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Conserved domains on  [gi|1046904065|ref|XP_017451895|]
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leucine-rich repeat and fibronectin type-III domain-containing protein 2 isoform X1 [Rattus norvegicus]

Protein Classification

leucine-rich repeat domain-containing protein; toll-like receptor( domain architecture ID 11471464)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions| toll-like receptor (TLR) is involved in the recognition of microbial pathogens by the innate immune system, which recognize different pathogen-associated molecular patterns

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 289-376 6.62e-42

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 cd05764:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 88  Bit Score: 147.24  E-value: 6.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNGTLDILITTSQDSGPFTCIAANAAGEA 368
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGEA 80


                  ....*...
gi 1046904065 369 TATVEVSI 376
Cdd:cd05764    81 TARVELHI 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-214 1.25e-24

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 107.33  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  56 ELRLGGNFIIHIGrQDFANMTGLVDLTLSRNTISHIqPFSFLDLESLRSLHLDSNRLPSLGEDtLRGLVNLQHLIVNNNQ 135
Cdd:COG4886   117 SLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046904065 136 LGGIADdAFEDfLLTLEDLDLSYNNLHGLPwDSVRRMVNLHQLSLDHNLLDHIAEgtFADLQKLARLDLTSNRLQKLPP 214
Cdd:COG4886   194 ITDLPE-PLGN-LTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP 267
fn3 pfam00041
Fibronectin type III domain;
428-493 2.30e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 428 VSDVTTTSALVKWSVSKSAPR-VKMYQLQY-NCSDDEVLIYRMIPASNKAFVVNNLVSGTGYDLCVLA 493
Cdd:pfam00041   8 VTDVTSTSLTVSWTPPPDGNGpITGYEVEYrPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
LRRCT smart00082
Leucine rich repeat C-terminal domain;
242-286 3.50e-05

Leucine rich repeat C-terminal domain;


:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 41.65  E-value: 3.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1046904065  242 NPLHCNCELLWLRRLERDDDLE------TCGSPGGLKGRYFwHIREEEFVC 286
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLqdpvdlRCASPSSLRGPLL-ELLHSEFKC 50
 
Name Accession Description Interval E-value
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 289-376 6.62e-42

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: 147.24  E-value: 6.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNGTLDILITTSQDSGPFTCIAANAAGEA 368
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGEA 80


                  ....*...
gi 1046904065 369 TATVEVSI 376
Cdd:cd05764    81 TARVELHI 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-214 1.25e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 107.33  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  56 ELRLGGNFIIHIGrQDFANMTGLVDLTLSRNTISHIqPFSFLDLESLRSLHLDSNRLPSLGEDtLRGLVNLQHLIVNNNQ 135
Cdd:COG4886   117 SLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046904065 136 LGGIADdAFEDfLLTLEDLDLSYNNLHGLPwDSVRRMVNLHQLSLDHNLLDHIAEgtFADLQKLARLDLTSNRLQKLPP 214
Cdd:COG4886   194 ITDLPE-PLGN-LTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP 267
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 288-360 3.16e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 3.16e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046904065 288 PPLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSR--TAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRsrSLSGSNSTLTISNVTRSDAGTYTCV 75
LRR_8 pfam13855
Leucine rich repeat;
76-136 7.16e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.00  E-value: 7.16e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065  76 TGLVDLTLSRNTISHIQPFSFLDLESLRSLHLDSNRLPSLGEDTLRGLVNLQHLIVNNNQL 136
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 61-213 4.55e-11

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: 63.27  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  61 GNFIIHIgrQDFANMTGLVDLTLSRNTISHIQPFSflDLESLRSLHLDSNRLPSL-GedtLRGLVNLQHLIVNNNQLGgi 139
Cdd:cd21340    33 DNKITKI--ENLEFLTNLTHLYLQNNQIEKIENLE--NLVNLKKLYLGGNRISVVeG---LENLTNLEELHIENQRLP-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 140 ADD--AFEDFLL-----TLEDLDLSYNNLHGLpwDSVRRMVNLHQLSLDHNLLDHIAE--GTFADLQKLARLDLTSNRLQ 210
Cdd:cd21340   104 PGEklTFDPRSLaalsnSLRVLNISGNNIDSL--EPLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPVC 181


                  ...
gi 1046904065 211 KLP 213
Cdd:cd21340   182 KKP 184
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 298-376 5.79e-09

