NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1143077087|ref|NP_001335497|]
View 

leucine-rich repeat-containing protein 4B precursor [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 12183462)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-312 1.32e-30

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 125.05  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENgiqvirtDTFKHLRHLEILQLSKNLVRKIEVgAFNGLPSLNTLELFDNRLTTVPTqAFEYLSKLRELWLR 166
Cdd:COG4886    97 NLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 167 NNPIESIPSyafnrvpslrrldlgelkrleyiseaAFEGLVNLRYLNLGMCNLKDIPN-LTALVRLEELELSGNRLDLIr 245
Cdd:COG4886   168 NNQLTDLPE--------------------------ELGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDL- 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 246 PGSFQGLTSLRKLWLMHAQVATIErnAFDDLKSLEELNLSHNNLMSLPHDLftPLHRLERVHLNHNP 312
Cdd:COG4886   221 PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQ 283
I-set pfam07679
Immunoglobulin I-set domain;
364-453 1.09e-15

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSyRVRISVLHD-GTLNFTNVTVQDTGQYTCMVTNS 441
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTvTGTPDPEVSWFK-DGQPLRSSD-RFKVTYEGGtYTLTISNVQPDDSGKYTCVATNS 78

                          90
                  ....*....|..
gi 1143077087 442 AGNTTASATLNV 453
Cdd:pfam07679  79 AGEAEASAELTV 90
LRRNT smart00013
Leucine rich repeat N-terminal domain;
57-90 1.69e-05

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 41.92  E-value: 1.69e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1143077087   57 CPVACSCSnqASRVICTRRDLAEVPASIPVNTRY 90
Cdd:smart00013   2 CPAPCNCS--GTAVDCSGRGLTEVPLDLPPDTTL 33
LRRCT smart00082
Leucine rich repeat C-terminal domain;
311-361 1.72e-05

Leucine rich repeat C-terminal domain;


:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.42  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1143077087  311 NPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRyIGELDQSHFTC 361
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVDLRCASPSSLRGP-LLELLHSEFKC 50
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-312 1.32e-30

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 125.05  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENgiqvirtDTFKHLRHLEILQLSKNLVRKIEVgAFNGLPSLNTLELFDNRLTTVPTqAFEYLSKLRELWLR 166
Cdd:COG4886    97 NLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 167 NNPIESIPSyafnrvpslrrldlgelkrleyiseaAFEGLVNLRYLNLGMCNLKDIPN-LTALVRLEELELSGNRLDLIr 245
Cdd:COG4886   168 NNQLTDLPE--------------------------ELGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDL- 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 246 PGSFQGLTSLRKLWLMHAQVATIErnAFDDLKSLEELNLSHNNLMSLPHDLftPLHRLERVHLNHNP 312
Cdd:COG4886   221 PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQ 283
I-set pfam07679
Immunoglobulin I-set domain;
364-453 1.09e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSyRVRISVLHD-GTLNFTNVTVQDTGQYTCMVTNS 441
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTvTGTPDPEVSWFK-DGQPLRSSD-RFKVTYEGGtYTLTISNVQPDDSGKYTCVATNS 78

                          90
                  ....*....|..
gi 1143077087 442 AGNTTASATLNV 453
Cdd:pfam07679  79 AGEAEASAELTV 90
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 126-312 1.44e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 76.36  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 126 EVGAFNGLPSLNTLELFDNRLTTVPtqAFEYLSKLRELWLRNNPIESIPSyaFNRVPSLRRLDLG--ELKRLEyiseaAF 203
Cdd:cd21340    16 KIDNLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGgnRISVVE-----GL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 204 EGLVNLRYLNL-------GMCNLKDIPNLTALVR-LEELELSGNRLDlirpgsfqgltSLRKLWLmhaqvatiernafdd 275
Cdd:cd21340    87 ENLTNLEELHIenqrlppGEKLTFDPRSLAALSNsLRVLNISGNNID-----------SLEPLAP--------------- 140

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1143077087 276 LKSLEELNLSHNNLMSLPH--DLFTPLHRLERVHLNHNP 312
Cdd:cd21340   141 LRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNP 179
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 370-453 5.39e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 5.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  370 PTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSyrvRISVLHDG---TLNFTNVTVQDTGQYTCMVTNSAGNT 445
Cdd:smart00410   1 PPSVTVKEGESVTLSCEaSGSPPPEVTWYKQGGKLLAESG---RFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                   ....*...
gi 1143077087  446 TASATLNV 453
Cdd:smart00410  78 SSGTTLTV 85
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 364-453 1.20e-13

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 66.73  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGSyrvRISVLHDGTLNFTNVTVQDTGQYTCMVTNSA 442
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKArGDPEPAIHWISPEGKLISNSS---RTLVYDNGTLDILITTVKDTGAFTCIASNPA 77

                          90
                  ....*....|.
gi 1143077087 443 GNTTASATLNV 453
Cdd:cd05764    78 GEATARVELHI 88
LRR_8 pfam13855
Leucine rich repeat;
87-146 6.90e-13

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 63.70  E-value: 6.90e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENGIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRL 146
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 111-311 9.71e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 55.62  E-value: 9.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 111 HLEILQLS-KNLVRKIEVGAFnGLPSLNTLELFDNRLT-TVPTQAFEYLSKLRELWLRNN------PIESIPS-YAFN-- 179
Cdd:PLN00113   70 RVVSIDLSgKNISGKISSAIF-RLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNnftgsiPRGSIPNlETLDls 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 180 ------RVP-------SLRRLDLG-------------ELKRLEYISEAA--FEGLV--------NLRYLNLGMCNLK-DI 222
Cdd:PLN00113  149 nnmlsgEIPndigsfsSLKVLDLGgnvlvgkipnsltNLTSLEFLTLASnqLVGQIprelgqmkSLKWIYLGYNNLSgEI 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 223 PN-LTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLH 301
Cdd:PLN00113  229 PYeIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQ 308

                         250
                  ....*....|
gi 1143077087 302 RLERVHLNHN 311
Cdd:PLN00113  309 NLEILHLFSN 318
LRRNT smart00013
Leucine rich repeat N-terminal domain;
57-90 1.69e-05

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 41.92  E-value: 1.69e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1143077087   57 CPVACSCSnqASRVICTRRDLAEVPASIPVNTRY 90
Cdd:smart00013   2 CPAPCNCS--GTAVDCSGRGLTEVPLDLPPDTTL 33
LRRCT smart00082
Leucine rich repeat C-terminal domain;
311-361 1.72e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.42  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1143077087  311 NPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRyIGELDQSHFTC 361
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVDLRCASPSSLRGP-LLELLHSEFKC 50
LRR smart00370
Leucine-rich repeats, outliers;
276-297 4.67e-04

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 37.72  E-value: 4.67e-04
                           10        20
                   ....*....|....*....|..
gi 1143077087  276 LKSLEELNLSHNNLMSLPHDLF 297
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAF 22
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 283-349 5.65e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 43.53  E-value: 5.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143077087  283 NLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKET-VPSNTTCCARCHAPAGLKGR 349
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKgVKVRQPEAALCAGPGALAGQ 68
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 57-85 2.22e-03

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 36.07  E-value: 2.22e-03
                          10        20
                  ....*....|....*....|....*....
gi 1143077087  57 CPVACSCSnqASRVICTRRDLAEVPASIP 85
Cdd:pfam01462   2 CPVPCHCS--ATVVNCSDRGLTAVPRDLP 28
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-312 1.32e-30

