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Conserved domains on  [gi|47777289|ref|NP_034862|]
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leucine-rich repeat neuronal protein 2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-324 4.99e-30

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 123.51  E-value: 4.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  85 DQTELAYLANLTELDLSQNSFSDArDCDFQALPQLLSLHLEENRLNRLEDhSFAGLTSLQELYLNHNQLCRIsPRAFAGL 164
Cdd:COG4886 105 GNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 165 GNLLRLHLNSNLLRTIdSRWFEMLPNLEILMIGGNKVDAiLDMNFRPLANLRSLVLAGMSLREISDyaLEGLQSLESLSF 244
Cdd:COG4886 182 TNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDL 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 245 YDNQLAQVPKraLEQVPGLKFLDLNKNPLQRvgpgdfanmLHLKELGLNNMEELVSIDKFALVNLPELTKLDITNNPRLS 324
Cdd:COG4886 258 SNNQLTDLPP--LANLTNLKTLDLSNNQLTD---------LKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 430-514 2.51e-15

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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPaGVRLtpaRSGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPL---RSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATNSAGEA 82


                  ....*...
gi 47777289   507 TKTVSVVV 514
Cdd:pfam07679  83 EASAELTV 90
LRR_8 pfam13855
Leucine rich repeat;
310-371 1.42e-11

Leucine rich repeat;


:

Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 1.42e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289   310 PELTKLDITNNpRLSFIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVGLHGNPI 371
Cdd:pfam13855   1 PNLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 342-420 1.79e-10

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.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 64.72  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289    342 LNNNALSALHQQTVESLPNLQEVGLHGNPIRCDC----VIRWANATGthVRFIEPQSTLCAEPPDLQRRPVREVPFreMT 417
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCglarLPRWAEEKG--VKVRQPEAALCAGPGALAGQPLLGIPL--LD 77


                   ...
gi 47777289    418 DHC 420
Cdd:TIGR00864   78 SGC 80
LRRNT smart00013
Leucine rich repeat N-terminal domain;
28-72 8.05e-03

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.60  E-value: 8.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 47777289     28 PCPPQCACqirpwytprssyrEATTVDCNDLFLTAVPPRLPAGTQ 72
Cdd:smart00013   1 ACPAPCNC-------------SGTAVDCSGRGLTEVPLDLPPDTT 32
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-324 4.99e-30

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 123.51  E-value: 4.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  85 DQTELAYLANLTELDLSQNSFSDArDCDFQALPQLLSLHLEENRLNRLEDhSFAGLTSLQELYLNHNQLCRIsPRAFAGL 164
Cdd:COG4886 105 GNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 165 GNLLRLHLNSNLLRTIdSRWFEMLPNLEILMIGGNKVDAiLDMNFRPLANLRSLVLAGMSLREISDyaLEGLQSLESLSF 244
Cdd:COG4886 182 TNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDL 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 245 YDNQLAQVPKraLEQVPGLKFLDLNKNPLQRvgpgdfanmLHLKELGLNNMEELVSIDKFALVNLPELTKLDITNNPRLS 324
Cdd:COG4886 258 SNNQLTDLPP--LANLTNLKTLDLSNNQLTD---------LKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-222 8.24e-17

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: 79.83  E-value: 8.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  51 TTVDCNDLFLTAVP-PRLPAGTQTLLLQSNSISRIDQteLAYLANLTELDLSQNSFSdaRDCDFQALPQLLSLHLEENRL 129
Cdd:cd21340   5 THLYLNDKNITKIDnLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIE--KIENLENLVNLKKLYLGGNRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 130 NRLEdhSFAGLTSLQELYLNHNQLCR-----ISPRAFAGLGNLLR-LHLNSNLLRTIDSrwFEMLPNLEILMIGGNKVDA 203
Cdd:cd21340  81 SVVE--GLENLTNLEELHIENQRLPPgekltFDPRSLAALSNSLRvLNISGNNIDSLEP--LAPLRNLEQLDASNNQISD 156

                       170       180
                ....*....|....*....|.
gi 47777289 204 ILDMN--FRPLANLRSLVLAG 222
Cdd:cd21340 157 LEELLdlLSSWPSLRELDLTG 177
I-set pfam07679
Immunoglobulin I-set domain;
430-514 2.51e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPaGVRLtpaRSGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPL---RSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATNSAGEA 82


                  ....*...
gi 47777289   507 TKTVSVVV 514
Cdd:pfam07679  83 EASAELTV 90
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 422-514 3.80e-15

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: 71.35  E-value: 3.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 422 PLISPRSfpSSLQIASGESTVLHCRALAEPEPEIYWVTPAGvRLTPARSgrRYRVFPEGTLELRRVTAEEAGLYTCVAQN 501
Cdd:cd05764   1 PLITRHT--HELRVLEGQRATLRCKARGDPEPAIHWISPEG-KLISNSS--RTLVYDNGTLDILITTVKDTGAFTCIASN 75

                        90
                ....*....|...
gi 47777289 502 LVGADTKTVSVVV 514
Cdd:cd05764  76 PAGEATARVELHI 88
LRR_8 pfam13855
Leucine rich repeat;
117-177 8.92e-15

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 69.09  E-value: 8.92e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47777289   117 PQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQLCRISPRAFAGLGNLLRLHLNSNLL 177
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 430-514 1.71e-13

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: 66.37  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289    430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTParsGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---SGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                   ....*...
gi 47777289    507 TKTVSVVV 514
Cdd:smart00410  78 SSGTTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
310-371 1.42e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 1.42e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289   310 PELTKLDITNNpRLSFIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVGLHGNPI 371
Cdd:pfam13855   1 PNLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 76-369 2.34e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 67.57  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   76 LQSNSISRIDQTELAYLANLTELDLSQNSFSDARDCDFQALPQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQLCR 155
Cdd:PLN00113 219 LGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  156 ISPRAFAGLGNLLRLHLNSNLLRTIDSRWFEMLPNLEILMIGGNKVDA-------------ILDMNFRPLA--------- 213
Cdd:PLN00113 299 EIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGeipknlgkhnnltVLDLSTNNLTgeipeglcs 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  214 --NLRSLVLAGMSLREISDYALEGLQSLESLSFYDNQLAQVPKRALEQVPGLKFLDLNKNPLQRVGPGDFANMLHLKELG 291
Cdd:PLN00113 379 sgNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLS 458

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  292 LnnmeelvSIDKFaLVNLPE------LTKLDITNNpRLSFIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVG 365
Cdd:PLN00113 459 L-------ARNKF-FGGLPDsfgskrLENLDLSRN-QFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLD 529


                 ....
gi 47777289  366 LHGN 369
Cdd:PLN00113 530 LSHN 533
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 342-420 1.79e-10

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: 64.72  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289    342 LNNNALSALHQQTVESLPNLQEVGLHGNPIRCDC----VIRWANATGthVRFIEPQSTLCAEPPDLQRRPVREVPFreMT 417
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCglarLPRWAEEKG--VKVRQPEAALCAGPGALAGQPLLGIPL--LD 77


                   ...
gi 47777289    418 DHC 420
Cdd:TIGR00864   78 SGC 80
LRRCT smart00082
Leucine rich repeat C-terminal domain;
369-412 3.80e-03

