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Conserved domains on  [gi|124339785|ref|NP_619623|]
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leucine-rich repeat-containing protein 4 precursor [Mus musculus]

Protein Classification

LRR and IG_like domain-containing protein( domain architecture ID 12183483)

protein containing domains LRRNT, LRR, LRRCT, and IG_like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-322 7.26e-26

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.79  E-value: 7.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  74 SNTRYLNLMENNIQMIqADTFRHLHHLEVLQLGRNSIRQIEVgAFNGLASLNTLELFDNWLTVIPSgAFEYLSKLRELWL 153
Cdd:COG4886  113 TNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 154 RNNPIESIPSyAFNRVPSLMRLDLGElKKLEYISEgAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIR 233
Cdd:COG4886  190 SNNQITDLPE-PLGNLTNLEELDLSG-NQLTDLPE-PLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 234 PGSfhGLSSLKKLWVMNSQVS---LIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWL 310
Cdd:COG4886  267 PLA--NLTNLKTLDLSNNQLTdlkLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSL 344

                        250
                 ....*....|..
gi 124339785 311 AWWLREYIPTNS 322
Cdd:COG4886  345 SLLALLTLLLLL 356
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 358-440 4.06e-10

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: 56.74  E-value: 4.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   358 PRDLNISEDRMAELKCRT--PPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNAS 435
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAsgSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 124339785   436 AYLNV 440
Cdd:smart00410  81 TTLTV 85
LRRCT smart00082
Leucine rich repeat C-terminal domain;
299-350 2.25e-06

Leucine rich repeat C-terminal domain;


:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.11  E-value: 2.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 124339785   299 NPWNCDCDILWLAWWLR--EYIPTN-STccgRCHAPMHMRGRyLVEVDQAAFQCS 350
Cdd:smart00082   1 NPFICDCELRWLLRWLQanEHLQDPvDL---RCASPSSLRGP-LLELLHSEFKCP 51
LRRNT smart00013
Leucine rich repeat N-terminal domain;
45-78 3.06e-04

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.45  E-value: 3.06e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 124339785    45 CPSVCSCSNqfSKVVCTRRGLSEVPQGIPSNTRY 78
Cdd:smart00013   2 CPAPCNCSG--TAVDCSGRGLTEVPLDLPPDTTL 33
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-322 7.26e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.79  E-value: 7.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  74 SNTRYLNLMENNIQMIqADTFRHLHHLEVLQLGRNSIRQIEVgAFNGLASLNTLELFDNWLTVIPSgAFEYLSKLRELWL 153
Cdd:COG4886  113 TNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 154 RNNPIESIPSyAFNRVPSLMRLDLGElKKLEYISEgAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIR 233
Cdd:COG4886  190 SNNQITDLPE-PLGNLTNLEELDLSG-NQLTDLPE-PLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 234 PGSfhGLSSLKKLWVMNSQVS---LIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWL 310
Cdd:COG4886  267 PLA--NLTNLKTLDLSNNQLTdlkLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSL 344

                        250
                 ....*....|..
gi 124339785 311 AWWLREYIPTNS 322
Cdd:COG4886  345 SLLALLTLLLLL 356
LRR_8 pfam13855
Leucine rich repeat;
74-132 2.98e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.77  E-value: 2.98e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124339785   74 SNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDN 132
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 96-300 5.71e-12

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 65.58  E-value: 5.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  96 HLHhlevLQlGRNsIRQIEvgAFNGLASLNTLELFDNWLTVIPSgaFEYLSKLRELWLRNNPIESIpsyafnrvpslmrl 175
Cdd:cd21340    6 HLY----LN-DKN-ITKID--NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKI-------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 176 dlgelkkleyisEGaFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPE-----IRPGSFHGLS-SLKKLWVM 249
Cdd:cd21340   62 ------------EN-LENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPPgekltFDPRSLAALSnSLRVLNIS 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124339785 250 NSQVSLIErnAFDGLASLVELNLAHNNLSSLPH--DLFTPLRYLVELHLHHNP 300
Cdd:cd21340  129 GNNIDSLE--PLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNP 179
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 358-440 4.06e-10

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: 56.74  E-value: 4.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   358 PRDLNISEDRMAELKCRT--PPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNAS 435
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAsgSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 124339785   436 AYLNV 440
Cdd:smart00410  81 TTLTV 85
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 353-440 2.71e-09

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 54.38  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 353 FIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLLpNGTVLSHASRHPRiSVLNDGTLNFSRVLLIDTGVYTCMVTNVAG 430
Cdd:cd04978    1 YWIIEPPSLVLSPGETGELICEAEgnPQPTITWRL-NGVPIEPAPEDMR-RTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78