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 125.05  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENgiqvirtDTFKHLRHLEILQLSKNLVRKIEVgAFNGLPSLNTLELFDNRLTTVPTqAFEYLSKLRELWLR 166
Cdd:COG4886    97 NLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 167 NNPIESIPSyafnrvpslrrldlgelkrleyiseaAFEGLVNLRYLNLGMCNLKDIPN-LTALVRLEELELSGNRLDLIr 245
Cdd:COG4886   168 NNQLTDLPE--------------------------ELGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDL- 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 246 PGSFQGLTSLRKLWLMHAQVATIErnAFDDLKSLEELNLSHNNLMSLPHDLftPLHRLERVHLNHNP 312
Cdd:COG4886   221 PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-334 2.47e-29

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 121.19  E-value: 2.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENGIQVIrTDTFKHLRHLEILQLSKNLVRKIEVgAFNGLPSLNTLELFDNRLTTVPTqAFEYLSKLRELWLR 166
Cdd:COG4886   114 NLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 167 NNPIESIPSyAFNRVPSLRRLDLGElKRLEYISEAaFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRP 246
Cdd:COG4886   191 NNQITDLPE-PLGNLTNLEELDLSG-NQLTDLPEP-LANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPP 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 247 GSfqGLTSLRKLWLMHAQVATI---ERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLS 323
Cdd:COG4886   268 LA--NLTNLKTLDLSNNQLTDLklkELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLS 345

                         250
                  ....*....|.
gi 1143077087 324 WWLKETVPSNT 334
Cdd:COG4886   346 LLALLTLLLLL 356
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
111-311 1.86e-20

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 111 HLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLG 190
Cdd:COG4886    17 LLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 191 ELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIP-NLTALVRLEELELSGNRLDLIrPGSFQGLTSLRKLWLMHAQVATIE 269
Cdd:COG4886    97 NLTELDLSGNEELSNLTNLESLDLSGNQLTDLPeELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLP 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1143077087 270 rNAFDDLKSLEELNLSHNNLMSLPHDLfTPLHRLERVHLNHN 311
Cdd:COG4886   176 -EELGNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSGN 215
I-set pfam07679
Immunoglobulin I-set domain;
364-453 1.09e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.68  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSyRVRISVLHD-GTLNFTNVTVQDTGQYTCMVTNS 441
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTvTGTPDPEVSWFK-DGQPLRSSD-RFKVTYEGGtYTLTISNVQPDDSGKYTCVATNS 78

                          90
                  ....*....|..
gi 1143077087 442 AGNTTASATLNV 453
Cdd:pfam07679  79 AGEAEASAELTV 90
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 126-312 1.44e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 76.36  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 126 EVGAFNGLPSLNTLELFDNRLTTVPtqAFEYLSKLRELWLRNNPIESIPSyaFNRVPSLRRLDLG--ELKRLEyiseaAF 203
Cdd:cd21340    16 KIDNLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGgnRISVVE-----GL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 204 EGLVNLRYLNL-------GMCNLKDIPNLTALVR-LEELELSGNRLDlirpgsfqgltSLRKLWLmhaqvatiernafdd 275
Cdd:cd21340    87 ENLTNLEELHIenqrlppGEKLTFDPRSLAALSNsLRVLNISGNNID-----------SLEPLAP--------------- 140

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1143077087 276 LKSLEELNLSHNNLMSLPH--DLFTPLHRLERVHLNHNP 312
Cdd:cd21340   141 LRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNP 179
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 370-453 5.39e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 5.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  370 PTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSyrvRISVLHDG---TLNFTNVTVQDTGQYTCMVTNSAGNT 445
Cdd:smart00410   1 PPSVTVKEGESVTLSCEaSGSPPPEVTWYKQGGKLLAESG---RFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                   ....*...
gi 1143077087  446 TASATLNV 453
Cdd:smart00410  78 SSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 364-440 3.94e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.98  E-value: 3.94e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWlTPNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTN 440
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEaTGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 364-453 1.20e-13

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 66.73  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGSyrvRISVLHDGTLNFTNVTVQDTGQYTCMVTNSA 442
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKArGDPEPAIHWISPEGKLISNSS---RTLVYDNGTLDILITTVKDTGAFTCIASNPA 77

                          90
                  ....*....|.
gi 1143077087 443 GNTTASATLNV 453
Cdd:cd05764    78 GEATARVELHI 88
LRR_8 pfam13855
Leucine rich repeat;
87-146 6.90e-13

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 63.70  E-value: 6.90e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENGIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRL 146
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 87-293 1.25e-12

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 67.50  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  87 NTRYLNLQENGIQVIrtDTFKHLRHLEILQLSKNLVRKIEVgaFNGLPSLNTLELFDNRLTTVptQAFEYLSKLRELWLR 166
Cdd:cd21340    25 NLKVLYLYDNKITKI--ENLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVV--EGLENLTNLEELHIE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 167 NNpiesipsyafnrvpslrRLDLGELKRLEYISEAAFEGlvNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDlirp 246
Cdd:cd21340    99 NQ-----------------RLPPGEKLTFDPRSLAALSN--SLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQIS---- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1143077087 247 gSFQGLTSLrklwlmhaqvatiernaFDDLKSLEELNLSHNNLMSLP 293
Cdd:cd21340   156 -DLEELLDL-----------------LSSWPSLRELDLTGNPVCKKP 184
LRR_8 pfam13855
Leucine rich repeat;
230-289 1.30e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.93  E-value: 1.30e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 230 RLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNL 289
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
110-170 2.23e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.16  E-value: 2.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143077087 110 RHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPI 170
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 367-453 3.27e-11

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.72  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 367 VEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMthgsyRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNT 445
Cdd:cd05725     1 VKRPQNQVVLVDDSAEFQCEVgGDPVPTVRWRKEDGELP-----KGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKI 75


                  ....*...
gi 1143077087 446 TASATLNV 453
Cdd:cd05725    76 EASATLTV 83
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 365-453 5.26e-11

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 59.43  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 365 VIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSyrvRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAG 443
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQaTGEPVPTISWLKDGVPLLGKDE---RITTLENGSLQIKGAEKSDTGEYTCVALNLSG 77

                          90
                  ....*....|
gi 1143077087 444 NTTASATLNV 453
Cdd:cd20952    78 EATWSAVLDV 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 381-450 1.54e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 57.34  E-value: 1.54e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143077087 381 AELKCR-TGTSMTSVNWLTpNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASAT 450
Cdd:cd00096     1 VTLTCSaSGNPPPTITWYK-NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-304 1.72e-10

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.80  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  76 DLAEVPASIPVNT--RYLNLQENGIQVIrTDTFKHLRHLEILQLSKNLVRKIEvgAFNGLPSLNTLELFDNRLTTVPTQA 153
Cdd:COG4886   193 QITDLPEPLGNLTnlEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 154 FeyLSKLRELWLRNNPIESIpsyafnrvpSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVR-LE 232
Cdd:COG4886   270 N--LTNLKTLDLSNNQLTDL---------KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVtLT 338