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: 53.66  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  298 LLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNG---TLDILITTSQDSGPFTCIAANAAGEATATVEV 374
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83


                   ..
gi 1046904065  375 SI 376
Cdd:smart00410  84 TV 85
fn3 pfam00041
Fibronectin type III domain;
428-493 2.30e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 428 VSDVTTTSALVKWSVSKSAPR-VKMYQLQY-NCSDDEVLIYRMIPASNKAFVVNNLVSGTGYDLCVLA 493
Cdd:pfam00041   8 VTDVTSTSLTVSWTPPPDGNGpITGYEVEYrPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
74-246 3.48e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 50.47  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  74 NMTGLVDLTLSRNTISHIQPfsfldlESLRSLHLDSNRLPSLGEDtLRGlvNLQHLIVNNNQLGGIAddafEDFLLTLED 153
Cdd:PRK15370  179 NKTELRLKILGLTTIPACIP------EQITTLILDNNELKSLPEN-LQG--NIKTLYANSNQLTSIP----ATLPDTIQE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 154 LDLSYNNLHGLPwdsVRRMVNLHQLSLDHNLLDHIAEGTFADLQKlarLDLTSNRLQKLP---PDPIFARS-QASLLTAT 229
Cdd:PRK15370  246 MELSINRITELP---ERLPSALQSLDLFHNKISCLPENLPEELRY---LSVYDNSIRTLPahlPSGITHLNvQSNSLTAL 319

                         170       180
                  ....*....|....*....|
gi 1046904065 230 PFAPPLSFSF---GGNPLHC 246
Cdd:PRK15370  320 PETLPPGLKTleaGENALTS 339
LRRCT smart00082
Leucine rich repeat C-terminal domain;
242-286 3.50e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 41.65  E-value: 3.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1046904065  242 NPLHCNCELLWLRRLERDDDLE------TCGSPGGLKGRYFwHIREEEFVC 286
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLqdpvdlRCASPSSLRGPLL-ELLHSEFKC 50
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 428-493 5.65e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.79  E-value: 5.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 428 VSDVTTTSALVKWSVSKSAP-RVKMYQLQY-NCSDDEVLIYRMIPASNKAFVVNNLVSGTGYDLCVLA 493
Cdd:cd00063     9 VTDVTSTSVTLSWTPPEDDGgPITGYVVEYrEKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 422-493 6.20e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.13  E-value: 6.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046904065  422 PERAVLVSDVTTTSALVKWSVSKSAPRVK---MYQLQYNCSDDEVLIYRMIPASNKaFVVNNLVSGTGYDLCVLA 493
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGyivGYRVEYREEGSEWKEVNVTPSSTS-YTLTGLKPGTEYEFRVRA 76
 
Name Accession Description Interval E-value
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 289-376 6.62e-42

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: 147.24  E-value: 6.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNGTLDILITTSQDSGPFTCIAANAAGEA 368
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGEA 80


                  ....*...
gi 1046904065 369 TATVEVSI 376
Cdd:cd05764    81 TARVELHI 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-214 1.25e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 107.33  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  56 ELRLGGNFIIHIGrQDFANMTGLVDLTLSRNTISHIqPFSFLDLESLRSLHLDSNRLPSLGEDtLRGLVNLQHLIVNNNQ 135
Cdd:COG4886   117 SLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046904065 136 LGGIADdAFEDfLLTLEDLDLSYNNLHGLPwDSVRRMVNLHQLSLDHNLLDHIAEgtFADLQKLARLDLTSNRLQKLPP 214
Cdd:COG4886   194 ITDLPE-PLGN-LTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP 267
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-264 4.85e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 99.62  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  56 ELRLGGNFIIHIGRqDFANMTGLVDLTLSRNTISHIqPFSFLDLESLRSLHLDSNRLPSLGEdTLRGLVNLQHLIVNNNQ 135
Cdd:COG4886   140 ELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQ 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 136 LGGIaDDAFEDfLLTLEDLDLSYNNLHGLPWdsVRRMVNLHQLSLDHNLLDHIAEgtFADLQKLARLDLTSNRLQKLPPD 215
Cdd:COG4886   217 LTDL-PEPLAN-LTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLTDLKLK 290