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 35.87  E-value: 3.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 47777289    369 NPIRCDCVI----RWANATgthVRFIEPQSTLCAEPPDLqRRPVREVP 412
Cdd:smart00082   1 NPFICDCELrwllRWLQAN---EHLQDPVDLRCASPSSL-RGPLLELL 44
LRRNT smart00013
Leucine rich repeat N-terminal domain;
28-72 8.05e-03

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.60  E-value: 8.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 47777289     28 PCPPQCACqirpwytprssyrEATTVDCNDLFLTAVPPRLPAGTQ 72
Cdd:smart00013   1 ACPAPCNC-------------SGTAVDCSGRGLTEVPLDLPPDTT 32
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-324 4.99e-30

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 123.51  E-value: 4.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  85 DQTELAYLANLTELDLSQNSFSDArDCDFQALPQLLSLHLEENRLNRLEDhSFAGLTSLQELYLNHNQLCRIsPRAFAGL 164
Cdd:COG4886 105 GNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 165 GNLLRLHLNSNLLRTIdSRWFEMLPNLEILMIGGNKVDAiLDMNFRPLANLRSLVLAGMSLREISDyaLEGLQSLESLSF 244
Cdd:COG4886 182 TNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDL 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 245 YDNQLAQVPKraLEQVPGLKFLDLNKNPLQRvgpgdfanmLHLKELGLNNMEELVSIDKFALVNLPELTKLDITNNPRLS 324
Cdd:COG4886 258 SNNQLTDLPP--LANLTNLKTLDLSNNQLTD---------LKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
49-371 1.20e-28

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 119.27  E-value: 1.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  49 EATTVDCNDLFLTAVPPRLPAGTQTLLLQSNSISRIDQTELAYLANLTELDLSQNSFSDARDCDFQALPQLLSLHLEENR 128
Cdd:COG4886  28 LLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 129 lnrledhSFAGLTSLQELYLNHNQLCRIsPRAFAGLGNLLRLHLNSNLLRTIDSrWFEMLPNLEILMIGGNKvdaildmn 208
Cdd:COG4886 108 -------ELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQ-------- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 209 frplanlrslvlagmsLREISDyALEGLQSLESLSFYDNQLAQVPKrALEQVPGLKFLDLNKNPLQRVgPGDFANMLHLK 288
Cdd:COG4886 171 ----------------LTDLPE-ELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDL-PEPLANLTNLE 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 289 ELGL--NNMEELVSidkfaLVNLPELTKLDITNNpRLSFIHPRAfhHLPQMETLMLNNNALSALHQQTVESLPNLQEVGL 366
Cdd:COG4886 232 TLDLsnNQLTDLPE-----LGNLTNLEELDLSNN-QLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLL 303


                ....*
gi 47777289 367 HGNPI 371
Cdd:COG4886 304 LLLLL 308
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-369 1.22e-25

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.41  E-value: 1.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  51 TTVDCNDLFLTAVPPRLPAGT--QTLLLQSNSISRIDqTELAYLANLTELDLSQNSFSDARDcDFQALPQLLSLHLEENR 128
Cdd:COG4886 116 ESLDLSGNQLTDLPEELANLTnlKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQ 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 129 LNRLEDhSFAGLTSLQELYLNHNQLCRIsPRAFAGLGNLLRLHLNSNLLRTIDsrWFEMLPNLEILMIGGNKvdaildmn 208
Cdd:COG4886 194 ITDLPE-PLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQ-------- 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 209 frplanlrslvlagmsLREISDyaLEGLQSLESLSFYDNQLAQVPKRALEQVPGLKFLDLNKNPLQRVGPGDFANMLHLK 288
Cdd:COG4886 262 ----------------LTDLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTL 323

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 289 ELGLNNMEELVSIDKFALVNLPELTKLDITNNPRLS--FIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVGL 366
Cdd:COG4886 324 LLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLslLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403


                ...
gi 47777289 367 HGN 369
Cdd:COG4886 404 TLA 406
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
163-372 2.64e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 2.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 163 GLGNLLRLHLNSNLLRTIDSRWFEMLPNLEILMIGGNKvdaildmNFRPLANLRSLVLAGMSLREISDyALEGLQSLESL 242
Cdd:COG4886  70 SLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKEL 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 243 SFYDNQLAQVPKrALEQVPGLKFLDLNKNPLQRVgPGDFANMLHLKELGL--NNMEELvsidKFALVNLPELTKLDITNN 320
Cdd:COG4886 142 DLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLsnNQITDL----PEPLGNLTNLEELDLSGN 215

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47777289 321 pRLSFIhPRAFHHLPQMETLMLNNNALSALHQqtVESLPNLQEVGLHGNPIR 372
Cdd:COG4886 216 -QLTDL-PEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLT 263
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-222 8.24e-17

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: 79.83  E-value: 8.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  51 TTVDCNDLFLTAVP-PRLPAGTQTLLLQSNSISRIDQteLAYLANLTELDLSQNSFSdaRDCDFQALPQLLSLHLEENRL 129
Cdd:cd21340   5 THLYLNDKNITKIDnLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIE--KIENLENLVNLKKLYLGGNRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 130 NRLEdhSFAGLTSLQELYLNHNQLCR-----ISPRAFAGLGNLLR-LHLNSNLLRTIDSrwFEMLPNLEILMIGGNKVDA 203
Cdd:cd21340  81 SVVE--GLENLTNLEELHIENQRLPPgekltFDPRSLAALSNSLRvLNISGNNIDSLEP--LAPLRNLEQLDASNNQISD 156

                       170       180
                ....*....|....*....|.
gi 47777289 204 ILDMN--FRPLANLRSLVLAG 222
Cdd:cd21340 157 LEELLdlLSSWPSLRELDLTG 177
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 122-371 3.03e-16

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: 78.29  E-value: 3.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 122 LHLEENRLNRLEDHSFagLTSLQELYLNHNQLCRIspRAFAGLGNLLRLHLNSNLLRTIDSrwFEMLPNLEILMIGGNKv 201
Cdd:cd21340   7 LYLNDKNITKIDNLSL--CKNLKVLYLYDNKITKI--ENLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 202 daildmnfrplanlrslvlagmslreISdyALEGLQSLESLsfydnqlaqvpkraleqvpglKFLDLNKnplQRVGPGdf 281
Cdd:cd21340  80 --------------------------IS--VVEGLENLTNL---------------------EELHIEN---QRLPPG-- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 282 anmlhlkelglnnmeELVSIDKFALVNL-PELTKLDITNNpRLSFIHPraFHHLPQMETLMLNNNALSALHQ--QTVESL 358
Cdd:cd21340 106 ---------------EKLTFDPRSLAALsNSLRVLNISGN-NIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSW 167

                       250
                ....*....|...
gi 47777289 359 PNLQEVGLHGNPI 371
Cdd:cd21340 168 PSLRELDLTGNPV 180
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 92-275 9.40e-16

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: 76.75  E-value: 9.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  92 LANLTELDLSQNSFSDarDCDFQALPQLLSLHLEENRLNRLEDhsFAGLTSLQELYLNHNQLCRISPraFAGLGNLLRLH 171
Cdd:cd21340   1 LKRITHLYLNDKNITK--IDNLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 172 LNSNLLRTIDSrwFEMLPNLEILMIGGNKVDAILDMNFRP-----LAN-LRSLVLAGMSLREISDyaLEGLQSLESLSFY 245
Cdd:cd21340  75 LGGNRISVVEG--LENLTNLEELHIENQRLPPGEKLTFDPrslaaLSNsLRVLNISGNNIDSLEP--LAPLRNLEQLDAS 150