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143077087 233 ELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLE 304
Cdd:COG4886   339 TLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDA 410
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 364-453 3.92e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 57.12  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSyrvRISVLHDG----TLNFTNVTVQDTGQYTCMV 438
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKvSGLPTPDLFWQL-NGKPVRPDS---AHKMLVREngrhSLIIEPVTKRDAGIYTCIA 76

                          90
                  ....*....|....*
gi 1143077087 439 TNSAGNTTASATLNV 453
Cdd:cd05744    77 RNRAGENSFNAELVV 91
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 96-210 4.34e-10

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 57.94  E-value: 4.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  96 NGIQVIRTDTFKHLRHLEILQLSKNLvRKIEVGAFNGLpSLNTLElFDNRLTTVPTQAFEYLSKLRELWLRNNpIESIPS 175
Cdd:pfam13306  20 SSLTSIGEYAFSNCTSLKSITLPSSL-TSIGSYAFYNC-SLTSIT-IPSSLTSIGEYAFSNCSNLKSITLPSN-LTSIGS 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1143077087 176 YAFNRVpSLRRLDLGELkrLEYISEAAFEGLVNLR 210
Cdd:pfam13306  96 YAFSNC-SLKSITIPSS--VTTIGSYAFSNCSNLK 127
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 366-443 6.74e-10

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 56.10  E-value: 6.74e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143077087 366 IVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGsyrvRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAG 443
Cdd:cd20968     2 ITRPPTNVTIIEGLKAVLPCTTmGNPKPSVSWIKGDDLIKENN----RIAVLESGSLRIHNVQKEDAGQYRCVAKNSLG 76
LRR_8 pfam13855
Leucine rich repeat;
158-219 9.01e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 9.01e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143077087 158 SKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGElKRLEYISEAAFEGLVNLRYLNLGMCNL 219
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSN-NLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 49-217 1.84e-09

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 59.68  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  49 GGSPPATSCPVACSCSNQASRVICTRR--------DLAEVpasIPVNTRY--LNLQENGIQV--IRT--DTFKHLRHLEI 114
Cdd:cd00116   121 GDRGLRLLAKGLKDLPPALEKLVLGRNrlegasceALAKA---LRANRDLkeLNLANNGIGDagIRAlaEGLKANCNLEV 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 115 LQLSKNLVRKIEVGAFNG----LPSLNTLELFDNRLTTVPTQAF-----EYLSKLRELWLRNNPIESIPSYAFNRV---- 181
Cdd:cd00116   198 LDLNNNGLTDEGASALAEtlasLKSLEVLNLGDNNLTDAGAAALasallSPNISLLTLSLSCNDITDDGAKDLAEVlaek 277

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1143077087 182 PSLRRLDLGELKRLEYISEAAFEGL----VNLRYLNLGMC 217
Cdd:cd00116   278 ESLLELDLRGNKFGEEGAQLLAESLlepgNELESLWVKDD 317
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 103-311 1.12e-08

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 57.37  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 103 TDTFKHLRHLEILQLSKNLVRKIEVGA-FNGL---PSLNTLELFDNRL------TTVPTQAFEYLSKLRELWLRNNPIE- 171
Cdd:cd00116    16 TELLPKLLCLQVLRLEGNTLGEEAAKAlASALrpqPSLKELCLSLNETgriprgLQSLLQGLTKGCGLQELDLSDNALGp 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 172 --SIPSYAFNRVPSLRRLDL---GELKR-LEYISEAAFEGLVNLRYLNLGMCNL-----KDIPN-LTALVRLEELELSGN 239
Cdd:cd00116    96 dgCGVLESLLRSSSLQELKLnnnGLGDRgLRLLAKGLKDLPPALEKLVLGRNRLegascEALAKaLRANRDLKELNLANN 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 240 rlDLIRPGS---FQGL---TSLRKLWL-----MHAQVATIErNAFDDLKSLEELNLSHNNLMSLP----HD-LFTPLHRL 303
Cdd:cd00116   176 --GIGDAGIralAEGLkanCNLEVLDLnnnglTDEGASALA-ETLASLKSLEVLNLGDNNLTDAGaaalASaLLSPNISL 252


                  ....*...
gi 1143077087 304 ERVHLNHN 311
Cdd:cd00116   253 LTLSLSCN 260
LRR_8 pfam13855
Leucine rich repeat;
134-189 1.49e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 51.37  E-value: 1.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1143077087 134 PSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDL 189
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDL 56
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 365-453 1.65e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 52.39  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 365 VIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSYRvriSVLHDGTLNFTNVTVQDTGQYTCMVTNSAG 443
Cdd:cd20978     3 FIQKPEKNVVVKGGQDVTLPCQvTGVPQPKITWLH-NGKPLQGPMER---ATVEDGTLTIINVQPEDTGYYGCVATNEIG 78

                          90
                  ....*....|
gi 1143077087 444 NTTASATLNV 453
Cdd:cd20978    79 DIYTETLLHV 88
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 370-453 1.66e-08

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 52.24  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 370 PTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSYRvRISVLHDGTLNF-TNVTVQDTGQYTCMVTNSAGNTTA 447
Cdd:cd05763     6 PHDITIRAGSTARLECAaTGHPTPQIAWQKDGGTDFPAARER-RMHVMPEDDVFFiVDVKIEDTGVYSCTAQNSAGSISA 84


                  ....*.
gi 1143077087 448 SATLNV 453
Cdd:cd05763    85 NATLTV 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 363-453 1.72e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 52.25  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 363 APVIVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTpNGTLMTHGSYRVRISVLhDGTLNFTNVTVQDTGQYTCMVTNS 441
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSArGKPVPRITWIR-NAQPLQYAADRSTCEAG-VGELHIQDVLPEDHGTYTCLAKNA 78

                          90
                  ....*....|..
gi 1143077087 442 AGNTTASATLNV 453
Cdd:cd20976    79 AGQVSCSAWVTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 369-451 1.79e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 52.20  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 369 PPTDLNVTEGMAAELKC--RTGTSMTSVNWLTPNGTL-----MTHGSYRVRISvlhdgTLNFTNVTVQDTGQYTCMVTNS 441
Cdd:pfam00047   2 APPTVTVLEGDSATLTCsaSTGSPGPDVTWSKEGGTLieslkVKHDNGRTTQS-----SLLISNVTKEDAGTYTCVVNNP 76

                          90
                  ....*....|
gi 1143077087 442 AGNTTASATL 451
Cdd:pfam00047  77 GGSATLSTSL 86
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 363-453 3.45e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 51.41  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 363 APVIVEPPTDLNVTEGMAAELKC-RTGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGT----LNFTNVTVQDTGQYTCM 437
Cdd:cd20956     1 APVLLETFSEQTLQPGPSVSLKCvASGNPLPQITWTLDGFPIPESPRFRVGDYVTSDGDvvsyVNISSVRVEDGGEYTCT 80

                          90
                  ....*....|....*.
gi 1143077087 438 VTNSAGNTTASATLNV 453
Cdd:cd20956    81 ATNDVGSVSHSARINV 96
IgV_1_Necl_like cd05717
First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the ...
 372-436 3.61e-08

First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells.