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1046904065 216 PIFARSQASLLTATPFAPPLSFSFGGNPLHCNCELLWLRRLERDDDLET 264
Cdd:COG4886   291 ELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTT 339
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
49-215 7.95e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.61  E-value: 7.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  49 DIDRRTVELRLGGNFIIHIGRQDFANMTGLVDLTLSRNTishiqpfSFLDLESLRSLHLDSNRLPSLGEDtLRGLVNLQH 128
Cdd:COG4886    69 LSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 129 LIVNNNQLGGIaDDAFEDfLLTLEDLDLSYNNLHGLPwDSVRRMVNLHQLSLDHNLLDHIAEgTFADLQKLARLDLTSNR 208
Cdd:COG4886   141 LDLSNNQLTDL-PEPLGN-LTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQ 216


                  ....*..
gi 1046904065 209 LQKLPPD 215
Cdd:COG4886   217 LTDLPEP 223
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 288-360 3.16e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 3.16e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046904065 288 PPLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSR--TAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRsrSLSGSNSTLTISNVTRSDAGTYTCV 75
LRR_8 pfam13855
Leucine rich repeat;
76-136 7.16e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.00  E-value: 7.16e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065  76 TGLVDLTLSRNTISHIQPFSFLDLESLRSLHLDSNRLPSLGEDTLRGLVNLQHLIVNNNQL 136
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 61-213 4.55e-11

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: 63.27  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  61 GNFIIHIgrQDFANMTGLVDLTLSRNTISHIQPFSflDLESLRSLHLDSNRLPSL-GedtLRGLVNLQHLIVNNNQLGgi 139
Cdd:cd21340    33 DNKITKI--ENLEFLTNLTHLYLQNNQIEKIENLE--NLVNLKKLYLGGNRISVVeG---LENLTNLEELHIENQRLP-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 140 ADD--AFEDFLL-----TLEDLDLSYNNLHGLpwDSVRRMVNLHQLSLDHNLLDHIAE--GTFADLQKLARLDLTSNRLQ 210
Cdd:cd21340   104 PGEklTFDPRSLaalsnSLRVLNISGNNIDSL--EPLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPVC 181


                  ...
gi 1046904065 211 KLP 213
Cdd:cd21340   182 KKP 184
LRR_8 pfam13855
Leucine rich repeat;
52-112 1.34e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.53  E-value: 1.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065  52 RRTVELRLGGNFIIHIGRQDFANMTGLVDLTLSRNTISHIQPFSFLDLESLRSLHLDSNRL 112
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
150-209 2.21e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 2.21e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 150 TLEDLDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLLDHIAEGTFADLQKLARLDLTSNRL 209
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
125-185 2.59e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 2.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065 125 NLQHLIVNNNQLGGIADDAFEDfLLTLEDLDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLL 185
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKG-LSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
101-161 6.24e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.61  E-value: 6.24e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065 101 SLRSLHLDSNRLPSLGEDTLRGLVNLQHLIVNNNQLGGIADDAFEDfLLTLEDLDLSYNNL 161
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSG-LPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-263 7.67e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.87  E-value: 7.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  56 ELRLGGNFIIHIGrQDFANMTGLVDLTLSRNTISHIQpfSFLDLESLRSLHLDSNRLPSLGEdtLRGLVNLQHLIVNNNQ 135
Cdd:COG4886   209 ELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQ 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 136 LGGIADDAFEDFLLTLEDLDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLLDHIAEGTFADLQKLARLDLTSNRLQKLPPD 215
Cdd:COG4886   284 LTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLL 363

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1046904065 216 PIFARSQASLLTATPFAPPLSFSFGGNPLHCNCELLWLRRLERDDDLE 263
Cdd:COG4886   364 TLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 298-376 5.79e-09

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: 53.66  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  298 LLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNG---TLDILITTSQDSGPFTCIAANAAGEATATVEV 374
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83


                   ..
gi 1046904065  375 SI 376
Cdd:smart00410  84 TV 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 291-360 1.36e-08

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: 52.63  E-value: 1.36e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 291 ITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDrLVGNSSRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd20968     2 ITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDD-LIKENNRIAVLESGSLRIHNVQKEDAGQYRCV 70
I-set pfam07679
Immunoglobulin I-set domain;
289-360 1.46e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.64  E-value: 1.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVApDDRLVGNSSR---TAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK-DGQPLRSSDRfkvTYEGGTYTLTISNVQPDDSGKYTCV 74
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 298-360 2.22e-08