                       170       180       190
                ....*....|....*....|....*....|..
gi 47777289 246 DNQLAQVP--KRALEQVPGLKFLDLNKNPLQR 275
Cdd:cd21340 151 NNQISDLEelLDLLSSWPSLRELDLTGNPVCK 182
I-set pfam07679
Immunoglobulin I-set domain;
430-514 2.51e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPaGVRLtpaRSGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPL---RSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATNSAGEA 82


                  ....*...
gi 47777289   507 TKTVSVVV 514
Cdd:pfam07679  83 EASAELTV 90
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 74-267 3.20e-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: 75.21  E-value: 3.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  74 LLLQSNSISRIDqtELAYLANLTELDLSQNSFSdaRDCDFQALPQLLSLHLEENRLNRLEDhsFAGLTSLQELYLNHNQL 153
Cdd:cd21340   7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKIT--KIENLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 154 CRISprafaGLGNL--LR-LHLNSNLL----------RTIDSrwfeMLPNLEILMIGGNKVDAILDmnFRPLANLRSLVL 220
Cdd:cd21340  81 SVVE-----GLENLtnLEeLHIENQRLppgekltfdpRSLAA----LSNSLRVLNISGNNIDSLEP--LAPLRNLEQLDA 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47777289 221 AGMSLREISD--YALEGLQSLESLSFYDNQLAQVPK---RALEQVPGLKFLD 267
Cdd:cd21340 150 SNNQISDLEEllDLLSSWPSLRELDLTGNPVCKKPKyrdKIILASKSLEVLD 201
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 422-514 3.80e-15

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: 71.35  E-value: 3.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 422 PLISPRSfpSSLQIASGESTVLHCRALAEPEPEIYWVTPAGvRLTPARSgrRYRVFPEGTLELRRVTAEEAGLYTCVAQN 501
Cdd:cd05764   1 PLITRHT--HELRVLEGQRATLRCKARGDPEPAIHWISPEG-KLISNSS--RTLVYDNGTLDILITTVKDTGAFTCIASN 75

                        90
                ....*....|...
gi 47777289 502 LVGADTKTVSVVV 514
Cdd:cd05764  76 PAGEATARVELHI 88
LRR_8 pfam13855
Leucine rich repeat;
117-177 8.92e-15

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 69.09  E-value: 8.92e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47777289   117 PQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQLCRISPRAFAGLGNLLRLHLNSNLL 177
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 430-514 1.80e-14

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: 68.96  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVrlTPARsgrRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADTKT 509
Cdd:cd05725   4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGE--LPKG---RYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEAS 78


                ....*
gi 47777289 510 VSVVV 514
Cdd:cd05725  79 ATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 422-501 5.79e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.59  E-value: 5.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   422 PLISprSFPSSLQIASGESTVLHCRALAEPEPEIYWvTPAGVRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQN 501
Cdd:pfam13927   2 PVIT--VSPSSVTVREGETVTLTCEATGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 437-514 8.34e-14

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: 67.41  E-value: 8.34e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47777289 437 SGESTVLHCRALAEPEPEIYWVTPaGVRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd20969  16 EGHTVQFVCRADGDPPPAILWLSP-RKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 430-514 1.71e-13

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: 66.37  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289    430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTParsGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---SGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                   ....*...
gi 47777289    507 TKTVSVVV 514
Cdd:smart00410  78 SSGTTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
94-153 3.08e-13

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 64.85  E-value: 3.08e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289    94 NLTELDLSQNSFSDARDCDFQALPQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQL 153
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
141-201 7.23e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.00  E-value: 7.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47777289   141 TSLQELYLNHNQLCRISPRAFAGLGNLLRLHLNSNLLRTIDSRWFEMLPNLEILMIGGNKV 201
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
310-371 1.42e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 1.42e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289   310 PELTKLDITNNpRLSFIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVGLHGNPI 371
Cdd:pfam13855   1 PNLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 76-369 2.34e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 67.57  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   76 LQSNSISRIDQTELAYLANLTELDLSQNSFSDARDCDFQALPQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQLCR 155
Cdd:PLN00113 219 LGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  156 ISPRAFAGLGNLLRLHLNSNLLRTIDSRWFEMLPNLEILMIGGNKVDA-------------ILDMNFRPLA--------- 213
Cdd:PLN00113 299 EIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGeipknlgkhnnltVLDLSTNNLTgeipeglcs 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  214 --NLRSLVLAGMSLREISDYALEGLQSLESLSFYDNQLAQVPKRALEQVPGLKFLDLNKNPLQRVGPGDFANMLHLKELG 291
Cdd:PLN00113 379 sgNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLS 458

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  292 LnnmeelvSIDKFaLVNLPE------LTKLDITNNpRLSFIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVG 365
Cdd:PLN00113 459 L-------ARNKF-FGGLPDsfgskrLENLDLSRN-QFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLD 529


                 ....
gi 47777289  366 LHGN 369
Cdd:PLN00113 530 LSHN 533
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 430-514 5.37e-11

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: 59.74  E-value: 5.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLTPARSGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:cd20951   7 LQSHTVWEKSDAKLRVEVQGKPDPEVKWYK-NGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAKNIHGEA 85


                ....*...
gi 47777289 507 TKTVSVVV 514
Cdd:cd20951  86 SSSASVVV 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 442-510 6.42e-11

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: 58.49  E-value: 6.42e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 442 VLHCRALAEPEPEIYWVTPaGVRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLV-GADTKTV 510
Cdd:cd00096   2 TLTCSASGNPPPTITWYKN-GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 342-420 1.79e-10

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: 64.72  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289    342 LNNNALSALHQQTVESLPNLQEVGLHGNPIRCDC----VIRWANATGthVRFIEPQSTLCAEPPDLQRRPVREVPFreMT 417
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCglarLPRWAEEKG--VKVRQPEAALCAGPGALAGQPLLGIPL--LD 77


                   ...
gi 47777289    418 DHC 420
Cdd:TIGR00864   78 SGC 80
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 422-514 7.35e-10

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: 56.36  E-value: 7.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 422 PLISPRSFPSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTPArsgRRYRVFPEGT-LELRRVTAEEAGLYTCVAQ 500
Cdd:cd20970   1 PVISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN---TRYIVRENGTtLTIRNIRRSDMGIYLCIAS 77

                        90
                ....*....|....*
gi 47777289 501 NLV-GADTKTVSVVV 514
Cdd:cd20970  78 NGVpGSVEKRITLQV 92
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 62-288 6.00e-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: 58.14  E-value: 6.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  62 AVPPRLPA--GTQTLLLQSNSISRID---QTELAYL---ANLTELDLSQNSFSDARDCDFQALPQLLSL---HLEENRL- 129
Cdd:cd00116  42 ALASALRPqpSLKELCLSLNETGRIPrglQSLLQGLtkgCGLQELDLSDNALGPDGCGVLESLLRSSSLqelKLNNNGLg 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 130 NRLEDHSFAGLTSLQ----ELYLNHNQLCRISPRAFAGL----GNLLRLHLNSNLLR----TIDSRWFEMLPNLEILMIG 197
Cdd:cd00116 122 DRGLRLLAKGLKDLPpaleKLVLGRNRLEGASCEALAKAlranRDLKELNLANNGIGdagiRALAEGLKANCNLEVLDLN 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 198 GNKV----DAILDMNFRPLANLRSLVLAGMSLR-----EISDYALEGLQSLESLSFYDNQL----AQVPKRALEQVPGLK 264
Cdd:cd00116 202 NNGLtdegASALAETLASLKSLEVLNLGDNNLTdagaaALASALLSPNISLLTLSLSCNDItddgAKDLAEVLAEKESLL 281