Pssm-ID: 409382  Cd Length: 94  Bit Score: 51.36  E-value: 3.61e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143077087 372 DLNVTEGMAAELKCRTGTSM-TSVNWLTPNGTLMTHGSYRV----RISVL----HDGTLNFTNVTVQDTGQYTC 436
Cdd:cd05717     5 DVTVVEGETLTLKCQVSLRDdSSLQWLNPNGQTIYFNDKRAlrdsRYQLLnhsaSELSISVSNVTLSDEGVYTC 78
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 111-311 9.71e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 55.62  E-value: 9.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 111 HLEILQLS-KNLVRKIEVGAFnGLPSLNTLELFDNRLT-TVPTQAFEYLSKLRELWLRNN------PIESIPS-YAFN-- 179
Cdd:PLN00113   70 RVVSIDLSgKNISGKISSAIF-RLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNnftgsiPRGSIPNlETLDls 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 180 ------RVP-------SLRRLDLG-------------ELKRLEYISEAA--FEGLV--------NLRYLNLGMCNLK-DI 222
Cdd:PLN00113  149 nnmlsgEIPndigsfsSLKVLDLGgnvlvgkipnsltNLTSLEFLTLASnqLVGQIprelgqmkSLKWIYLGYNNLSgEI 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 223 PN-LTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLH 301
Cdd:PLN00113  229 PYeIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQ 308

                         250
                  ....*....|
gi 1143077087 302 RLERVHLNHN 311
Cdd:PLN00113  309 NLEILHLFSN 318
LRR_8 pfam13855
Leucine rich repeat;
208-262 1.12e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.06  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 208 NLRYLNLGMCNLKDIP--NLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMH 262
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDdgAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSG 58
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 375-453 1.17e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.77  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 375 VTEGMAAELKCR-TGTSMTSVNWlTPNGTLMTHGSyrvRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNV 453
Cdd:cd04969    14 AAKGGDVIIECKpKASPKPTISW-SKGTELLTNSS---RICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 124-280 1.73e-07

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 50.62  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 124 KIEVGAFNGLpSLNTLELFDNrLTTVPTQAFEYLSKLRELWLRNNpIESIPSYAFNRVpSLRRLDLGElkRLEYISEAAF 203
Cdd:pfam13306   2 SIGSYAFYNC-SLTSITIPSS-LTSIGEYAFSNCTSLKSITLPSS-LTSIGSYAFYNC-SLTSITIPS--SLTSIGEYAF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 204 EGLVNLRYLNLgMCNLKDIPNltalvrleelelsgnrldlirpGSFQGlTSLRKLwLMHAQVATIERNAFDDLKSLE 280
Cdd:pfam13306  76 SNCSNLKSITL-PSNLTSIGS----------------------YAFSN-CSLKSI-TIPSSVTTIGSYAFSNCSNLK 127
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 363-453 2.11e-07

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 49.93  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 363 APVIVEPptDLNVTEGMAAELKCR--TGTSMTSVNW--LTPNG--TLMTH---------GSYRVRISV----LHDGTLNF 423
Cdd:cd05887     1 GPIIVEP--HVTAVWGKNVSLKCLieVNETITQISWekIHGKSsqTVAVHhpqygisiqGEYQGRVSFknysLNDATITL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1143077087 424 TNVTVQDTGQYTC-MVTNSAGNTTASATLNV 453
Cdd:cd05887    79 HNVGFSDSGKYICkAVTFPLGNAQSSTTVTV 109
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 364-454 4.34e-07

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 48.70  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMT-HGSYRVRISVLHDGTLNFTNV-----TVQDTGQYTC 436
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAeGRPTPTIQWLKNGQPLETdKDDPRSHRIVLPSGSLFFLRVvhgrkGRSDEGVYVC 80

                          90
                  ....*....|....*....
gi 1143077087 437 MVTNSAGN-TTASATLNVS 454
Cdd:cd07693    81 VAHNSLGEaVSRNASLEVA 99
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 368-453 1.10e-06

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 47.84  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 368 EPPTDLNVTEGMAAELKCRTGTSM----TSVNW------------LTPNGTLMTHGSYRVRISVL-----HDGTLNFTNV 426
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMseasTSVYWyrqppgkgptflIAYYSNGSEEGVKKGRFSGRgdpsnGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*...
gi 1143077087 427 TVQDTGQYTCMV-TNSAGNTTASATLNV 453
Cdd:pfam07686  81 TLSDSGTYTCAViPSGEGVFGKGTRLTV 108
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 375-453 1.24e-06

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 47.00  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 375 VTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGSyRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNV 453
Cdd:cd20969    14 VDEGHTVQFVCRAdGDPPPAILWLSPRKHLVSAKS-NGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 366-451 4.56e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 4.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 366 IVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGSYRVrISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGN 444
Cdd:cd05747     6 ILTKPRSLTVSEGESARFSCDVdGEPAPTVTWMREGQIIVSSQRHQI-TSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84


                  ....*..
gi 1143077087 445 TTASATL 451
Cdd:cd05747    85 QEAQFTL 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 364-453 5.47e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.42  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGT-LNFTNVTVQDTGQYTCMVTNS 441
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHvSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAkLSIPAVTKANSGRYSLTATNG 80

                          90
                  ....*....|..
gi 1143077087 442 AGNTTASATLNV 453
Cdd:cd20974    81 SGQATSTAELLV 92
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 366-453 5.58e-06

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 45.32  E-value: 5.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 366 IVEPPTDLNVteGMAAELKCRTGTSMTSVNWLTPNG--TLMTHGSYRVrisVLHDG---TLNFTNVTVQDTGQYTCMVTN 440
Cdd:cd04977     5 IIPSYAEISV--GESKFFLCKVSGDAKNINWVSPNGekVLTKHGNLKV---VNHGSvlsSLTIYNANINDAGIYKCVATN 79

                          90
                  ....*....|...
gi 1143077087 441 SAGnTTASATLNV 453
Cdd:cd04977    80 GKG-TESEATVKL 91
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 367-456 5.67e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 45.33  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 367 VEPPTDLNVTEGMAAELKCRT-GTSMTSVNW--------LTPNGTLMTHGsyrvRISVLHDGTLNFTNVTVQDTGQYTCM 437
Cdd:cd05726     3 VVKPRDQVVALGRTVTFQCETkGNPQPAIFWqkegsqnlLFPYQPPQPSS----RFSVSPTGDLTITNVQRSDVGYYICQ 78

                          90
                  ....*....|....*....
gi 1143077087 438 VTNSAGNTTASATLNVSAV 456
Cdd:cd05726    79 ALNVAGSILAKAQLEVTDV 97
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 383-453 5.96e-06

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 45.46  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 383 LKCR-TGTSMTSVNWLTPNGTLMTH-------------GSYRVRISVLHD------GTLNFTNVTVQDTGQYTCMVTNSA 442
Cdd:cd16091    17 LPCSfTPGSEVVIHWYKQDSDIKVHsyyygkdqlesqdQRYRNRTSLFKDqisngnASLLLRRVQLQDEGRYKCYTSTII 96

                          90
                  ....*....|.
gi 1143077087 443 GNTTASATLNV 453
Cdd:cd16091    97 GNQESFVNLKV 107
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 367-453 6.12e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.13  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 367 VEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGSYRVRisVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNT 445
Cdd:cd04978     3 IIEPPSLVLSPGETGELICEAeGNPQPTITWRLNGVPIEPAPEDMRR--TVDGRTLIFSNLQPNDTAVYQCNASNVHGYL 80