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: 51.84  E-value: 2.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046904065 298 LLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSrTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd05876     5 LVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRV-KYQNHNKTLQLLNVGESDDGEYVCL 66
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 27-209 6.76e-08

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 55.05  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  27 CQNLSESlgtlcpskGLLFVPPDIDRR--TVELRLGGNFIIHIGR------QDFANMTGLVDLTLSRNTISHIQP---FS 95
Cdd:cd00116    32 GNTLGEE--------AAKALASALRPQpsLKELCLSLNETGRIPRglqsllQGLTKGCGLQELDLSDNALGPDGCgvlES 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  96 FLDLESLRSLHLDSNRLPSLGEDTL-RGLVNLQH----LIVNNNQL-GGIADDAFEDF--LLTLEDLDLSYNNLHGlpwD 167
Cdd:cd00116   104 LLRSSSLQELKLNNNGLGDRGLRLLaKGLKDLPPalekLVLGRNRLeGASCEALAKALraNRDLKELNLANNGIGD---A 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046904065 168 SVRRMV-------NLHQLSLDHNLLDHIA----EGTFADLQKLARLDLTSNRL 209
Cdd:cd00116   181 GIRALAeglkancNLEVLDLNNNGLTDEGasalAETLASLKSLEVLNLGDNNL 233
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 290-360 5.08e-07

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: 48.26  E-value: 5.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065 290 LITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGSLQIKGAEKSDTGEYTCV 71
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 300-360 7.73e-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: 47.77  E-value: 7.73e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065 300 VLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVyDNGTLDILITTSQDSGPFTCI 360
Cdd:cd20978    13 VKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATV-EDGTLTIINVQPEDTGYYGCV 72
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 300-360 9.97e-07

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: 47.50  E-value: 9.97e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904065 300 VLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNGT-LDILITTSQDSGPFTCI 360
Cdd:cd20970    14 AREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGTtLTIRNIRRSDMGIYLCI 75
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 302-360 1.01e-06

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


Pssm-ID: 409561  Cd Length: 92  Bit Score: 47.38  E-value: 1.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046904065 302 EGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSS--RTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd20969    16 EGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSngRLTVFPDGTLEVRYAQVQDNGTYLCI 76
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 297-359 1.07e-06

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: 47.30  E-value: 1.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046904065 297 KLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVgNSSRTAVYDNGTLDILITTSQDSGPFTC 359
Cdd:cd05852    11 KILAAKGGRVIIECKPKAAPKPKFSWSKGTELLV-NNSRISIWDDGSLEILNITKLDEGSYTC 72
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 300-359 1.59e-06

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: 46.62  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 300 VLEGQAATLKCKAIGDPSPLIHWVAPDDRLvgNSSRTAVYDNGTLDILITTSQDSGPFTC 359
Cdd:cd05725     9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGEL--PKGRYEILDDHSLKIRKVTAGDMGSYTC 66
LRR_8 pfam13855
Leucine rich repeat;
174-215 1.77e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.59  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1046904065 174 NLHQLSLDHNLLDHIAEGTFADLQKLARLDLTSNRLQKLPPD 215
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPG 43
fn3 pfam00041
Fibronectin type III domain;
428-493 2.30e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 428 VSDVTTTSALVKWSVSKSAPR-VKMYQLQY-NCSDDEVLIYRMIPASNKAFVVNNLVSGTGYDLCVLA 493
Cdd:pfam00041   8 VTDVTSTSLTVSWTPPPDGNGpITGYEVEYrPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
74-246 3.48e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 50.47  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  74 NMTGLVDLTLSRNTISHIQPfsfldlESLRSLHLDSNRLPSLGEDtLRGlvNLQHLIVNNNQLGGIAddafEDFLLTLED 153
Cdd:PRK15370  179 NKTELRLKILGLTTIPACIP------EQITTLILDNNELKSLPEN-LQG--NIKTLYANSNQLTSIP----ATLPDTIQE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 154 LDLSYNNLHGLPwdsVRRMVNLHQLSLDHNLLDHIAEGTFADLQKlarLDLTSNRLQKLP---PDPIFARS-QASLLTAT 229
Cdd:PRK15370  246 MELSINRITELP---ERLPSALQSLDLFHNKISCLPENLPEELRY---LSVYDNSIRTLPahlPSGITHLNvQSNSLTAL 319