                         90
                 ....*....|
gi 124339785 431 NSNASAYLNV 440
Cdd:cd04978   79 YLLANAFLHV 88
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
54-291 5.30e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 52.78  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  54 QFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQA---DTfrhlhhLEVLQLGRNSIRQIEvgafNGLAS-LNTLEL 129
Cdd:PRK15370 200 QITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPAtlpDT------IQEMELSINRITELP----ERLPSaLQSLDL 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 130 FDNWLTVIPSGAFEylsKLRELWLRNNPIESIPSYafnrVPSlmrldlgelkkleyisegafeglfNLKYLNLGMCNIKD 209
Cdd:PRK15370 270 FHNKISCLPENLPE---ELRYLSVYDNSIRTLPAH----LPS------------------------GITHLNVQSNSLTA 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 210 MPNLTPLvGLEELEMSGNHF---PEIRPgsfhglSSLKKLWVMNSQVSLIERNAfdgLASLVELNLAHNNLSSLPHDLFT 286
Cdd:PRK15370 319 LPETLPP-GLKTLEAGENALtslPASLP------PELQVLDVSKNQITVLPETL---PPTITTLDVSRNALTNLPENLPA 388


                 ....*
gi 124339785 287 PLRYL 291
Cdd:PRK15370 389 ALQIM 393
I-set pfam07679
Immunoglobulin I-set domain;
352-440 5.50e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  352 PFIMDAPRDLNISEDRMAELKCR---TPPMSsVKWLLpNGTVLSHASRHpriSVLNDG---TLNFSRVLLIDTGVYTCMV 425
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTvtgTPDPE-VSWFK-DGQPLRSSDRF---KVTYEGgtyTLTISNVQPDDSGKYTCVA 75

                          90
                  ....*....|....*
gi 124339785  426 TNVAGNSNASAYLNV 440
Cdd:pfam07679  76 TNSAGEAEASAELTV 90
LRRCT smart00082
Leucine rich repeat C-terminal domain;
299-350 2.25e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.11  E-value: 2.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 124339785   299 NPWNCDCDILWLAWWLR--EYIPTN-STccgRCHAPMHMRGRyLVEVDQAAFQCS 350
Cdd:smart00082   1 NPFICDCELRWLLRWLQanEHLQDPvDL---RCASPSSLRGP-LLELLHSEFKCP 51
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 271-354 1.00e-05

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 48.93  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   271 NLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLRE-----YIPTNSTCCGrchaPMHMRGRYLVEVDQA 345
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEkgvkvRQPEAALCAG----PGALAGQPLLGIPLL 76


                   ....*....
gi 124339785   346 AFQCSAPFI 354
Cdd:TIGR00864   77 DSGCDEEYV 85
LRRNT smart00013
Leucine rich repeat N-terminal domain;
45-78 3.06e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.45  E-value: 3.06e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 124339785    45 CPSVCSCSNqfSKVVCTRRGLSEVPQGIPSNTRY 78
Cdd:smart00013   2 CPAPCNCSG--TAVDCSGRGLTEVPLDLPPDTTL 33
LRR smart00370
Leucine-rich repeats, outliers;
264-285 1.43e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 36.18  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|..
gi 124339785   264 LASLVELNLAHNNLSSLPHDLF 285
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAF 22
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 45-73 2.50e-03

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


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 35.68  E-value: 2.50e-03
                          10        20
                  ....*....|....*....|....*....
gi 124339785   45 CPSVCSCSNqfSKVVCTRRGLSEVPQGIP 73
Cdd:pfam01462   2 CPVPCHCSA--TVVNCSDRGLTAVPRDLP 28
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-322 7.26e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.79  E-value: 7.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  74 SNTRYLNLMENNIQMIqADTFRHLHHLEVLQLGRNSIRQIEVgAFNGLASLNTLELFDNWLTVIPSgAFEYLSKLRELWL 153
Cdd:COG4886  113 TNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 154 RNNPIESIPSyAFNRVPSLMRLDLGElKKLEYISEgAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIR 233
Cdd:COG4886  190 SNNQITDLPE-PLGNLTNLEELDLSG-NQLTDLPE-PLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 234 PGSfhGLSSLKKLWVMNSQVS---LIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWL 310
Cdd:COG4886  267 PLA--NLTNLKTLDLSNNQLTdlkLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSL 344