                       250       260
                ....*....|....*....|....
gi 47777289 265 FLDLNKNPLQRVGPGDFANMLHLK 288
Cdd:cd00116 282 ELDLRGNKFGEEGAQLLAESLLEP 305
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 430-514 6.03e-09

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: 53.40  E-value: 6.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVrltpARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVG-ADTK 508
Cdd:cd20968   6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDL----IKENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGiAYSK 81


                ....*.
gi 47777289 509 TVSVVV 514
Cdd:cd20968  82 PVTIEV 87
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 427-505 7.73e-09

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: 53.17  E-value: 7.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 427 RSFPSSLQIASGESTVLHCRA-LAEPEPEIYWVTPaGVRLtpARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGA 505
Cdd:cd05724   1 RVEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKD-GQPL--NLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGE 77
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 437-514 7.88e-09

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: 53.34  E-value: 7.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 437 SGESTVLHCRALAEPEPEIYWvTPAGVRLTparSGRRYRVFPEGTLELRRVT-AEEAGLYTCVAQNLVG-ADTKTVSVVV 514
Cdd:cd20958  14 AGQTLRLHCPVAGYPISSITW-EKDGRRLP---LNHRQRVFPNGTLVIENVQrSSDEGEYTCTARNQQGqSASRSVFVKV 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 427-514 9.15e-09

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: 52.88  E-value: 9.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 427 RSFPSSLQIASGESTVLHCRALAEPEPEIYWvTPAGVRLtpARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGad 506
Cdd:cd20952   3 LQGPQNQTVAVGGTVVLNCQATGEPVPTISW-LKDGVPL--LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSG-- 77


                ....*...
gi 47777289 507 TKTVSVVV 514
Cdd:cd20952  78 EATWSAVL 85
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 56-359 9.43e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 59.09  E-value: 9.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   56 NDLFLTAVPPRLPAGTQTLLLQSNSISRIDQTELAYLANLTELDLSQNSFSDARDCDFQALPQLLSLHLEENRLNRLEDH 135
Cdd:PLN00113 127 NNNFTGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPR 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  136 SFAGLTSLQELYLNHNQLCRISPRAFAGLGNLLRLHL-NSNLLRTIDSRwFEMLPNLEILMIGGNKVDAILDMNFRPLAN 214
Cdd:PLN00113 207 ELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLvYNNLTGPIPSS-LGNLKNLQYLFLYQNKLSGPIPPSIFSLQK 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  215 LRSLVLAGMSLR-EISDYALEgLQSLESLSFYDNQLAQVPKRALEQVPGLKFLDLNKNPLQRVGPGDFA--NMLHLKELG 291
Cdd:PLN00113 286 LISLDLSDNSLSgEIPELVIQ-LQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGkhNNLTVLDLS 364

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47777289  292 LNNMEELVSIdkfALVNLPELTKLDITNNPRLSFIhPRAFHHLPQMETLMLNNNALSALHQQTVESLP 359
Cdd:PLN00113 365 TNNLTGEIPE---GLCSSGNLFKLILFSNSLEGEI-PKSLGACRSLRRVRLQDNSFSGELPSEFTKLP 428
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 429-507 9.61e-09

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 52.93  E-value: 9.61e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47777289 429 FPSSLQIASGESTVLHCRALAEPEPEIYWVtpagvRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADT 507
Cdd:cd04968   7 FPADTYALKGQTVTLECFALGNPVPQIKWR-----KVDGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKDT 80
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 430-504 1.20e-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: 52.62  E-value: 1.20e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTPARSgRRYRVFPE-GTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05763   6 PHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARE-RRMHVMPEdDVFFIVDVKIEDTGVYSCTAQNSAG 80
LRR_8 pfam13855
Leucine rich repeat;
286-347 1.66e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 51.37  E-value: 1.66e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289   286 HLKELGLNNmEELVSIDKFALVNLPELTKLDITNNpRLSFIHPRAFHHLPQMETLMLNNNAL 347
Cdd:pfam13855   2 NLRSLDLSN-NRLTSLDDGAFKGLSNLKVLDLSNN-LLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 428-514 5.46e-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: 51.10  E-value: 5.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 428 SFPSSLQIASGESTVLHCRALAEPEPEIYWVTPAgvrlTP-ARSGRRYRVFPE-GTLELRRVTAEEAGLYTCVAQNLVGA 505
Cdd:cd20976   6 SVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNA----QPlQYAADRSTCEAGvGELHIQDVLPEDHGTYTCLAKNAAGQ 81


                ....*....
gi 47777289 506 DTKTVSVVV 514
Cdd:cd20976  82 VSCSAWVTV 90
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 443-504 8.41e-08

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth 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: 143223  Cd Length: 69  Bit Score: 49.87  E-value: 8.41e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289 443 LHCRALAEPEPEIYWvTPAGVRLTpaRSGRrYRVFPEGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05746   3 IPCSAQGDPEPTITW-NKDGVQVT--ESGK-FHISPEGYLAIRDVGVADQGRYECVARNTIG 60
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 438-514 1.44e-07

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: 49.70  E-value: 1.44e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47777289 438 GESTVLHCRALAEPEPEIYWvTPAGVRLTpARSGRryRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd20978  16 GQDVTLPCQVTGVPQPKITW-LHNGKPLQ-GPMER--ATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 427-514 1.61e-07

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: 49.57  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 427 RSFPSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLTPARSgRRYRVFPEGT-LELRRVTAEEAGLYTCVAQNLVGA 505
Cdd:cd05736   4 RVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLK-NGMDINPKLS-KQLTLIANGSeLHISNVRYEDTGAYTCIAKNEGGV 81


                ....*....
gi 47777289 506 DTKTVSVVV 514
Cdd:cd05736  82 DEDISSLFV 90
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 431-514 1.69e-07

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: 49.14  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 431 SSLQIASGESTVLHCRALAEPEPEIYWVTPAGVrLTPARSGRRYRvfpEGTLELRRVTAEEAGLYTCVAQNLVGADTKTV 510
Cdd:cd05876   3 SSLVALRGQSLVLECIAEGLPTPTVKWLRPSGP-LPPDRVKYQNH---NKTLQLLNVGESDDGEYVCLAENSLGSARHAY 78


                ....
gi 47777289 511 SVVV 514
Cdd:cd05876  79 YVTV 82
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 65-294 1.92e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 54.85  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   65 PRLpagtQTLLLQSNSISRIDQTELAYLANLTELDLSQNSFSDARDCDFQALPQLLSLHLEENRLNRLEDHSFAGLTSLQ 144
Cdd:PLN00113 332 PRL----QVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLR 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  145 ELYLNHNQLCRISPRAFAGLGNLLRLHL-NSNLLRTIDSRWFEM----------------LP------NLEILMIGGNKV 201
Cdd:PLN00113 408 RVRLQDNSFSGELPSEFTKLPLVYFLDIsNNNLQGRINSRKWDMpslqmlslarnkffggLPdsfgskRLENLDLSRNQF 487