                         170       180
                  ....*....|....*....|
gi 1046904065 230 PFAPPLSFSF---GGNPLHC 246
Cdd:PRK15370  320 PETLPPGLKTleaGENALTS 339
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 289-360 4.77e-06

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: 45.56  E-value: 4.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVApDDRLVGNSSRTAVY--DNGTLDILIT--TSQDSGPFTCI 360
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQL-NGKPVRPDSAHKMLvrENGRHSLIIEpvTKRDAGIYTCI 75
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 289-360 5.79e-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: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNS----SRTAVYDNGTLDILIT-----TSQDSGPFTC 359
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKddprSHRIVLPSGSLFFLRVvhgrkGRSDEGVYVC 80


                  .
gi 1046904065 360 I 360
Cdd:cd07693    81 V 81
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 306-360 1.10e-05

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: 43.86  E-value: 1.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046904065 306 ATLKCKAIGDPSPLIHWVAPDDRLVGNS--SRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSrdSRRSELGNGTLTISNVTLEDSGTYTCV 57
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 74-215 1.62e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  74 NMTGLVDLTLSRNTISHIQPFSFLDLESLRSLHLDSNRLPSLGEDTLRGLVNLQHLIVNNNQL-GGIADDAFEDFLLTLe 152
Cdd:PLN00113  282 SLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFsGEIPKNLGKHNNLTV- 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046904065 153 dLDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLLDHIAEGTFADLQKLARLDLTSNRLQ-KLPPD 215
Cdd:PLN00113  361 -LDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSgELPSE 423
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 57-159 1.74e-05

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 46.70  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  57 LRLGGNFIIHIgrQDFANMTGLVDLTLSRNTISHIQPFSFLD------LESLRSLHLDSNRLPSLGEdtLRGLVNLQHLI 130
Cdd:cd21340    73 LYLGGNRISVV--EGLENLTNLEELHIENQRLPPGEKLTFDPrslaalSNSLRVLNISGNNIDSLEP--LAPLRNLEQLD 148

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1046904065 131 VNNNQLGGIADdaFEDFLLT---LEDLDLSYN 159
Cdd:cd21340   149 ASNNQISDLEE--LLDLLSSwpsLRELDLTGN 178
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 36-215 1.92e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.31  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  36 TLCPS----KGLLF-------VPPDID--RRTVELRLGGNFIIHIGRQDFANMTGLVDLTLSRNTISHIQPFSFLDLESL 102
Cdd:PLN00113  375 GLCSSgnlfKLILFsnslegeIPKSLGacRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSL 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 103 RSLHLDSNR----LP-SLGEDtlrglvNLQHLIVNNNQLGGIADDAFEDFLlTLEDLDLSYNNLHGLPWDSVRRMVNLHQ 177
Cdd:PLN00113  455 QMLSLARNKffggLPdSFGSK------RLENLDLSRNQFSGAVPRKLGSLS-ELMQLKLSENKLSGEIPDELSSCKKLVS 527

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1046904065 178 LSLDHNLLDHIAEGTFADLQKLARLDLTSNRLQ-KLPPD 215
Cdd:PLN00113  528 LDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSgEIPKN 566
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 74-224 2.11e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.31  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  74 NMTGLVDLTLSRNTISHIQPFSFLDlESLRSLHLDSNRLPSLGEDTLRGLVNLQHLIVNNNQLGGIADDAFEDfLLTLED 153
Cdd:PLN00113  450 DMPSLQMLSLARNKFFGGLPDSFGS-KRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSS-CKKLVS 527

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904065 154 LDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLLDHIAEGTFADLQKLARLDLTSNRLQ-KLPPDPIFARSQAS 224
Cdd:PLN00113  528 LDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHLHgSLPSTGAFLAINAS 599
LRRCT smart00082
Leucine rich repeat C-terminal domain;
242-286 3.50e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 41.65  E-value: 3.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1046904065  242 NPLHCNCELLWLRRLERDDDLE------TCGSPGGLKGRYFwHIREEEFVC 286
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLqdpvdlRCASPSSLRGPLL-ELLHSEFKC 50
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 297-359 3.77e-05