                        250
                 ....*....|..
gi 124339785 311 AWWLREYIPTNS 322
Cdd:COG4886  345 SLLALLTLLLLL 356
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-300 2.80e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 105.79  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  74 SNTRYLNLMENNiqmiqadTFRHLHHLEVLQLGRNSIRQIEVgAFNGLASLNTLELFDNWLTVIPSgAFEYLSKLRELWL 153
Cdd:COG4886   96 TNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 154 RNNPIESIPSyafnrvpslmrldlgelkkleyisegAFEGLFNLKYLNLGMCNIKDMPN-LTPLVGLEELEMSGNHFPEI 232
Cdd:COG4886  167 SNNQLTDLPE--------------------------ELGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDL 220

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124339785 233 rPGSFHGLSSLKKLWVMNSQVSLIErnAFDGLASLVELNLAHNNLSSLPHDLftPLRYLVELHLHHNP 300
Cdd:COG4886  221 -PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
96-299 1.87e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 81.90  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  96 HLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRL 175
Cdd:COG4886   14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 176 DLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMP-NLTPLVGLEELEMSGNHFPEIrPGSFHGLSSLKKLWVMNSQVS 254
Cdd:COG4886   94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPeELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLT 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 124339785 255 LIErNAFDGLASLVELNLAHNNLSSLPHDLfTPLRYLVELHLHHN 299
Cdd:COG4886  173 DLP-EELGNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSGN 215
LRR_8 pfam13855
Leucine rich repeat;
74-132 2.98e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.77  E-value: 2.98e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124339785   74 SNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDN 132
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 96-300 5.71e-12

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 65.58  E-value: 5.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  96 HLHhlevLQlGRNsIRQIEvgAFNGLASLNTLELFDNWLTVIPSgaFEYLSKLRELWLRNNPIESIpsyafnrvpslmrl 175
Cdd:cd21340    6 HLY----LN-DKN-ITKID--NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKI-------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 176 dlgelkkleyisEGaFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPE-----IRPGSFHGLS-SLKKLWVM 249
Cdd:cd21340   62 ------------EN-LENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPPgekltFDPRSLAALSnSLRVLNIS 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124339785 250 NSQVSLIErnAFDGLASLVELNLAHNNLSSLPH--DLFTPLRYLVELHLHHNP 300
Cdd:cd21340  129 GNNIDSLE--PLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNP 179
LRR_8 pfam13855
Leucine rich repeat;
99-158 8.42e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.92  E-value: 8.42e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   99 HLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPI 158
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 358-440 4.06e-10

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: 56.74  E-value: 4.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   358 PRDLNISEDRMAELKCRT--PPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNAS 435
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAsgSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 124339785   436 AYLNV 440
Cdd:smart00410  81 TTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
218-277 1.20e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.45  E-value: 1.20e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  218 GLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNL 277
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 84-198 1.60e-09

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


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 56.01  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   84 NNIQMIQADTFRHLHHLEVLQLGrNSIRQIEVGAFNGlASLNTLELFDNwLTVIPSGAFEYLSKLRELWLRNNpIESIPS 163
Cdd:pfam13306  20 SSLTSIGEYAFSNCTSLKSITLP-SSLTSIGSYAFYN-CSLTSITIPSS-LTSIGEYAFSNCSNLKSITLPSN-LTSIGS 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 124339785  164 YAFNRVpSLMRLDLGelKKLEYISEGAFEGLFNLK 198
Cdd:pfam13306  96 YAFSNC-SLKSITIP--SSVTTIGSYAFSNCSNLK 127
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 75-246 1.84e-09

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: 58.26  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  75 NTRYLNLMENNIQMIQAdtFRHLHHLEVLQLGRNSIRQIEVgaFNGLASLNTLELFDNWLTVIpSGaFEYLSKLRELWLR 154
Cdd:cd21340   25 NLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVV-EG-LENLTNLEELHIE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 155 NNpiesipsyafnrvpslmRLDLGElkKLE-------YISEgafeglfNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGN 227
Cdd:cd21340   99 NQ-----------------RLPPGE--KLTfdprslaALSN-------SLRVLNISGNNIDSLEPLAPLRNLEQLDASNN 152

                        170       180
                 ....*....|....*....|.
gi 124339785 228 HFPEIRP--GSFHGLSSLKKL 246
Cdd:cd21340  153 QISDLEEllDLLSSWPSLREL 173
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 353-440 2.71e-09

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 54.38  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 353 FIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLLpNGTVLSHASRHPRiSVLNDGTLNFSRVLLIDTGVYTCMVTNVAG 430
Cdd:cd04978    1 YWIIEPPSLVLSPGETGELICEAEgnPQPTITWRL-NGVPIEPAPEDMR-RTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78

                         90
                 ....*....|
gi 124339785 431 NSNASAYLNV 440
Cdd:cd04978   79 YLLANAFLHV 88
LRR_8 pfam13855
Leucine rich repeat;
146-207 8.44e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.14  E-value: 8.44e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124339785  146 SKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGElKKLEYISEGAFEGLFNLKYLNLGMCNI 207
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSN-NLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 352-440 9.41e-09