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  202 DAILDMNFRPLANLRSLVLAGMSLR-EISDyALEGLQSLESLSFYDNQLA-QVPKrALEQVPGLKFLDLNKNPLQRVGPG 279
Cdd:PLN00113 488 SGAVPRKLGSLSELMQLKLSENKLSgEIPD-ELSSCKKLVSLDLSHNQLSgQIPA-SFSEMPVLSQLDLSQNQLSGEIPK 565

                        250
                 ....*....|....*
gi 47777289  280 DFANMLHLKELGLNN 294
Cdd:PLN00113 566 NLGNVESLVQVNISH 580
LRR_8 pfam13855
Leucine rich repeat;
166-222 2.22e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.29  E-value: 2.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 47777289   166 NLLRLHLNSNLLRTIDSRWFEMLPNLEILMIGGNKVDAILDMNFRPLANLRSLVLAG 222
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSG 58
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 430-512 4.71e-07

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: 47.96  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   430 PSSLQIASGESTVLHCRA-LAEPEPEIYWVTPAGVRLTPARSG---RRYRVFpegTLELRRVTAEEAGLYTCVAQNLVGA 505
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKhdnGRTTQS---SLLISNVTKEDAGTYTCVVNNPGGS 79


                  ....*..
gi 47777289   506 DTKTVSV 512
Cdd:pfam00047  80 ATLSTSL 86
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 421-514 4.80e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM 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-non-NCAM), 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 Ig1, Ig2, and Ig3. 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.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.39  E-value: 4.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 421 LPLISPRSFPSSLQIASGESTVLHCRALAEPEPEIYWVTPAgvrlTPARSGRRYRVFPEGTLEL--RRVTAEEAGLYTCV 498
Cdd:cd05730   1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDG----EPIESGEEKYSFNEDGSEMtiLDVDKLDEAEYTCI 76

                        90
                ....*....|....*.
gi 47777289 499 AQNLVGADTKTVSVVV 514
Cdd:cd05730  77 AENKAGEQEAEIHLKV 92
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 438-506 4.82e-07

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 48.26  E-value: 4.82e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47777289 438 GESTVLHCRALAEPEPEIYWVTPAG----VRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:cd05734  16 GKAVVLNCSADGYPPPTIVWKHSKGsgvpQFQHIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCKVSNDVGAD 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
187-372 5.72e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 5.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 187 MLPNLEILMIGGNKVDAILDMNFRPLANLRSLVLAGMSLREISDYALEGLQSLESLSFYDNQLAQVPKRALEQVPGLKFL 266
Cdd:COG4886   1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 267 DLNKNPLqrvGPGDFANMLHLKELGLNNMEELVsidkfalvNLPELTKLDITNNpRLSFIhPRAFHHLPQMETLMLNNNA 346
Cdd:COG4886  81 LLSLLLL---GLTDLGDLTNLTELDLSGNEELS--------NLTNLESLDLSGN-QLTDL-PEELANLTNLKELDLSNNQ 147

                       170       180
                ....*....|....*....|....*.
gi 47777289 347 LSALHQQtVESLPNLQEVGLHGNPIR 372
Cdd:COG4886 148 LTDLPEP-LGNLTNLKSLDLSNNQLT 172
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 438-514 5.78e-07

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: 47.63  E-value: 5.78e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47777289 438 GESTVLHCRALAEPEPEIYWvTPAGVRLTparSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAW-TKGGSQLS---VDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 430-514 6.23e-07

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: 48.08  E-value: 6.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVrlTPA-----RSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd20954   8 PVDANVAAGQDVMLHCQADGFPTPTVTWKKATGS--TPGeykdlLYDPNVRILPNGTLVFGHVQKENEGHYLCEAKNGIG 85

                        90
                ....*....|
gi 47777289 505 ADtktVSVVV 514
Cdd:cd20954  86 SG---LSKVI 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 438-514 9.36e-07

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: 47.55  E-value: 9.36e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47777289 438 GESTVLHCRALAEPEPEIYWVTPaGVRLTPARSGRRYRvfPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd05856  19 GSSVRLKCVASGNPRPDITWLKD-NKPLTPPEIGENKK--KKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
LRR_8 pfam13855
Leucine rich repeat;
214-273 1.01e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.36  E-value: 1.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   214 NLRSLVLAGMSLREISDYALEGLQSLESLSFYDNQLAQVPKRALEQVPGLKFLDLNKNPL 273
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 431-514 1.14e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; 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 and 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, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 47.02  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 431 SSLQIASGESTVLHCRALAEPEPEIYWVtPAGVRLTPARSGrrYRVFPEgTLELRRVTAEEAGLYTCVAQNLVGADTKTV 510
Cdd:cd05731   3 SSTMVLRGGVLLLECIAEGLPTPDIRWI-KLGGELPKGRTK--FENFNK-TLKIENVSEADSGEYQCTASNTMGSARHTI 78


                ....
gi 47777289 511 SVVV 514
Cdd:cd05731  79 SVTV 82
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 430-514 1.18e-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: 47.25  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEpEIYWVTPAGVRLTPaRSGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNlvGAD 506
Cdd:cd04977   7 PSYAEISVGESKFFLCKVSGDAK-NINWVSPNGEKVLT-KHGNLKVVNHGSvlsSLTIYNANINDAGIYKCVATN--GKG 82


                ....*...
gi 47777289 507 TKTVSVVV 514
Cdd:cd04977  83 TESEATVK 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 430-504 1.69e-06

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: 46.56  E-value: 1.69e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTPARSGRRYRVFPEGtLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd20949   6 AYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADG-LLINKVTQDDTGEYTCRAYQVNS 79
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 436-514 1.91e-06

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: 46.30  E-value: 1.91e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47777289 436 ASGESTVLHCRALAEPEPEIYWVTPAGVrltpARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd04969  15 AKGGDVIIECKPKASPKPTISWSKGTEL----LTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 430-518 3.70e-06

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: 46.00  E-value: 3.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWV-TPAGVRLTPARSG----RRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd04970   9 PSNADITVGENATLQCHASHDPTLDLTFTwSFNGVPIDLEKIEghyrRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVD 88

                        90
                ....*....|....
gi 47777289 505 ADTKTVSVVVGHAP 518
Cdd:cd04970  89 SDSASATLVVRGPP 102
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 430-504 4.48e-06

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: 45.62  E-value: 4.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVT---PAGVRLTPARSGRryRVFPEGTLELRRV-----TAEEAGLYTCVAQN 501
Cdd:cd07693   7 PSDLIVSKGDPATLNCKAEGRPTPTIQWLKngqPLETDKDDPRSHR--IVLPSGSLFFLRVvhgrkGRSDEGVYVCVAHN 84


                ...
gi 47777289 502 LVG 504
Cdd:cd07693  85 SLG 87
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 430-504 6.77e-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: 45.04  E-value: 6.77e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTPAR---SGRRYRvfpeGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05747  10 PRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRhqiTSTEYK----STFEISKVQMSDEGNYTVVVENSEG 83
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 430-512 9.99e-06

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: 44.65  E-value: 9.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPE-PEIYWVTPAGVRLTPARsgRRYRVFPE----GTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05865   7 PSQGEISVGESKFFLCQVAGEAKdKDISWFSPNGEKLTPNQ--QRISVVRNddysSTLTIYNANIDDAGIYKCVVSNEDE 84