                  ....*...
gi 1143077087 446 TASATLNV 453
Cdd:cd04978    81 LANAFLHV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 368-453 7.26e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.87  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 368 EPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMThgSYRVRISVLHDG--TLNFTNVTVQDTGQYTCMVTNSAGN 444
Cdd:cd20973     2 QTLRDKEVVEGSAARFDCKVeGYPDPEVKWMKDDNPIVE--SRRFQIDQDEDGlcSLIISDVCGDDSGKYTCKAVNSLGE 79


                  ....*....
gi 1143077087 445 TTASATLNV 453
Cdd:cd20973    80 ATCSAELTV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 370-451 7.78e-06

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 370 PTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSyrvRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTAS 448
Cdd:cd20957     8 PPVQTVDFGRTAVFNCSvTGNPIHTVLWMK-DGKPLGHSS---RVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQAT 83


                  ...
gi 1143077087 449 ATL 451
Cdd:cd20957    84 AEL 86
LRR_9 pfam14580
Leucine-rich repeat;
91-196 1.02e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 46.68  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  91 LNLQENGIQviRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPT-QAFEYLSKLRELWLRNNP 169
Cdd:pfam14580  47 IDFSDNEIR--KLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDlDPLASLKKLTFLSLLRNP 124

                          90       100       110
                  ....*....|....*....|....*....|
gi 1143077087 170 IESIP---SYAFNRVPSLRRLDLGELKRLE 196
Cdd:pfam14580 125 VTNKPhyrLYVIYKVPQLRLLDFRKVKQKE 154
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 364-453 1.22e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.33  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSYRVRISVLHDG---TLNFTNVTVQDTGQYTCMVT 439
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEvQGKPDPEVKWYK-NGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAK 79

                          90
                  ....*....|....
gi 1143077087 440 NSAGNTTASATLNV 453
Cdd:cd20951    80 NIHGEASSSASVVV 93
LRRNT smart00013
Leucine rich repeat N-terminal domain;
57-90 1.69e-05

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 41.92  E-value: 1.69e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1143077087   57 CPVACSCSnqASRVICTRRDLAEVPASIPVNTRY 90
Cdd:smart00013   2 CPAPCNCS--GTAVDCSGRGLTEVPLDLPPDTTL 33
LRRCT smart00082
Leucine rich repeat C-terminal domain;
311-361 1.72e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.42  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1143077087  311 NPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRyIGELDQSHFTC 361
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVDLRCASPSSLRGP-LLELLHSEFKC 50
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 364-453 1.84e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.60  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLMTHGSYRvrISVLHDGT----LNFTNVTVQDTGQYTCMVT 439
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDR--ISLYQDNCgricLLIQNANKKDAGWYTVSAV 78

                          90
                  ....*....|....
gi 1143077087 440 NSAGNTTASATLNV 453
Cdd:cd05892    79 NEAGVVSCNARLDV 92
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 208-241 2.45e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.85  E-value: 2.45e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1143077087 208 NLRYLNLGMCNLKDIPNLTALVRLEELELSGNRL 241
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNNK 35
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 363-453 2.51e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 43.34  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 363 APVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLmtHGSYRVRISV---LHdgTLNFTNVTVQDTGQYTCMV 438
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRvTGNPTPVVRWFCEGKEL--QNSPDIQIHQegdLH--SLIIAEAFEEDTGRYSCLA 76

                          90
                  ....*....|....*
gi 1143077087 439 TNSAGNTTASATLNV 453
Cdd:cd20972    77 TNSVGSDTTSAEIFV 91
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 392-453 2.69e-05

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 43.49  E-value: 2.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143077087 392 TSVNWLTPNGTLMThgSYRVRISVLHD----GTLNFTNVTVQDTGQYTCMVTNSAGnTTASATLNV 453
Cdd:cd05865    31 KDISWFSPNGEKLT--PNQQRISVVRNddysSTLTIYNANIDDAGIYKCVVSNEDE-GESEATVNV 93
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 383-453 3.03e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 43.36  E-value: 3.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143077087 383 LKC-RTGTSMTSVNWLTPNGTLMTH---GSYRVRISVLhdgTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNV 453
Cdd:cd05729    24 LECgAGGNPMPNITWLKDGKEFKKEhriGGTKVEEKGW---SLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 366-443 3.06e-05

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 43.07  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 366 IVEPpTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTlmTHGSYR-----VRISVLHDGTLNFTNVTVQDTGQYTCMVT 439
Cdd:cd20954     5 IVEP-VDANVAAGQDVMLHCQAdGFPTPTVTWKKATGS--TPGEYKdllydPNVRILPNGTLVFGHVQKENEGHYLCEAK 81


                  ....
gi 1143077087 440 NSAG 443
Cdd:cd20954    82 NGIG 85
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 125-285 3.16e-05

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 47.56  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  125 IEVGAFNGLPSLNTLELFDNRLTTVP------TQAFEYL-SKLRELWLRNNPIESIPSyAFnRVPSLRRLDLGELKrLEY 197
Cdd:PLN03210   549 IHENAFKGMRNLLFLKFYTKKWDQKKevrwhlPEGFDYLpPKLRLLRWDKYPLRCMPS-NF-RPENLVKLQMQGSK-LEK 625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  198 ISEAAFEgLVNLRYLNL-GMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWL---MHAQVATIERNaf 273
Cdd:PLN03210   626 LWDGVHS-LTGLRNIDLrGSKNLKEIPDLSMATNLETLKLSDCSSLVELPSSIQYLNKLEDLDMsrcENLEILPTGIN-- 702

                          170
                   ....*....|..
gi 1143077087  274 ddLKSLEELNLS 285
Cdd:PLN03210   703 --LKSLYRLNLS 712
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 105-313 3.27e-05

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 47.56  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  105 TFKHLRHLEiLQLSKNLvrkIEVGAFNGLPSLNTLELFD-NRLTTVPTqAFEYLSKLRELWL-RNNPIESIPSyAFNrVP 182
Cdd:PLN03210   632 SLTGLRNID-LRGSKNL---KEIPDLSMATNLETLKLSDcSSLVELPS-SIQYLNKLEDLDMsRCENLEILPT-GIN-LK 704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  183 SLRRLDLGELKRLE------------YISEAAFEGL-VNLRY---LNLGMCNLKD------IPNLTALVR-----LEELE 235
Cdd:PLN03210   705 SLYRLNLSGCSRLKsfpdistniswlDLDETAIEEFpSNLRLenlDELILCEMKSeklwerVQPLTPLMTmlspsLTRLF 784

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  236 LSGNRLDLIRPGSFQGLTSLRKLWLMHA-QVATIERNAfdDLKSLEELNLSH-NNLMSLP------HDLFTPLHRLERVh 307
Cdd:PLN03210   785 LSDIPSLVELPSSIQNLHKLEHLEIENCiNLETLPTGI--NLESLESLDLSGcSRLRTFPdistniSDLNLSRTGIEEV- 861


                   ....*.
gi 1143077087  308 lnhnPW 313
Cdd:PLN03210   862 ----PW 863
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 365-451 3.33e-05

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 42.93  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 365 VIVEPPTDLNVTEGMAAELKCR--TGTSMTSVNWLTPNGTLMTHGsyrvrisvlHD--GTLNFTNVTVQDTGQYTCMVTN 440
Cdd:cd05754     3 VTVEEPRSQEVRPGADVSFICRakSKSPAYTLVWTRVNGTLPSRA---------MDfnGILTIRNVQLSDAGTYVCTGSN 73