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: 52.86  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 352 PFIMDAPRDLNISEDRMAELKCRT--PPMSSVKWLLPNGTVLSHASRhprISVLNDGTLNFSRVLLIDTGVYTCMVTNVA 429
Cdd:cd05764    1 PLITRHTHELRVLEGQRATLRCKArgDPEPAIHWISPEGKLISNSSR---TLVYDNGTLDILITTVKDTGAFTCIASNPA 77

                         90
                 ....*....|.
gi 124339785 430 GNSNASAYLNV 440
Cdd:cd05764   78 GEATARVELHI 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 369-430 1.33e-08

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: 51.95  E-value: 1.33e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124339785 369 AELKCRT--PPMSSVKWLLpNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAG 430
Cdd:cd00096    1 VTLTCSAsgNPPPTITWYK-NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 352-440 2.88e-08

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: 51.73  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 352 PFIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLLpNGTVLSHASRHPRIsVLNDG--TLNFSRVLLIDTGVYTCMVTN 427
Cdd:cd05744    1 PHFLQAPGDLEVQEGRLCRFDCKVSglPTPDLFWQL-NGKPVRPDSAHKML-VRENGrhSLIIEPVTKRDAGIYTCIARN 78

                         90
                 ....*....|...
gi 124339785 428 VAGNSNASAYLNV 440
Cdd:cd05744   79 RAGENSFNAELVV 91
LRR_8 pfam13855
Leucine rich repeat;
241-300 5.81e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.83  E-value: 5.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  241 SSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNP 300
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNR 60
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 354-440 1.81e-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: 49.03  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 354 IMDAPRDLNISEDRMAELKCRT--PPMSSVKWLLPNGTVLShasRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGN 431
Cdd:cd20952    2 ILQGPQNQTVAVGGTVVLNCQAtgEPVPTISWLKDGVPLLG---KDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                 ....*....
gi 124339785 432 SNASAYLNV 440
Cdd:cd20952   79 ATWSAVLDV 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 370-440 2.14e-07

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.00  E-value: 2.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124339785 370 ELKCRTPPMSSVKWllPNGTVLSHASrhPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd04969   23 ECKPKASPKPTISW--SKGTELLTNS--SRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 370-440 4.96e-07

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: 48.15  E-value: 4.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124339785 370 ELKCRTPPMSSVKWLLPNGTVLShASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd20969   23 VCRADGDPPPAILWLSPRKHLVS-AKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 358-440 5.08e-07

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


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.00  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 358 PRDLNISEDRMAELKCRTP--PMSSVKWLLPNGTVLShASRHPRISVLNDGTLNF-SRVLLIDTGVYTCMVTNVAGNSNA 434
Cdd:cd05763    6 PHDITIRAGSTARLECAATghPTPQIAWQKDGGTDFP-AARERRMHVMPEDDVFFiVDVKIEDTGVYSCTAQNSAGSISA 84


                 ....*.
gi 124339785 435 SAYLNV 440
Cdd:cd05763   85 NATLTV 90
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 91-304 5.12e-07

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: 51.97  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  91 ADTFRHLHHLEVLQLGRNSIRQIEVGA-FNGLA---SLNTLELFDNWLTVIPSG------AFEYLSKLRELWLRNNPIE- 159
Cdd:cd00116   16 TELLPKLLCLQVLRLEGNTLGEEAAKAlASALRpqpSLKELCLSLNETGRIPRGlqsllqGLTKGCGLQELDLSDNALGp 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 160 --SIPSYAFNRVPSLMRLDLG----ELKKLEYISEGAFEGLFNLKYLNLGMCNI-----KDMPNLTPLVG-LEELEMSGN 227
Cdd:cd00116   96 dgCGVLESLLRSSSLQELKLNnnglGDRGLRLLAKGLKDLPPALEKLVLGRNRLegascEALAKALRANRdLKELNLANN 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 228 HF-PEIRPGSFHGL---SSLKKLWVMNSQVSLIERNAFDG----LASLVELNLAHNNLSSLP----HD-LFTPLRYLVEL 294
Cdd:cd00116  176 GIgDAGIRALAEGLkanCNLEVLDLNNNGLTDEGASALAEtlasLKSLEVLNLGDNNLTDAGaaalASaLLSPNISLLTL 255