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: 42.83  E-value: 3.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046904065 297 KLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVgNSSRTAVYDNGTLDILITTSQDSGPFTC 359
Cdd:cd04969    11 KILAAKGGDVIIECKPKASPKPTISWSKGTELLT-NSSRICILPDGSLKIKNVTKSDEGKYTC 72
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 288-360 6.47e-05

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: 42.15  E-value: 6.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046904065 288 PPLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVgnSSRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd04968     1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPS--SQWEITTSEPVLEIPNVQFEDEGTYECE 71
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 298-360 2.11e-04

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: 40.64  E-value: 2.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046904065 298 LLVLEGQAATLKCKAI-GDPSPLIHWVAPDDRLVGNS-SRTAVYDNGTLDILI--TTSQDSGPFTCI 360
Cdd:pfam00047   6 VTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLkVKHDNGRTTQSSLLIsnVTKEDAGTYTCV 72
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 288-376 3.18e-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: 40.26  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 288 PPLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVApDDRLVGNSSRTAVYDNGTLDILITTS---QDSGPFTCIAANA 364
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFC-EGKELQNSPDIQIHQEGDLHSLIIAEafeEDTGRYSCLATNS 79

                          90
                  ....*....|..
gi 1046904065 365 AGEATATVEVSI 376
Cdd:cd20972    80 VGSDTTSAEIFV 91
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 303-360 4.91e-04

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 39.84  E-value: 4.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 303 GQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd05856    19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCH 76
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 288-376 5.07e-04

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: 39.93  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 288 PPLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSR-TAVYDNGTLDILITTSQDSGPFTCIAANAAG 366
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRsTCEAGVGELHIQDVLPEDHGTYTCLAKNAAG 80

                          90
                  ....*....|
gi 1046904065 367 EATATVEVSI 376
Cdd:cd20976    81 QVSCSAWVTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 428-493 5.65e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.79  E-value: 5.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 428 VSDVTTTSALVKWSVSKSAP-RVKMYQLQY-NCSDDEVLIYRMIPASNKAFVVNNLVSGTGYDLCVLA 493
Cdd:cd00063     9 VTDVTSTSVTLSWTPPEDDGgPITGYVVEYrEKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 422-493 6.20e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.13  E-value: 6.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046904065  422 PERAVLVSDVTTTSALVKWSVSKSAPRVK---MYQLQYNCSDDEVLIYRMIPASNKaFVVNNLVSGTGYDLCVLA 493
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGyivGYRVEYREEGSEWKEVNVTPSSTS-YTLTGLKPGTEYEFRVRA 76
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 289-376 7.01e-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: 39.31  E-value: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHW------VAPDdrlvgNSSRTAVYDNGTLDILI--TTSQDSGPFTCI 360
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWqldgkpIRPD-----SAHKMLVRENGVHSLIIepVTSRDAGIYTCI 75

                          90
                  ....*....|....*.
gi 1046904065 361 AANAAGEATATVEVSI 376
Cdd:cd20990    76 ATNRAGQNSFNLELVV 91
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 300-360 9.45e-04

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 38.70  E-value: 9.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904065 300 VLEGQAATLKCKAIGDPSPLIHWVApDDRLVGNSSRTAVYDNGTLDIL-ITTSQDSGPFTCI 360
Cdd:cd20958    12 AVAGQTLRLHCPVAGYPISSITWEK-DGRRLPLNHRQRVFPNGTLVIEnVQRSSDEGEYTCT 72
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 46-218 1.15e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.53  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  46 VPPDIDRRTVELRL----GGNFIIHIGRqdfANMTGLVDLTLSRNTISHIQPFSFLDLESLRSLHLDSNRLPSLGEDTLR 121
Cdd:PLN00113  109 IPDDIFTTSSSLRYlnlsNNNFTGSIPR---GSIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLT 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 122 GLVNLQHLIVNNNQL-GGIADDAFEdfLLTLEDLDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLLDHIAEGTFADLQKLA 200
Cdd:PLN00113  186 NLTSLEFLTLASNQLvGQIPRELGQ--MKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQ 263

                         170
                  ....*....|....*...
gi 1046904065 201 RLDLTSNRLQKLPPDPIF 218
Cdd:PLN00113  264 YLFLYQNKLSGPIPPSIF 281
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
 288-359 1.33e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) 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: 409398  Cd Length: 101  Bit Score: 39.01  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 288 PPLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDrlVGNSSRTAVY-----DNG-----TLDILITTSQDSGPF 357
Cdd:cd05735     3 PAMITSYPNTTLATKGQKKEMSCTAHGEKPIIVRWEKEDT--IINPSEMSRYlvttkEVGdevisTLQILPTVREDSGFF 80