                          90
                  ....*....|.
gi 1143077087 441 SAGNTTASATL 451
Cdd:cd05754    74 MLDTDEATATL 84
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 367-453 4.86e-05

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409454  Cd Length: 89  Bit Score: 42.66  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 367 VEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLM----THGSYRVrisvlhDG-TLNFTNVTVQDTGQYTCMVTN 440
Cdd:cd05868     3 ITAPTNLVLSPGEDGTLICRaNGNPKPSISWLT-NGVPIeiapTDPSRKV------DGdTIIFSKVQERSSAVYQCNASN 75

                          90
                  ....*....|...
gi 1143077087 441 SAGNTTASATLNV 453
Cdd:cd05868    76 EYGYLLANAFVNV 88
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 370-451 5.16e-05

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.18  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 370 PTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSYrvrISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTAS 448
Cdd:cd05723     4 PSNIYAHESMDIVFECEvTGKPTPTVKWVK-NGDVVIPSDY---FKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQAS 79


                  ...
gi 1143077087 449 ATL 451
Cdd:cd05723    80 AQL 82
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 89-188 6.56e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.78  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  89 RYLNLQENGIQVIrtDTFKHLRHLEILQLSKNLVRKIEvgafnglpslntlELfdnrlttvpTQAFEYLSKLRELWLRNN 168
Cdd:cd21340   123 RVLNISGNNIDSL--EPLAPLRNLEQLDASNNQISDLE-------------EL---------LDLLSSWPSLRELDLTGN 178

                          90       100
                  ....*....|....*....|....
gi 1143077087 169 PIESIPSYaFNRV----PSLRRLD 188
Cdd:cd21340   179 PVCKKPKY-RDKIilasKSLEVLD 201
IgI_3_CSF-1R cd20936
Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), ...
 364-453 6.75e-05

Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), and similar domains; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R) and similar proteins. CSF-1R, a class III receptor tyrosine kinase (RTKIII), is critical to the survival, proliferation, and differentiation of mononuclear phagocytic cells such as monocytes, tissue macrophages, muscularis macrophages, microglia, osteoclasts, Paneth cells, and myeloid dendritic cells. Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409530  Cd Length: 93  Bit Score: 42.25  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCrtGTSMTSVNWltpnGTLMTHGSYRVRI---SVLHDG------TLNFTNVTVQDTGQY 434
Cdd:cd20936     1 PALTLEPAELVRIRGEAAQIVC--SASNVDVNF----DVFLQHGDTKLAIpqqSDFHDNryqkvlTLNLDQVDFQDAGNY 74

                          90
                  ....*....|....*....
gi 1143077087 435 TCMVTNSAGNTTASATLNV 453
Cdd:cd20936    75 SCVASNVQGKHSASMFFRV 93
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 412-453 7.17e-05

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 41.91  E-value: 7.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1143077087 412 RISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNV 453
Cdd:cd05852    48 RISIWDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 364-453 9.63e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 41.72  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEP--PTDLNVTEGMAAELKCR-TGTSMTSVNWLTpNGTLMTHGSYRVRisVLHDGT-LNFTNVTVQDTGQYTCMVT 439
Cdd:cd20970     1 PVISTPqpSFTVTAREGENATFMCRaEGSPEPEISWTR-NGNLIIEFNTRYI--VRENGTtLTIRNIRRSDMGIYLCIAS 77

                          90
                  ....*....|....*
gi 1143077087 440 NSAGNTTASA-TLNV 453
Cdd:cd20970    78 NGVPGSVEKRiTLQV 92
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 364-451 1.01e-04

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 41.85  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAE---LKCRT-GTSMTSVNWLTPNGTLMTHGSYRVRisvLHDGTLNFTN-VTVQDTGQYTCMV 438
Cdd:cd04967     2 PVFEEQPDDTIFPEDSDEKkvaLNCRArANPVPSYRWLMNGTEIDLESDYRYS---LVDGTLVISNpSKAKDAGHYQCLA 78

                          90
                  ....*....|....
gi 1143077087 439 TNSAGNTTAS-ATL 451
Cdd:cd04967    79 TNTVGSVLSReATL 92
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 367-453 1.22e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 41.05  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 367 VEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGsyrvRISVLhDGTLNFTNVTVQDTGQYTCMVTNSAGNT 445
Cdd:cd05728     3 LKVISDTEADIGSSLRWECKaSGNPRPAYRWLKNGQPLASEN----RIEVE-AGDLRITKLSLSDSGMYQCVAENKHGTI 77


                  ....*...
gi 1143077087 446 TASATLNV 453
Cdd:cd05728    78 YASAELAV 85
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 109-314 1.26e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 109 LRHLEILQL-SKNLVRKIEVgAFNGLPSLNTLELFDNRLT-------------TVPTQAFEYLS-----------KLREL 163
Cdd:PLN00113  307 LQNLEILHLfSNNFTGKIPV-ALTSLPRLQVLQLWSNKFSgeipknlgkhnnlTVLDLSTNNLTgeipeglcssgNLFKL 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 164 WLRNNPIES-IPSyAFNRVPSLRRLDL------GELKR------LEY---ISEAAFEGLVNLRYLN---LGMCNLK---- 220
Cdd:PLN00113  386 ILFSNSLEGeIPK-SLGACRSLRRVRLqdnsfsGELPSeftklpLVYfldISNNNLQGRINSRKWDmpsLQMLSLArnkf 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 221 --DIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLM------------------------HAQVATIERNAFD 274
Cdd:PLN00113  465 fgGLPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSenklsgeipdelssckklvsldlsHNQLSGQIPASFS 544

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1143077087 275 DLKSLEELNLSHNNLM-SLPHDLfTPLHRLERVHLNHNPWH 314
Cdd:PLN00113  545 EMPVLSQLDLSQNQLSgEIPKNL-GNVESLVQVNISHNHLH 584
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 412-454 1.39e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 41.01  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1143077087 412 RISVLHDGTLNFTNVT-VQDTGQYTCMVTNSAGNtTASATLNVS 454
Cdd:cd20958    46 RQRVFPNGTLVIENVQrSSDEGEYTCTARNQQGQ-SASRSVFVK 88
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 364-453 1.43e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 41.24  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSYR--VRISVLHdgTLNFTNVTVQDTGQYTCMVTN 440
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKvSGLPTPDLSWQLDGKPIRPDSAHKmlVRENGVH--SLIIEPVTSRDAGIYTCIATN 78

                          90
                  ....*....|...
gi 1143077087 441 SAGNTTASATLNV 453
Cdd:cd20990    79 RAGQNSFNLELVV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 367-453 1.71e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.78  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 367 VEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGtLNFTNVTVQDTGQYTCMVTNSAGNT 445
Cdd:cd20949     3 TENAYVTTVKEGQSATILCEVkGEPQPNVTWHFNGQPISASVADMSKYRILADG-LLINKVTQDDTGEYTCRAYQVNSIA 81


                  ....*...
gi 1143077087 446 TASATLNV 453
Cdd:cd20949    82 SDMQERTV 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 370-443 1.90e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 40.85  E-value: 1.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143077087 370 PTDLNVTEGMAAELKCRT--GTSMTSVNWLTpNGTLMTHGSYRVRIsvLHDGTLNFTNVTVQDTGQYTCMVTNSAG 443
Cdd:cd05724     4 PSDTQVAVGEMAVLECSPprGHPEPTVSWRK-DGQPLNLDNERVRI--VDDGNLLIAEARKSDEGTYKCVATNMVG 76
IgI_3_hemolin-like cd20977
Third immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 364-450 2.01e-04

Third immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The third Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM).