                        250
                 ....*....|
gi 124339785 295 HLhhnpWNCD 304
Cdd:cd00116  256 SL----SCND 261
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
54-291 5.30e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 52.78  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  54 QFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQA---DTfrhlhhLEVLQLGRNSIRQIEvgafNGLAS-LNTLEL 129
Cdd:PRK15370 200 QITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPAtlpDT------IQEMELSINRITELP----ERLPSaLQSLDL 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 130 FDNWLTVIPSGAFEylsKLRELWLRNNPIESIPSYafnrVPSlmrldlgelkkleyisegafeglfNLKYLNLGMCNIKD 209
Cdd:PRK15370 270 FHNKISCLPENLPE---ELRYLSVYDNSIRTLPAH----LPS------------------------GITHLNVQSNSLTA 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 210 MPNLTPLvGLEELEMSGNHF---PEIRPgsfhglSSLKKLWVMNSQVSLIERNAfdgLASLVELNLAHNNLSSLPHDLFT 286
Cdd:PRK15370 319 LPETLPP-GLKTLEAGENALtslPASLP------PELQVLDVSKNQITVLPETL---PPTITTLDVSRNALTNLPENLPA 388


                 ....*
gi 124339785 287 PLRYL 291
Cdd:PRK15370 389 ALQIM 393
I-set pfam07679
Immunoglobulin I-set domain;
352-440 5.50e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  352 PFIMDAPRDLNISEDRMAELKCR---TPPMSsVKWLLpNGTVLSHASRHpriSVLNDG---TLNFSRVLLIDTGVYTCMV 425
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTvtgTPDPE-VSWFK-DGQPLRSSDRF---KVTYEGgtyTLTISNVQPDDSGKYTCVA 75

                          90
                  ....*....|....*
gi 124339785  426 TNVAGNSNASAYLNV 440
Cdd:pfam07679  76 TNSAGEAEASAELTV 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 351-440 6.97e-07

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: 47.63  E-value: 6.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 351 APFIMDAPRDLNISEDRMAELKC--RTPPMSSVKWLLpNGTVLSHASRHPRISVLNdGTLNFSRVLLIDTGVYTCMVTNV 428
Cdd:cd20976    1 APSFSSVPKDLEAVEGQDFVAQCsaRGKPVPRITWIR-NAQPLQYAADRSTCEAGV-GELHIQDVLPEDHGTYTCLAKNA 78

                         90
                 ....*....|..
gi 124339785 429 AGNSNASAYLNV 440
Cdd:cd20976   79 AGQVSCSAWVTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 352-427 8.39e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.18  E-value: 8.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124339785  352 PFIMDAPRDLNISEDRMAELKCRT--PPMSSVKWLLpNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTN 427
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEAtgSPPPTITWYK-NGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 358-440 1.01e-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: 47.00  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 358 PRDLNISEDRMAELKCRT--PPMSSVKWL-----LPNGtvlshasrhpRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAG 430
Cdd:cd05725    4 PQNQVVLVDDSAEFQCEVggDPVPTVRWRkedgeLPKG----------RYEILDDHSLKIRKVTAGDMGSYTCVAENMVG 73

                         90
                 ....*....|
gi 124339785 431 NSNASAYLNV 440
Cdd:cd05725   74 KIEASATLTV 83
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 360-440 1.45e-06

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.44  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 360 DLNISEDRMAELKCRTPPMSSVKWLlPNGTVLShasRHPRISVLNdGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLN 439
Cdd:cd05728   10 EADIGSSLRWECKASGNPRPAYRWL-KNGQPLA---SENRIEVEA-GDLRITKLSLSDSGMYQCVAENKHGTIYASAELA 84


                 .
gi 124339785 440 V 440
Cdd:cd05728   85 V 85
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 358-440 2.00e-06

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: 46.24  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 358 PRDLNISEDRMAELKCRTP---PMSSVKWLlPNGTVLshASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAG-NSN 433
Cdd:cd05724    4 PSDTQVAVGEMAVLECSPPrghPEPTVSWR-KDGQPL--NLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGeRES 80


                 ....*..
gi 124339785 434 ASAYLNV 440
Cdd:cd05724   81 RAARLSV 87
LRRCT smart00082
Leucine rich repeat C-terminal domain;
299-350 2.25e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.11  E-value: 2.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 124339785   299 NPWNCDCDILWLAWWLR--EYIPTN-STccgRCHAPMHMRGRyLVEVDQAAFQCS 350
Cdd:smart00082   1 NPFICDCELRWLLRWLQanEHLQDPvDL---RCASPSSLRGP-LLELLHSEFKCP 51
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 354-434 3.94e-06

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


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 354 IMDAPRDLNISEDRMAELKCRT--PPMSSVKWLlPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGN 431
Cdd:cd05747    6 ILTKPRSLTVSEGESARFSCDVdgEPAPTVTWM-REGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84