                ....*....
gi 47777289 505 ADTK-TVSV 512
Cdd:cd05865  85 GESEaTVNV 93
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 430-504 1.04e-05

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: 44.36  E-value: 1.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLTPARSGRRYRVFPeGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd04978   6 PPSLVLSPGETGELICEAEGNPQPTITWRL-NGVPIEPAPEDMRRTVDG-RTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 437-514 1.39e-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: 44.13  E-value: 1.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47777289 437 SGESTVLHCRALAEPEPEIYWVTPaGVRLTPARSGRRYRVFPEG-TLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd05729  18 AANKVRLECGAGGNPMPNITWLKD-GKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the ...
 431-514 1.41e-05

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; 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-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. 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: 409452  Cd Length: 93  Bit Score: 44.27  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 431 SSLQIASGESTVLHCRALAEPEpEIYWVTPAGVRLTparSGRRYRVFPEGT---LELRRVTAEEAGLYTCVAQNLVGaDT 507
Cdd:cd05866   8 SKVELSVGESKFFTCTAIGEPE-SIDWYNPQGEKIV---SSQRVVVQKEGVrsrLTIYNANIEDAGIYRCQATDAKG-QT 82


                ....*..
gi 47777289 508 KTVSVVV 514
Cdd:cd05866  83 QEATVVL 89
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 214-372 1.90e-05

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: 47.35  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 214 NLRSLVLAGMSLREISDyALEGLQSLESLSFYDNQLAQVPK------RALEQVPGLKFLDLNKNPLQRVGPGDFANMLH- 286
Cdd:cd00116  29 RLEGNTLGEEAAKALAS-ALRPQPSLKELCLSLNETGRIPRglqsllQGLTKGCGLQELDLSDNALGPDGCGVLESLLRs 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 287 --LKELGLNNMEELVSIDKF---ALVNLPE-LTKLDITNNpRLS----------FIHPRAFH------------------ 332
Cdd:cd00116 108 ssLQELKLNNNGLGDRGLRLlakGLKDLPPaLEKLVLGRN-RLEgascealakaLRANRDLKelnlanngigdagirala 186

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 47777289 333 ----HLPQMETLMLNNNAL-----SALhQQTVESLPNLQEVGLHGNPIR 372
Cdd:cd00116 187 eglkANCNLEVLDLNNNGLtdegaSAL-AETLASLKSLEVLNLGDNNLT 234
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 430-501 2.22e-05

First 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 first 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: 409387  Cd Length: 97  Bit Score: 43.62  E-value: 2.22e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWvTPAGVRLTPArSGRRYRVFPEGTL-----ELRRVTAEEAGLYTCVAQN 501
Cdd:cd05722   8 PSDIVAMRGGPVVLNCSAESDPPPKIEW-KKDGVLLNLV-SDERRQQLPNGSLlitsvVHSKHNKPDEGFYQCVAQN 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 430-514 2.34e-05

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: 43.64  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYW------VTP-AGVRLTPARSGRRyrvfpegTLELRRVTAEEAGLYTCVAQNL 502
Cdd:cd05744   7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWqlngkpVRPdSAHKMLVRENGRH-------SLIIEPVTKRDAGIYTCIARNR 79

                        90
                ....*....|..
gi 47777289 503 VGADTKTVSVVV 514
Cdd:cd05744  80 AGENSFNAELVV 91
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 436-514 2.43e-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: 43.45  E-value: 2.43e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47777289 436 ASGESTVLHCRALAEPEPEIYWvtPAGVRLTParSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVV 514
Cdd:cd05852  15 AKGGRVIIECKPKAAPKPKFSW--SKGTELLV--NNSRISIWDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 429-504 4.64e-05

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: 43.02  E-value: 4.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 429 FPSSLQIASGESTVLHCRALAEPEPEIYW---VTPAGVRLTParSGRRY-RVFPEG----------TLELRRVTAEEAGL 494
Cdd:cd05858   7 LPANTSVVVGTDAEFVCKVYSDAQPHIQWlkhVEKNGSKYGP--DGLPYvEVLKTAgvnttdkeieVLYLRNVTFEDAGE 84

                        90
                ....*....|
gi 47777289 495 YTCVAQNLVG 504
Cdd:cd05858  85 YTCLAGNSIG 94
LRR_8 pfam13855
Leucine rich repeat;
189-249 5.85e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 5.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47777289   189 PNLEILMIGGNKVDAILDMNFRPLANLRSLVLAGMSLREISDYALEGLQSLESLSFYDNQL 249
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 430-514 8.90e-05

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). 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 all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 41.80  E-value: 8.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRaLAEPEPEIYWVTPaGVRLTPARsgrRYRVFPEgTLELRRVTAEEAGLYTCVAQNLVGADTKT 509
Cdd:cd04973  16 VESYSAHPGDLLQLRCR-LRDDVQSINWTKD-GVQLGENN---RTRITGE-EVQIKDAVPRDSGLYACVTSSPSGSDTTY 89


                ....*
gi 47777289 510 VSVVV 514
Cdd:cd04973  90 FSVNV 94
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 430-505 1.10e-04

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: 41.87  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRL----TPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGA 505
Cdd:cd05726   6 PRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLlfpyQPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAGS 85
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 430-514 1.13e-04

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. 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. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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: 409540  Cd Length: 76  Bit Score: 40.94  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLTPARSgrryrvfpegtLELRRVTAEEAGLYTCVAQNLVGA-DTK 508
Cdd:cd20948   2 PSDTYYLSGENLNLSCHAASNPPAQYSWTI-NGTFQTSSQE-----------LFLPAITENNEGTYTCSAHNSLTGkNIS 69


                ....*.
gi 47777289 509 TVSVVV 514
Cdd:cd20948  70 LVLSVT 75
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 424-514 1.18e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 409404  Cd Length: 102  Bit Score: 41.76  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 424 ISPRSFPSSLQIasGESTVLHCRALAEPEP--EIYWVTPAGVRLTPARSGRRYRV-FPEG-----TLELRRVTAEEAGLY 495
Cdd:cd05742   5 LSPNAEPTVLPQ--GETLVLNCTANVNLNEvvDFQWTYPSEKEGKLALLKPDIKVdWSEPgefvsTLTIPEATLKDSGTY 82

                        90
                ....*....|....*....
gi 47777289 496 TCVAQNLVGADTKTVSVVV 514
Cdd:cd05742  83 TCAARSGVMKKEKQTSVSV 101
LRR_9 pfam14580
Leucine-rich repeat;
236-340 1.35e-04

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 43.21  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   236 LQSLESLSFYDNQLaqvpkRALEQVP---GLKFLDLNKNPLQRVGPGDFANMLHLKELGL--NNMEELVSIDkfALVNLP 310
Cdd:pfam14580  41 LDQFDTIDFSDNEI-----RKLDGFPllrRLKTLLLNNNRICRIGEGLGEALPNLTELILtnNNLQELGDLD--PLASLK 113