Pssm-ID: 409569  Cd Length: 93  Bit Score: 40.84  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCRTGTSMTS-VNWLTPNGTLMTHGSYRV-RISVLHDGTLNFTNVTVQDTGQYTCMVTNS 441
Cdd:cd20977     1 PVPQYVSKDMMAKAGDVTMIYCMYGSNPTAhPNYFKNGKDVNGNPEDRItRHNRTSGKRLLFKTTLPEDEGVYTCEVDNG 80


                  ....*....
gi 1143077087 442 AGNTTASAT 450
Cdd:cd20977    81 VGKPQKHSL 89
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 375-439 2.09e-04

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 40.98  E-value: 2.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143077087 375 VTEGMAAELKCRTGTSMTS--VNWLTPNGTLMT--------HGSYRVRISVLhDGTLNFTNVTVQDTGQYTCMVT 439
Cdd:cd20946    11 VVENQEVILSCKTPKKTSSprVEWKKLQRDVTFvvfqnnkiQGDYKGRAEIL-GTNITIKNVTRSDSGKYRCEVS 84
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 375-453 2.27e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 40.57  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 375 VTEGMAAELKCRT--GTSMTSVNWLTPNGTLMTHGSYRVRI-SVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATL 451
Cdd:cd05750    11 VQEGSKLVLKCEAtsENPSPRYRWFKDGKELNRKRPKNIKIrNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNV 90


                  ..
gi 1143077087 452 NV 453
Cdd:cd05750    91 TV 92
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 171-297 2.92e-04

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 41.38  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 171 ESIPSYAFNRVpSLRRLDLGElkRLEYISEAAFEGLVNLRYLNLGMcNLKDIPNLT-ALVRLEELELSGNrLDLIRPGSF 249
Cdd:pfam13306   1 TSIGSYAFYNC-SLTSITIPS--SLTSIGEYAFSNCTSLKSITLPS-SLTSIGSYAfYNCSLTSITIPSS-LTSIGEYAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1143077087 250 QGLTSLRKLWLMHaQVATIERNAFDDLkSLEELNLShNNLMSLPHDLF 297
Cdd:pfam13306  76 SNCSNLKSITLPS-NLTSIGSYAFSNC-SLKSITIP-SSVTTIGSYAF 120
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
 376-451 3.79e-04

Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form.


Pssm-ID: 409457  Cd Length: 87  Bit Score: 39.80  E-value: 3.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143077087 376 TEGMAAELKCRTGTSMTSVNWLTPNGTLmTHGSYRVRIsvLHDGTLNFtNVTVQDTGQYTCMVTNSAGNTTASATL 451
Cdd:cd05873     9 KLGGNAELKCSPKSNLARVVWKFQGKVL-KAESPKYGL--YGDGLLIF-NASEADAGRYQCLSVEKSKAKTFFQTV 80
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 363-453 4.02e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 40.23  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 363 APVIVEPPTDLNVTEGMAAELKCRTG--TSMTSVNWLTPNGTLM----THGSYRVRISVLHDGTLNFTNVTVQDTGQYTC 436
Cdd:cd04970     2 ATRITLAPSNADITVGENATLQCHAShdPTLDLTFTWSFNGVPIdlekIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTC 81

                          90
                  ....*....|....*..
gi 1143077087 437 MVTNSAGNTTASATLNV 453
Cdd:cd04970    82 TAQTVVDSDSASATLVV 98
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 134-177 4.54e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.38  E-value: 4.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1143077087 134 PSLNTLELFDNRLTTVPtqAFEYLSKLRELWL-RNNPIESIPSYA 177
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP--PLAKLPNLETLDLsGNNKITDLSDLA 43
LRR smart00370
Leucine-rich repeats, outliers;
276-297 4.67e-04

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 37.72  E-value: 4.67e-04
                           10        20
                   ....*....|....*....|..
gi 1143077087  276 LKSLEELNLSHNNLMSLPHDLF 297
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAF 22
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
276-297 4.67e-04

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 37.72  E-value: 4.67e-04
                           10        20
                   ....*....|....*....|..
gi 1143077087  276 LKSLEELNLSHNNLMSLPHDLF 297
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAF 22
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 283-349 5.65e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 43.53  E-value: 5.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143077087  283 NLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKET-VPSNTTCCARCHAPAGLKGR 349
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKgVKVRQPEAALCAGPGALAGQ 68
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 364-453 5.90e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 39.55  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCRT-GTSMTSVNWLTpNGTLMTHGSYRvRISVLHDGT-LNFTNVTVQDTGQYTCMVTNS 441
Cdd:cd05736     1 PVIRVYPEFQAKEPGVEASLRCHAeGIPLPRVQWLK-NGMDINPKLSK-QLTLIANGSeLHISNVRYEDTGAYTCIAKNE 78

                          90
                  ....*....|..
gi 1143077087 442 AGNTTASATLNV 453
Cdd:cd05736    79 GGVDEDISSLFV 90
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 378-453 6.79e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 39.46  E-value: 6.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 378 GMAAELKCR-TGTSMTSVNWLTPNGTLMTHGSYRVRISVLhdgTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNV 453
Cdd:cd05856    19 GSSVRLKCVaSGNPRPDITWLKDNKPLTPPEIGENKKKKW---TLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 370-453 7.89e-04

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 39.56  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 370 PTDLNVTEGMAAELKCRT-GTSMTSVNWLT----------PNGT-----LMTHG--SYRVRISVLHdgtlnFTNVTVQDT 431
Cdd:cd05858     8 PANTSVVVGTDAEFVCKVySDAQPHIQWLKhvekngskygPDGLpyvevLKTAGvnTTDKEIEVLY-----LRNVTFEDA 82

                          90       100
                  ....*....|....*....|..
gi 1143077087 432 GQYTCMVTNSAGNTTASATLNV 453
Cdd:cd05858    83 GEYTCLAGNSIGISHHSAWLTV 104
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 377-453 8.55e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 38.38  E-value: 8.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143077087 377 EGMAAELKCR-TGTSMTSVNWLTPNGTLmthgSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNV 453
Cdd:cd05745     1 EGQTVDFLCEaQGYPQPVIAWTKGGSQL----SVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 369-453 8.65e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 38.74  E-value: 8.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 369 PPTDLNVTEGMAAELKC-RTGTSMTSVNWLTPNGTLMTHgsyrvRISVL-HDGTLNFTNVTVQDTGQYTCMVTNSAGNTT 446
Cdd:cd05876     1 SSSSLVALRGQSLVLECiAEGLPTPTVKWLRPSGPLPPD-----RVKYQnHNKTLQLLNVGESDDGEYVCLAENSLGSAR 75