                 ...
gi 124339785 432 SNA 434
Cdd:cd05747   85 QEA 87
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 67-299 3.95e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.23  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  67 EVPQGIPSNTRY--LNLMENNIQ-MIQADTFRHlHHLEVLQLGRNSIR-QIEVGAFNGlASLNTLELFDNWL-TVIPSgA 141
Cdd:PLN00113 323 KIPVALTSLPRLqvLQLWSNKFSgEIPKNLGKH-NNLTVLDLSTNNLTgEIPEGLCSS-GNLFKLILFSNSLeGEIPK-S 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 142 FEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEgLFNLKYLNLGMCNI-KDMPNLTPLVGLE 220
Cdd:PLN00113 400 LGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWD-MPSLQMLSLARNKFfGGLPDSFGSKRLE 478

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124339785 221 ELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHN 299
Cdd:PLN00113 479 NLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQN 557
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 369-440 5.12e-06

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: 45.08  E-value: 5.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124339785 369 AELKCRT--PPMSSVKWLlPNGTVLShaSRHPRISVlNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd20978   19 VTLPCQVtgVPQPKITWL-HNGKPLQ--GPMERATV-EDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 358-443 8.98e-06

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


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 44.56  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 358 PRDLNISEDRMAELKCRTP--PMSSVKWLLPNGTVLSHASRHP----RISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGN 431
Cdd:cd05726    6 PRDQVVALGRTVTFQCETKgnPQPAIFWQKEGSQNLLFPYQPPqpssRFSVSPTGDLTITNVQRSDVGYYICQALNVAGS 85

                         90
                 ....*....|..
gi 124339785 432 SNASAYLNVSSA 443
Cdd:cd05726   86 ILAKAQLEVTDV 97
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 271-354 1.00e-05

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 48.93  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785   271 NLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLRE-----YIPTNSTCCGrchaPMHMRGRYLVEVDQA 345
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEkgvkvRQPEAALCAG----PGALAGQPLLGIPLL 76


                   ....*....
gi 124339785   346 AFQCSAPFI 354
Cdd:TIGR00864   77 DSGCDEEYV 85
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 355-440 1.66e-05

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


Pssm-ID: 409454  Cd Length: 89  Bit Score: 43.82  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 355 MDAPRDLNISEDRMAELKCRTP--PMSSVKWLLpNGTVLSHASRHPRISVLNDgTLNFSRVLLIDTGVYTCMVTNVAGNS 432
Cdd:cd05868    3 ITAPTNLVLSPGEDGTLICRANgnPKPSISWLT-NGVPIEIAPTDPSRKVDGD-TIIFSKVQERSSAVYQCNASNEYGYL 80


                 ....*...
gi 124339785 433 NASAYLNV 440
Cdd:cd05868   81 LANAFVNV 88
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 377-440 2.23e-05

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: 43.00  E-value: 2.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124339785 377 PMSSVKWLlPNGTVLSHASRHpriSVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd05745   15 PQPVIAWT-KGGSQLSVDRRH---LVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 352-440 3.95e-05

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: 42.78  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 352 PFIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLLpNGTVLSHASRHpRISVLNDG--TLNFSRVLLIDTGVYTCMVTN 427
Cdd:cd20990    1 PHFLQAPGDLTVQEGKLCRMDCKVSglPTPDLSWQL-DGKPIRPDSAH-KMLVRENGvhSLIIEPVTSRDAGIYTCIATN 78

                         90
                 ....*....|...
gi 124339785 428 VAGNSNASAYLNV 440
Cdd:cd20990   79 RAGQNSFNLELVV 91
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 68-299 4.25e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.76  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  68 VPQGI---PSNTRYLNLMENNIQMIQADTFrhLHHLEVLQLGRNSIR---QIEVGAFnglASLNTLELFDNWLTVIPSGA 141
Cdd:PLN00113 109 IPDDIfttSSSLRYLNLSNNNFTGSIPRGS--IPNLETLDLSNNMLSgeiPNDIGSF---SSLKVLDLGGNVLVGKIPNS 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 142 FEYLSKLRELWLRNNPIesipsyaFNRVPSlmrlDLGELKkleyisegafeglfNLKYLNLGMCNIK-DMPN-LTPLVGL 219
Cdd:PLN00113 184 LTNLTSLEFLTLASNQL-------VGQIPR----ELGQMK--------------SLKWIYLGYNNLSgEIPYeIGGLTSL 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 220 EELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHN 299
Cdd:PLN00113 239 NHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSN 318
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 351-440 2.70e-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: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 351 APFIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLLpNGTVLSHAsrhPRISVLNDGTLNfsrVLLI------DTGVYT 422
Cdd:cd20972    1 PPQFIQKLRSQEVAEGSKVRLECRVTgnPTPVVRWFC-EGKELQNS---PDIQIHQEGDLH---SLIIaeafeeDTGRYS 73

                         90
                 ....*....|....*...
gi 124339785 423 CMVTNVAGNSNASAYLNV 440
Cdd:cd20972   74 CLATNSVGSDTTSAEIFV 91
LRRNT smart00013
Leucine rich repeat N-terminal domain;
45-78 3.06e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.45  E-value: 3.06e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 124339785    45 CPSVCSCSNqfSKVVCTRRGLSEVPQGIPSNTRY 78
Cdd:smart00013   2 CPAPCNCSG--TAVDCSGRGLTEVPLDLPPDTTL 33
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 359-440 3.53e-04

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 39.87  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 359 RDLNISEDRMAELKCRTP--PMSSVKWLLPNGTVLShaSRHPRISVLNDG--TLNFSRVLLIDTGVYTCMVTNVAGNSNA 434
Cdd:cd20973    5 RDKEVVEGSAARFDCKVEgyPDPEVKWMKDDNPIVE--SRRFQIDQDEDGlcSLIISDVCGDDSGKYTCKAVNSLGEATC 82


                 ....*.
gi 124339785 435 SAYLNV 440
Cdd:cd20973   83 SAELTV 88
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 370-440 5.08e-04

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: 39.60  E-value: 5.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124339785 370 ELKCRTPPMSSVKW-----LLPNGTvlshasrhpRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd05852   23 ECKPKAAPKPKFSWskgteLLVNNS---------RISIWDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 159-285 5.09e-04

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


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 40.22  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  159 ESIPSYAFnrvpslMRLDLGEL---KKLEYISEGAFEGLFNLKYLNLgmcnikdmPNLTPLVG--------LEELEMSGN 227
Cdd:pfam13306   1 TSIGSYAF------YNCSLTSItipSSLTSIGEYAFSNCTSLKSITL--------PSSLTSIGsyafyncsLTSITIPSS 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124339785  228 hFPEIRPGSFHGLSSLKKLwVMNSQVSLIERNAFDGlASLVELNLaHNNLSSLPHDLF 285
Cdd:pfam13306  67 -LTSIGEYAFSNCSNLKSI-TLPSNLTSIGSYAFSN-CSLKSITI-PSSVTTIGSYAF 120
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 371-440 6.35e-04

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 39.42  E-value: 6.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124339785 371 LKCRTP---PMSSVKWLlPNGTVLShASRHPRISVLN---DGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd05750   19 LKCEATsenPSPRYRWF-KDGKELN-RKRPKNIKIRNkkkNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 352-435 9.49e-04

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: 39.07  E-value: 9.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 352 PFIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLlPNGTVLSHASRHPRIS--VLNDGTLNFSRVL-----LIDTGVYT 422
Cdd:cd07693    1 PRIVEHPSDLIVSKGDPATLNCKAEgrPTPTIQWL-KNGQPLETDKDDPRSHriVLPSGSLFFLRVVhgrkgRSDEGVYV 79

                         90
                 ....*....|....*.
gi 124339785 423 CMVTNVAGNS---NAS 435
Cdd:cd07693   80 CVAHNSLGEAvsrNAS 95
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
64-281 1.33e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 42.07  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  64 GLSEVPQGIPSNTRYLNLMENNIQMIQADTfrhlHHLEVLQLGRNSIRQIEVGAfnglASLNTLELFDNWLTVIPSgafe 143
Cdd:PRK15387 212 GLTTLPDCLPAHITTLVIPDNNLTSLPALP----PELRTLEVSGNQLTSLPVLP----PGLLELSIFSNPLTHLPA---- 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 144 YLSKLRELWLRNNPIESIPSYAfnrvPSLMRLDLGElKKLEYISEGAFEgLFNLKYLNLGMCNIKDMPNltplvGLEELE 223
Cdd:PRK15387 280 LPSGLCKLWIFGNQLTSLPVLP----PGLQELSVSD-NQLASLPALPSE-LCKLWAYNNQLTSLPTLPS-----GLQELS 348

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124339785 224 MSGNHFPEIRPGSfhglSSLKKLWVMNSQVSliernAFDGLAS-LVELNLAHNNLSSLP 281
Cdd:PRK15387 349 VSDNQLASLPTLP----SELYKLWAYNNRLT-----SLPALPSgLKELIVSGNRLTSLP 398
LRR smart00370
Leucine-rich repeats, outliers;
264-285 1.43e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 36.18  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|..
gi 124339785   264 LASLVELNLAHNNLSSLPHDLF 285
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAF 22
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
264-285 1.43e-03