                  ..
gi 1046904065 358 TC 359
Cdd:cd05735    81 SC 82
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 302-359 1.38e-03

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 38.00  E-value: 1.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046904065 302 EGQAATLKCKAIGDPSPLIHWVAPDDRLVGNsSRTAVYDNGTLDILITTSQDSGPFTC 359
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVD-RRHLVLSSGTLRISRVALHDQGQYEC 57
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 300-359 1.41e-03

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: 38.47  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046904065 300 VLEGQAATLKCKAIGDPSPLIHWVAPDDRL---VGNSSRTAVYDNGtLDILITTSQDSGPFTC 359
Cdd:cd20949    11 VKEGQSATILCEVKGEPQPNVTWHFNGQPIsasVADMSKYRILADG-LLINKVTQDDTGEYTC 72
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 74-209 1.82e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.76  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065  74 NMTGLVDLTLSRNTISHIQPFSFLDLESLRSLHLDSNRLP-SLGEDTLRGLVNLQHLIVNNNQLGGIADDAFedfLLTLE 152
Cdd:PLN00113   67 NSSRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNNFTGSIPRGS---IPNLE 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046904065 153 DLDLSYNNLHGLPWDSVRRMVNLHQLSLDHNLLDHIAEGTFADLQKLARLDLTSNRL 209
Cdd:PLN00113  144 TLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQL 200
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 299-360 1.96e-03

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: 37.77  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046904065 299 LVLEGQAATLKCKAIGDPSPLIHWVapddRLVGN--SSRTAVYD-NGTLDILITTSQDSGPFTCI 360
Cdd:cd05731     6 MVLRGGVLLLECIAEGLPTPDIRWI----KLGGElpKGRTKFENfNKTLKIENVSEADSGEYQCT 66
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 303-359 2.21e-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: 37.47  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904065 303 GQAATLKCKAIGDPSPLIHWV-----APDDRLVGNSSRTAvydNGTLDILITTSQDSGPFTC 359
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWRlnwghVPDSARVSITSEGG---YGTLTIRDVKESDQGAYTC 59
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 292-376 2.79e-03

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: 37.55  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 292 TQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVApDDRLVGNSSR-TAVYDNGTLDILITTS---QDSGPFTCIAANAAGE 367
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMK-DDNPIVESRRfQIDQDEDGLCSLIISDvcgDDSGKYTCKAVNSLGE 79


                  ....*....
gi 1046904065 368 ATATVEVSI 376
Cdd:cd20973    80 ATCSAELTV 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 289-358 3.99e-03

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: 37.06  E-value: 3.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046904065 289 PLITQHTHKLLVLEGQAATLKCKAIGDPSPLIHWVAPDDRLVGNSSRTAVY-DN-GTLDILI--TTSQDSGPFT 358
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYqDNcGRICLLIqnANKKDAGWYT 74
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 300-360 7.15e-03

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: 36.22  E-value: 7.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904065 300 VLEGQAATLKCKA-IGDPSPLIHWVAPDDRLVGNSSRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd05724     9 VAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVDDGNLLIAEARKSDEGTYKCV 70
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 291-360 8.09e-03

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: 36.53  E-value: 8.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046904065 291 ITQHTHKLLVLE-GQAATLKCKAIGDPSPLIHWVA---PDDRLVGNSsRTAVYDNGTLDILITTSQDSGPFTCI 360
Cdd:cd05738     1 IIDMGPQLKVVEkARTATMLCAASGNPDPEISWFKdflPVDTATSNG-RIKQLRSGALQIENSEESDQGKYECV 73
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 303-378 9.17e-03

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: 36.46  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904065 303 GQAATLKCKAIGDPSPlIHWVAPD-DRLVGNSSRTAVYDNG----TLDILITTSQDSGPFTCIAANAA-GEATATVEVSI 376
Cdd:cd04977    15 GESKFFLCKVSGDAKN-INWVSPNgEKVLTKHGNLKVVNHGsvlsSLTIYNANINDAGIYKCVATNGKgTESEATVKLDI 93


                  ..
gi 1046904065 377 VQ 378
Cdd:cd04977    94 IQ 95
 
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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