                  ....*..
gi 1143077087 447 ASATLNV 453
Cdd:cd05876    76 HAYYVTV 82
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 91-289 9.99e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 42.08  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087  91 LNLQENGIQVIRTDTFKHlrHLEILQLsknlvrkIEVGAFNGLPSLNTLELFDNRLTTVPTQAF-EYLSK---LRELWLR 166
Cdd:COG5238   146 VLKDPLGGNAVHLLGLAA--RLGLLAA-------ISMAKALQNNSVETVYLGCNQIGDEGIEELaEALTQnttVTTLWLK 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 167 NNPIESIPSYAFNRV----PSLRRLDLGElkrlEYISEaafEGLVNLrylnlgmcnlkdIPNLTALVRLEELELSGNRLD 242
Cdd:COG5238   217 RNPIGDEGAEILAEAlkgnKSLTTLDLSN----NQIGD---EGVIAL------------AEALKNNTTVETLYLSGNQIG 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 243 ---LIRPGS-FQGLTSLRKLWLMHAQVA---------TIERNafddlKSLEELNLSHNNL 289
Cdd:COG5238   278 aegAIALAKaLQGNTTLTSLDLSVNRIGdegaialaeGLQGN-----KTLHTLNLAYNGI 332
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 364-443 1.58e-03

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 38.39  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDL---NVTEGMAAELKCRT-GTSMTSVNWLTpNGT-LMTHGSYRVRisvLHDGTLNFTNVT-VQDTGQYTCM 437
Cdd:cd05848     2 PVFVQEPDDAifpTDSDEKKVILNCEArGNPVPTYRWLR-NGTeIDTESDYRYS---LIDGNLIISNPSeVKDSGRYQCL 77


                  ....*.
gi 1143077087 438 VTNSAG 443
Cdd:cd05848    78 ATNSIG 83
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 366-444 1.60e-03

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 38.85  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 366 IVEPPTDLNVTEGMAAELKCR--TGTSMTSVNWL--TPNGTL---------------MTHGSYRVRISVLHDGTLNFTNV 426
Cdd:cd00099     1 VTQSPRSLSVQEGESVTLSCEvsSSFSSTYIYWYrqKPGQGPefliylssskgktkgGVPGRFSGSRDGTSSFSLTISNL 80

                          90
                  ....*....|....*...
gi 1143077087 427 TVQDTGQYTCMVTNSAGN 444
Cdd:cd00099    81 QPEDSGTYYCAVSESGGT 98
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 253-289 1.60e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.84  E-value: 1.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1143077087 253 TSLRKLWLMHAQVATIErnAFDDLKSLEELNLSHNNL 289
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNK 35
IgV_1_Necl-3 cd07701
First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3; member of the ...
 372-436 2.00e-03

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-3, Necl-3 (also known as cell adhesion molecule 2 (CADM2), SynCAM2, IGSF4D). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region, belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-3 accumulates in central and peripheral nervous system tissue, and has been shown to selectively interact with oligodendrocytes.


Pssm-ID: 409498  Cd Length: 96  Bit Score: 38.15  E-value: 2.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143077087 372 DLNVTEGMAAELKCRTG-TSMTSVNWLTPNGTLMTHGSYRV----RISVL----HDGTLNFTNVTVQDTGQYTC 436
Cdd:cd07701     6 NVTVVEGGTANLTCRVDqNDNTSLQWSNPAQQTLYFDDKKAlrdnRIELVraswHELSISISDVSLSDEGQYTC 79
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 57-85 2.22e-03

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 36.07  E-value: 2.22e-03
                          10        20
                  ....*....|....*....|....*....
gi 1143077087  57 CPVACSCSnqASRVICTRRDLAEVPASIP 85
Cdd:pfam01462   2 CPVPCHCS--ATVVNCSDRGLTAVPRDLP 28
IgC2_CD22_d3 cd20937
Third immunoglobulin domain in Cluster of Differentiation (CD) 22; member of the Constant 2 ...
 370-443 2.27e-03

Third immunoglobulin domain in Cluster of Differentiation (CD) 22; member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain in Cluster of Differentiation (CD) 22 (also known as Siglec-2). CD22, a sialic-acid binding immunoglobulin type-lectin (Siglec) family member, is an inhibitory co-receptor of the B-cell receptor (BCR). The inhibitory function of CD22 and its restricted expression on B cells makes CD22 an attractive target against dysregulated B cells that cause autoimmune diseases and B-cell-derived cancers. CD22 plays a vital role in establishing a baseline level of B-cell inhibition, and thus is an important determinant of homeostasis in humoral immunity. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409531  Cd Length: 88  Bit Score: 37.86  E-value: 2.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143077087 370 PTDLNVTEGMAAELKCRTGTS---MTSVNWLTPNGTLMTHGSYrvrisvlhdgTLNFTNVTVQDTGQYTCMVTNSAG 443
Cdd:cd20937     9 PSDAIVREGDSVTMTCEVSSSnpeYTTVSWLKDGTSLKKQNTF----------TLNLREVTKDQSGKYCCQVSNDVG 75
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 159-200 2.42e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.45  E-value: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1143077087 159 KLRELWLRNNPIESIPsyAFNRVPSLRRLDLGELKRLEYISE 200
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNKITDLSD 41
LRR_8 pfam13855
Leucine rich repeat;
278-311 2.62e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 2.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1143077087 278 SLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHN 311
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN 35
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 277-312 2.67e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.07  E-value: 2.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1143077087 277 KSLEELNLSHNNLMSLPhdLFTPLHRLERVHLNHNP 312
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNN 34
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 364-453 3.37e-03

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 37.53  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 364 PVIVEPPTDLNVTEGMAAELKCR-TGTSMTSVNWLT----PNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMV 438
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDvTGRPQPEITWEKqvpgKENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80

                          90
                  ....*....|....*
gi 1143077087 439 TNSAGNTTASATLNV 453
Cdd:cd05765    81 RNSGGLLRANFPLSV 95
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
157-179 3.42e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 3.42e-03
                           10        20
                   ....*....|....*....|...
gi 1143077087  157 LSKLRELWLRNNPIESIPSYAFN 179
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAFQ 23
LRR smart00370
Leucine-rich repeats, outliers;
157-179 3.42e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 3.42e-03
                           10        20
                   ....*....|....*....|...
gi 1143077087  157 LSKLRELWLRNNPIESIPSYAFN 179
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQ 23
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 394-453 4.44e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 36.80  E-value: 4.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 394 VNWLTPNGTLMTHGSYRVRISVLHdGTLNFTNVTVQDTGQYTCMVTNSAGntTASATLNV 453
Cdd:cd05748    24 VTWSKDGQPLKETGRVQIETTASS-TSLVIKNAKRSDSGKYTLTLKNSAG--EKSATINV 80
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
 383-453 8.38e-03

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 36.22  E-value: 8.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143077087 383 LKCRTGTSMTSVNWLTPNGTLMTHGsyrvRISVLHDG-TLNFTNVTVQDTGQYTCMVTNSAG-NTTASATLNV 453
Cdd:cd05740    20 LTCEPETQNTSYLWWFNGQSLPVTP----RLTLSNGNrTLTLLNVTREDAGAYQCEISNPVSaNRSDPVTLDV 88
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 369-436 8.88e-03

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.


Pssm-ID: 409472  Cd Length: 111  Bit Score: 36.76  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143077087 369 PPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLM-------THG-----SYRVRISVLH------DGTLNFTNVTVQD 430
Cdd:cd05889     7 WDTSVPLSENMSLECVYPSTGILTQVEWTKIGGQKDniavyhpTHGmhirkPYAGRVYFLNstmasnNMSLSFRNASEDD 86


                  ....*.
gi 1143077087 431 TGQYTC 436
Cdd:cd05889    87 VGYYSC 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH