA03307   304 GSGPAPSSPRASSSSSSSRESSSSS--TSSSSESSRGAAvSPGPSPSRSPSPSRpPPPADPSSPRKRPRPSRAPSSPAAS 381

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136  746 GSTEPP----SLDGTSGPKEGATGPRRRTLSEPTGPSESPGPSAPT--GPVSDTEEEPGPEGTPPSRGS 808
Cdd:PHA03307   382 AGRPTRrrarAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYarYPLLTPSGEPWPGSPPPPPGR 450
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 153-211 1.35e-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: 37.78  E-value: 1.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHesqrgtDRVGYFPPGIVE 211
Cdd:cd11827      1 QCKALYAY-DAQDTDELSFNEGDIIEILKEDPSGWWTGRLR------GKEGLFPGNYVE 52
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 154-211 1.39e-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: 37.88  E-value: 1.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136  154 VRALKDFWNLhDPTALNVRAGDVITVLEQHPDGRWKGHIHEsqrgtdRVGYFPPGIVE 211
Cdd:cd11950      2 VRALYDFEAL-EDDELGFNSGDVIEVLDSSNPSWWKGRLHG------KLGLFPANYVA 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 550-973 2.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  550 GGSEPLPLPPARS-----PSQESIGARSRGSGHSQEQPVPQPSVGDPSAPQERnLPEGTERPSKLCSPL-PGQGPAPYVF 623
Cdd:PHA03247  2610 GPAPPSPLPPDTHapdppPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVS-RPRRARRLGRAAQASsPPQRPRRRAA 2688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  624 MCP-QNLPSSPAPGPPPGVPRAFSYLAGSPAAPPDPPRPKRRSHSLSRPGPAEGEAEGEAEGPVGSALGSYATLTRRPGR 702
Cdd:PHA03247  2689 RPTvGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  703 STLARtSPSLTPTRGTPRSQSFALRARRKGPPPPPPKRLSSVSGSTEPPSLDGTSGPKEGATGPrrrTLSEPTGPSESPG 782
Cdd:PHA03247  2769 PAPPA-APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---TSAQPTAPPPPPG 2844

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  783 PSAPT----------------GPVSDTEEEPGPEGTPPSRGSSGEGLPFAEEGNLTIKQRPKPAGPPPRETPVPPGLDFN 846
Cdd:PHA03247  2845 PPPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  847 LTESDTVKRRPKCKEREPLQTALLAFGV-----------VGSDTPG----PSNPLSTQAPCDPPSASSNPPQRSEPsvLP 911
Cdd:PHA03247  2925 PPPQPQPPPPPPPRPQPPLAPTTDPAGAgepsgavpqpwLGALVPGrvavPRFRVPQPAPSREAPASSTPPLTGHS--LS 3002

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  912 SQGTSASSL-----------------------------SSVTQSPGHPGPSAGPALANSTGSKPNVETEPPAPPAALLKV 962
Cdd:PHA03247  3003 RVSSWASSLalheetdpppvslkqtlwppddtedsdadSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARES 3082

                          490
                   ....*....|.
gi 1720364136  963 PGAGTAPKPVS 973
Cdd:PHA03247  3083 PSSQFGPPPLS 3093
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-126 2.10e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 2.10e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364136   54 DPNYTTPLHLAAKNGHREVIRQLLKAGIEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTAL 126
Cdd:PLN03192   522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-145 2.42e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   62 HLAAkNGHREVIRQLLKAGIEIN-RQTKTGTALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDIVNQFTTsqasRE 140
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNcRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF----RE 162


                   ....*
gi 1720364136  141 IKQLL 145
Cdd:PTZ00322   163 VVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 44-109 2.59e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364136   44 LLEGEAKDPC-DPNYTTPLHLAAKNGHREVIRQLLKAGIEINRQTKTG-TALHEAALYGKTEVVRLLL 109
Cdd:PTZ00322   101 LLTGGADPNCrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGkTPLELAEENGFREVVQLLS 168
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 417-486 2.76e-03

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 37.30  E-value: 2.76e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  417 SIAEWLPNyipvDLLEWLCALGLPQYHKQLVSSGYDSMGLvADLTWEELQEIGVNKLGHQKKLMLGVKRL 486
Cdd:cd09506      1 PVHEWTVD----DVGDWLESLNLGEHRERFMDNEIDGSHL-PNLDKEDLTELGVTRVGHRMNIERALKKL 65
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 169-212 2.86e-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: 36.94  E-value: 2.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720364136  169 LNVRAGDVITVLEQHPDGRWKGhiheSQRGTdrVGYFPPGIVEV 212
Cdd:cd11823     16 LSLQPGDIIEVHEKQDDGWWLG----ELNGK--KGIFPATYVEE 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 18-126 3.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   18 TPLDLACEFgRLKVAQLLLNSHlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLLKAGIEINR--QTKTGTALHE 95
Cdd:PHA02875    37 SPIKLAMKF-RDSEAIKLLMKH-------GAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfYKDGMTPLHL 108

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720364136   96 AALYGKTEVVRLLLEGGVDVNIRNTYNQTAL 126
Cdd:PHA02875   109 ATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
PHA03247 PHA03247
large tegument protein UL36; Provisional
 714-960 3.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  714 PTRGTPRSQSFA-LRARRKGPPPPPPKRLSSVSGSTEPPSLDGTSGPKEGATGPRRRTLSEPTGPSESPGPSAPTGPVSD 792
Cdd:PHA03247   247 PLRGDIAAPAPPpVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAEE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  793 TEEEPG------PEGTPPSRGSSG-------EGLPFAEEGNLTIKQRPKPAGPPPretpvppgldfnltesdTVKRRPKC 859
Cdd:PHA03247   327 EDDEDGamevvsPLPRPRQHYPLGfpkrrrpTWTPPSSLEDLSAGRHHPKRASLP-----------------TRKRRSAR 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  860 KEREPLqtallAFGVVGSDTPGPSNPL--STQAPCDPPSASSNPPQRSEPSVLPSQGTSASslSSVTQSPGHPGPSAGPA 937
Cdd:PHA03247   390 HAATPF-----ARGPGGDDQTRPAAPVpaSVPTPAPTPVPASAPPPPATPLPSAEPGSDDG--PAPPPERQPPAPATEPA 462

                          250       260
                   ....*....|....*....|....*...
gi 1720364136  938 LANSTGSKPNV-----ETEPPAPPAALL 960
Cdd:PHA03247   463 PDDPDDATRKAldalrERRPPEPPGADL 490
SH3_Abp1_eu cd11960
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ...
 153-211 3.76e-03

Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. 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: 212893 [Multi-domain]  Cd Length: 54  Bit Score: 36.61  E-value: 3.76e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136  153 KVRALKDFwNLHDPTALNVRAGDVITVLEQHPDGRWKGhihesqRGTD-RVGYFPPGIVE 211
Cdd:cd11960      1 RARALYDY-QAADDTEISFDPGDIITDIEQIDEGWWRG------TGPDgTYGLFPANYVE 53
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 364-416 4.16e-03

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: 36.62  E-value: 4.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364136  364 WLSEFQLEGYTAHFLQ---AGYDVPTISRmtpEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09507     13 WLESLQLGEYRDIFARndiRGSELLHLER---RDLKDLGITKVGHVKRILQAIKDL 65
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-108 4.63e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 4.63e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364136   43 ALLEGEAKDPCDPNYT-----TPLHLAAKNGHREVIRQLLKAGIEIN-RQTKTGTALHEAALYGKTEVVRLL 108
Cdd:PLN03192   539 ALLEELLKAKLDPDIGdskgrTPLHIAASKGYEDCVLVLLKHACNVHiRDANGNTALWNAISAKHHKIFRIL 610
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-160 5.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136    1 MLLQHQSNPCLVNKLKKTPLDLACEFG---RLKVAQLLLNshlcvalleGEAKDPCDPNYTTPLHLAAKNGHREVIRQLL 77
Cdd:PHA03095   207 ELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA---------GISINARNRYGQTPLHYAAVFNNPRACRRLI 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364136   78 KAGIEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVN-IRNTYNQTALDIVnqFTTSQASRE--IKQLLREASGILK 153
Cdd:PHA03095   278 ALGADINAVSSDGnTPLSLMVRNNNGRAVRAALAKNPSAEtVAATLNTASVAGG--DIPSDATRLcvAKVVLRGAFSLLP 355


                   ....*..
gi 1720364136  154 VRALKDF 160
Cdd:PHA03095   356 EPIRAYH 362
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 390-416 6.83e-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: 36.11  E-value: 6.83e-03
                           10        20
                   ....*....|....*....|....*..
gi 1720364136  390 MTPEDLTAIGVTKPGHRKKIASEIAQL 416
Cdd:cd09521     37 MTEEDLEKIGITQPGDQKKILDAIKEV 63
PHA02917 PHA02917
ankyrin-like protein; Provisional
 53-128 8.39e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.98  E-value: 8.39e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364136   53 CDPNYTTPLhLAAKNghreVIRQLLKagiEINRQTKTG-TALHEAALYGKTEVVRLLLEGGVDVNIRNTYNQTALDI 128
Cdd:PHA02917   423 CDMSYACPI-LSTIN----ICLPYLK---DINMIDKRGeTLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAI 491
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
 153-211 9.44e-03

Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. 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: 212810 [Multi-domain]  Cd Length: 53  Bit Score: 35.37  E-value: 9.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364136  153 KVRALKDFWNLHDpTALNVRAGDVITVLEQHPDGRWKGHIHesqrgtDRVGYFPPGIVE 211
Cdd:cd11877      1 LVRAKFNFEGTNE-DELSFDKGDIITVTQVVEGGWWEGTLN------GKTGWFPSNYVK 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.
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