                          90       100       110
                  ....*....|....*....|....*....|..
gi 47777289   311 ELTKLDITNNPRLSFIHPRAF--HHLPQMETL 340
Cdd:pfam14580 114 KLTFLSLLRNPVTNKPHYRLYviYKVPQLRLL 145
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 438-514 1.69e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 40.78  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 438 GESTVLHCRALAEPEPEIYW-----VTPAGVRLTpaRSGRRYRVFpegtlelrRVTAEEAGLYTCVAQNLVGADTKTVSV 512
Cdd:cd05851  16 GQNVTLECFALGNPVPVIRWrkilePMPATAEIS--MSGAVLKIF--------NIQPEDEGTYECEAENIKGKDKHQARV 85


                ..
gi 47777289 513 VV 514
Cdd:cd05851  86 YV 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 430-514 2.53e-04

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: 40.64  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLtpaRSGRRYRVFPEG---TLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:cd20972   8 LRSQEVAEGSKVRLECRVTGNPTPVVRWFC-EGKEL---QNSPDIQIHQEGdlhSLIIAEAFEEDTGRYSCLATNSVGSD 83


                ....*...
gi 47777289 507 TKTVSVVV 514
Cdd:cd20972  84 TTSAEIFV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 430-514 3.46e-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: 40.08  E-value: 3.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPAgvrlTPAR--SGRRYRVFPEG--TLELRRVTAEEAGLYTCVAQNLVGA 505
Cdd:cd20990   7 PGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDG----KPIRpdSAHKMLVRENGvhSLIIEPVTSRDAGIYTCIATNRAGQ 82


                ....*....
gi 47777289 506 DTKTVSVVV 514
Cdd:cd20990  83 NSFNLELVV 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 427-514 4.12e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 39.88  E-value: 4.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 427 RSFPSSLQIASGESTVLHCRALAEPEPEIYWVTPAGVRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVGAD 506
Cdd:cd05737   5 GGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSE 84


                ....*...
gi 47777289 507 TKTVSVVV 514
Cdd:cd05737  85 TSDVTVSV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 433-514 4.48e-04

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: 39.87  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 433 LQIASGESTVLHCRALAEPEPEIYWVTPAgvrlTPARSGRRYRVFPEG----TLELRRVTAEEAGLYTCVAQNLVGADTK 508
Cdd:cd20973   7 KEVVEGSAARFDCKVEGYPDPEVKWMKDD----NPIVESRRFQIDQDEdglcSLIISDVCGDDSGKYTCKAVNSLGEATC 82


                ....*.
gi 47777289 509 TVSVVV 514
Cdd:cd20973  83 SAELTV 88
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
 430-518 4.67e-04

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. 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. 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-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 40.03  E-value: 4.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWV-TPAGVRLTPARSGRRYRVF--PEGTLELRRVTAE--EAGLYTCVAQNLVG 504
Cdd:cd05854   9 PSSADINQGENLTLQCHASHDPTMDLTFTwSLDDFPIDLDKPNGHYRRMevKETIGDLVIVNAQlsHAGTYTCTAQTVVD 88

                        90
                ....*....|....
gi 47777289 505 ADTKTVSVVVGHAP 518
Cdd:cd05854  89 SASASATLVVRGPP 102
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 430-509 4.73e-04

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: 39.75  E-value: 4.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYW--------VTPAGVRLTPARSGRRyrvfpegTLELRRVTAEEAGLYTCVAQN 501
Cdd:cd05892   7 PQNKKVLEGDPVRLECQISAIPPPQIFWkknnemlqYNTDRISLYQDNCGRI-------CLLIQNANKKDAGWYTVSAVN 79


                ....*...
gi 47777289 502 LVGADTKT 509
Cdd:cd05892  80 EAGVVSCN 87
LRR_9 pfam14580
Leucine-rich repeat;
116-274 5.17e-04

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 41.67  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   116 LPQLLSLHLEENRLNRLEdhSFAGLTSLQELYLNHNQLCRISPrafaGLGnllrlhlnsnllrtidsrwfEMLPNLEILM 195
Cdd:pfam14580  41 LDQFDTIDFSDNEIRKLD--GFPLLRRLKTLLLNNNRICRIGE----GLG--------------------EALPNLTELI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   196 IGGNKVDAILDMNfrPLAnlrslvlagmslreisdyaleGLQSLESLSFYDNQLAQVPK---RALEQVPGLKFLDLNKNP 272
Cdd:pfam14580  95 LTNNNLQELGDLD--PLA---------------------SLKKLTFLSLLRNPVTNKPHyrlYVIYKVPQLRLLDFRKVK 151


                  ..
gi 47777289   273 LQ 274
Cdd:pfam14580 152 QK 153
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 430-504 6.20e-04

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: 39.19  E-value: 6.20e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTPA-GVRLTPARSGRRYrvfpEG-TLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05868   6 PTNLVLSPGEDGTLICRANGNPKPSISWLTNGvPIEIAPTDPSRKV----DGdTIIFSKVQERSSAVYQCNASNEYG 78
LRR_8 pfam13855
Leucine rich repeat;
237-294 7.04e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.27  E-value: 7.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 47777289   237 QSLESLSFYDNQLAQVPKRALEQVPGLKFLDLNKNPLQRVGPGDFANMLHLKELGLNN 294
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSG 58
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 422-504 7.04e-04

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: 39.45  E-value: 7.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 422 PLISPRSFPSSLQIasGESTVLHCRALAEPEPEIYWVTPA----GVRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTC 497
Cdd:cd05765   1 PALVNSPTHQTVKV--GETASFHCDVTGRPQPEITWEKQVpgkeNLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTC 78


                ....*..
gi 47777289 498 VAQNLVG 504
Cdd:cd05765  79 TARNSGG 85
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 440-504 7.15e-04

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 39.22  E-value: 7.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47777289 440 STVLHCRALAEPEPEIYWVTPAgVRLTPARSGRRYRVFPEGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05738  16 TATMLCAASGNPDPEISWFKDF-LPVDTATSNGRIKQLRSGALQIENSEESDQGKYECVATNSAG 79
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 421-504 9.88e-04

Sixth 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 sixth 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: 409551  Cd Length: 94  Bit Score: 39.01  E-value: 9.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 421 LPLISPRSFPSSLQiASGESTVLHCRALAEPEP-EIYWVT-----PAGVRLTPARSGRRYRVfpegtLELRRVTAEEAGL 494
Cdd:cd20959   1 PPRIIPFAFGEGAA-QVGMRAQLHCGVPGGDLPlNIRWTLdgqpiSDDLGITVSRLGRRSSI-----LSIDSLEASHAGN 74

                        90
                ....*....|
gi 47777289 495 YTCVAQNLVG 504
Cdd:cd20959  75 YTCHARNSAG 84
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 430-501 9.98e-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: 38.74  E-value: 9.98e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLtpARSGRRYrvFPEGTLELRRVTAEEAGLYTCVAQN 501
Cdd:cd05728   6 ISDTEADIGSSLRWECKASGNPRPAYRWLK-NGQPL--ASENRIE--VEAGDLRITKLSLSDSGMYQCVAEN 72
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 72-127 1.60e-03

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: 40.54  E-value: 1.60e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47777289  72 QTLLLQSNSISRIdqTELAYLANLTELDLSQNSFSDARD--CDFQALPQLLSLHLEEN 127
Cdd:cd21340 123 RVLNISGNNIDSL--EPLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGN 178
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 430-514 2.26e-03

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 37.57  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 430 PSSLQIASGESTVLHCRALAEPEPEIYWVTpAGVRLTPARSgrryrvFPEG--TLELRRVtaEEAGLYTCVAQNLVGADT 507
Cdd:cd05739   4 PSNHEVMPGGSVNLTCVAVGAPMPYVKWMK-GGEELTKEDE------MPVGrnVLELTNI--YESANYTCVAISSLGMIE 74


                ....*..
gi 47777289 508 KTVSVVV 514
Cdd:cd05739  75 ATAQVTV 81
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 214-331 2.46e-03

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: 38.68  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   214 NLRSLVLAGmSLREISDYALEGLQSLESLSFYDNqLAQVPKRALEQVPgLKFLDLNKNpLQRVGPGDFANMLHLKELGLN 293
Cdd:pfam13306  12 SLTSITIPS-SLTSIGEYAFSNCTSLKSITLPSS-LTSIGSYAFYNCS-LTSITIPSS-LTSIGEYAFSNCSNLKSITLP 87

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 47777289   294 NmeELVSIDKFALVNLPeLTKLDITNNprLSFIHPRAF 331
Cdd:pfam13306  88 S--NLTSIGSYAFSNCS-LKSITIPSS--VTTIGSYAF 120
PLN03150 PLN03150
hypothetical protein; Provisional
 92-171 2.62e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.95  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   92 LANLTELDLSQNSFSDARDCDFQALPQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQLcriSPRAFAGLGNLLrLH 171
Cdd:PLN03150 441 LRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL---SGRVPAALGGRL-LH 516
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 72-377 2.94e-03

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: 40.42  E-value: 2.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  72 QTLLLQSNSISRIDQTEL-AYLANLTELDLSQNSFSDARdCDF-----QALPQLLSLHLEENRLNRLED------HSFAG 139
Cdd:cd00116   1 LQLSLKGELLKTERATELlPKLLCLQVLRLEGNTLGEEA-AKAlasalRPQPSLKELCLSLNETGRIPRglqsllQGLTK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 140 LTSLQELYLNHNQLCRISPRAFAGL---GNLLRLHLNSNLLRTidsrwfemlpnleilMIGGNKVDAILDmnfrPLANLR 216
Cdd:cd00116  80 GCGLQELDLSDNALGPDGCGVLESLlrsSSLQELKLNNNGLGD---------------RGLRLLAKGLKD----LPPALE 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 217 SLVLA-----GMSLREISDyALEGLQSLESLSFYDNQL----AQVPKRALEQVPGLKFLDLNKNPLQRVGPGDFANmlhl 287
Cdd:cd00116 141 KLVLGrnrleGASCEALAK-ALRANRDLKELNLANNGIgdagIRALAEGLKANCNLEVLDLNNNGLTDEGASALAE---- 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 288 kelglnnmeelvsidkfalvnlpeltklditnnprlsfihprAFHHLPQMETLMLNNNAL-----SALHQQTVESLPNLQ 362
Cdd:cd00116 216 ------------------------------------------TLASLKSLEVLNLGDNNLtdagaAALASALLSPNISLL 253

                       330
                ....*....|....*
gi 47777289 363 EVGLHGNPIRCDCVI 377
Cdd:cd00116 254 TLSLSCNDITDDGAK 268
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 67-277 3.64e-03

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: 40.54  E-value: 3.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289  67 LPAGTQ--TLLLQSNSI-----SRIDQTeLAYLANLTELDLSQNSFSDArdcDFQALPQLL-------SLHLEENRLN-- 130
Cdd:COG5238 204 LTQNTTvtTLWLKRNPIgdegaEILAEA-LKGNKSLTTLDLSNNQIGDE---GVIALAEALknnttveTLYLSGNQIGae 279

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 131 ---RLEDHsFAGLTSLQELYLNHNQlcrISPRAFAGLGNLLRlhlNSNLLRTIDsrwfemlpnleilmIGGNKVDailDM 207
Cdd:COG5238 280 gaiALAKA-LQGNTTLTSLDLSVNR---IGDEGAIALAEGLQ---GNKTLHTLN--------------LAYNGIG---AQ 335

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47777289 208 NFRPLANlrslvlagmslreisdyALEGLQSLESLSFYDNQL----AQVPKRALEQVPGLKFLDLNKNPLQRVG 277
Cdd:COG5238 336 GAIALAK-----------------ALQENTTLHSLDLSDNQIgdegAIALAKYLEGNTTLRELNLGKNNIGKQG 392
LRRCT smart00082
Leucine rich repeat C-terminal domain;
369-412 3.80e-03

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 35.87  E-value: 3.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 47777289    369 NPIRCDCVI----RWANATgthVRFIEPQSTLCAEPPDLqRRPVREVP 412
Cdd:smart00082   1 NPFICDCELrwllRWLQAN---EHLQDPVDLRCASPSSL-RGPLLELL 44
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 426-514 3.90e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 36.60  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289   426 PRSFPSSLQIASGESTVLHCRALAEPEPEIYWVTPAgvrlTPARSGRRYRVfpegtlelRRVTAEEAGLYTCVAQNLVGA 505
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDG----SAISSSPNFFT--------LSVSAEDSGTYTCVARNGRGG 69

                          90
                  ....*....|
gi 47777289   506 -DTKTVSVVV 514
Cdd:pfam13895  70 kVSNPVELTV 79
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 429-514 4.13e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 37.20  E-value: 4.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 429 FPSSLQIASGESTVLHCRALAEPEPEIYW------VTPAGVRLTPARSGRRyrvfpeGTLELRRVTAEEAGLYTCVAQNL 502
Cdd:cd05891   7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWfkndqdIELSEHYSVKLEQGKY------ASLTIKGVTSEDSGKYSINVKNK 80

                        90
                ....*....|..
gi 47777289 503 VGADTKTVSVVV 514
Cdd:cd05891  81 YGGETVDVTVSV 92
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 438-509 4.86e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM 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-non-NCAM), 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 Ig1, Ig2, and Ig3. 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). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 37.12  E-value: 4.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777289 438 GESTVLHCRALAEPEPEIYWvtpagvrltpaRSGRRYRVFPEGTLE---------------LRRVTAEEAGLYTCVAQNL 502
Cdd:cd05732  16 LEQITLTCEAEGDPIPEITW-----------RRATRGISFEEGDLDgrivvrgharvssltLKDVQLTDAGRYDCEASNR 84


                ....*..
gi 47777289 503 VGADTKT 509
Cdd:cd05732  85 IGGDQQS 91
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 438-504 5.38e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 36.31  E-value: 5.38e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47777289 438 GESTVLHCRALAEPEPEIYWV-----TPAGVRLTPARSGRRyrvfpeGTLELRRVTAEEAGLYTCVAQNLVG 504
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRlnwghVPDSARVSITSEGGY------GTLTIRDVKESDQGAYTCEAINTRG 66
PLN03150 PLN03150
hypothetical protein; Provisional
 112-177 7.86e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 39.41  E-value: 7.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47777289  112 DFQALPQLLSLHLEENRLNRLEDHSFAGLTSLQELYLNHNQLCRISPRAFAGLGNLLRLHLNSNLL 177
Cdd:PLN03150 437 DISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
LRRNT smart00013
Leucine rich repeat N-terminal domain;
28-72 8.05e-03

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.60  E-value: 8.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 47777289     28 PCPPQCACqirpwytprssyrEATTVDCNDLFLTAVPPRLPAGTQ 72
Cdd:smart00013   1 ACPAPCNC-------------SGTAVDCSGRGLTEVPLDLPPDTT 32
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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