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


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 36.18  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|..
gi 124339785   264 LASLVELNLAHNNLSSLPHDLF 285
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAF 22
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 358-438 1.55e-03

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


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 37.90  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 358 PRDLNISEDRMAELKCRTP--PMSSVKWLlPNGTVLSHASRhprISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNAS 435
Cdd:cd20957    8 PPVQTVDFGRTAVFNCSVTgnPIHTVLWM-KDGKPLGHSSR---VQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQAT 83


                 ...
gi 124339785 436 AYL 438
Cdd:cd20957   84 AEL 86
LRR_8 pfam13855
Leucine rich repeat;
170-246 1.87e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 1.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124339785  170 PSLMRLDLGElKKLEYISEGAFEGLFNLKYLNLgmcnikdmpnltplvgleelemSGNHFPEIRPGSFHGLSSLKKL 246
Cdd:pfam13855   1 PNLRSLDLSN-NRLTSLDDGAFKGLSNLKVLDL----------------------SNNLLTTLSPGAFSGLPSLRYL 54
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 77-164 2.33e-03

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 39.77  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  77 RYLNLMENNIQMIQAdtFRHLHHLEVLQLGRNSIRQIEVgafnglaslnTLELFDNWltvipsgafeylSKLRELWLRNN 156
Cdd:cd21340  123 RVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEE----------LLDLLSSW------------PSLRELDLTGN 178


                 ....*...
gi 124339785 157 PIESIPSY 164
Cdd:cd21340  179 PVCKKPKY 186
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 45-73 2.50e-03

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


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 35.68  E-value: 2.50e-03
                          10        20
                  ....*....|....*....|....*....
gi 124339785   45 CPSVCSCSNqfSKVVCTRRGLSEVPQGIP 73
Cdd:pfam01462   2 CPVPCHCSA--TVVNCSDRGLTAVPRDLP 28
LRR smart00370
Leucine-rich repeats, outliers;
145-167 2.62e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 2.62e-03
                           10        20
                   ....*....|....*....|...
gi 124339785   145 LSKLRELWLRNNPIESIPSYAFN 167
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQ 23
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
145-167 2.62e-03

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


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 2.62e-03
                           10        20
                   ....*....|....*....|...
gi 124339785   145 LSKLRELWLRNNPIESIPSYAFN 167
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAFQ 23
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 371-440 2.75e-03

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 37.54  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 371 LKC--RTPPMSSVKWLLpNGTVLShasRHPRIS----VLNDGT----LNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNV 440
Cdd:cd20956   21 LKCvaSGNPLPQITWTL-DGFPIP---ESPRFRvgdyVTSDGDvvsyVNISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 352-440 2.83e-03

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 37.40  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 352 PFIMDAPRDLNISEDRMAELKCRTP--PMSSVKWLlPNGTVLSHASRHPRISVLNDG---TLNFSRVLLIDTGVYTCMVT 426
Cdd:cd20951    1 PEFIIRLQSHTVWEKSDAKLRVEVQgkPDPEVKWY-KNGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAK 79

                         90
                 ....*....|....
gi 124339785 427 NVAGNSNASAYLNV 440
Cdd:cd20951   80 NIHGEASSSASVVV 93
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 196-227 3.59e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.68  E-value: 3.59e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 124339785  196 NLKYLNLGMCNIKDMPNLTPLVGLEELEMSGN 227
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGN 33
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 354-437 3.74e-03

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: 36.84  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785 354 IMDAPRDLNISEDRMAELKCRT--PPMSSVKWLLPNGTVLSHAsrhpRISVLNDGTLNFSRVLLIDTGVYTCmvtnVAGN 431
Cdd:cd20968    2 ITRPPTNVTIIEGLKAVLPCTTmgNPKPSVSWIKGDDLIKENN----RIAVLESGSLRIHNVQKEDAGQYRC----VAKN 73


                 ....*.
gi 124339785 432 SNASAY 437
Cdd:cd20968   74 SLGIAY 79
LRR_8 pfam13855
Leucine rich repeat;
74-110 3.83e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 3.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 124339785   74 SNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSI 110
Cdd:pfam13855  25 SNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 113-272 7.19e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 39.47  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  113 IEVGAFNGLASLNTLELFDNWLTV-------IPSGaFEYL-SKLRELWLRNNPIESIPSyAFnRVPSLMRLDLGElKKLE 184
Cdd:PLN03210  549 IHENAFKGMRNLLFLKFYTKKWDQkkevrwhLPEG-FDYLpPKLRLLRWDKYPLRCMPS-NF-RPENLVKLQMQG-SKLE 624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124339785  185 YISEGAFEgLFNLKYLNL-GMCNIKDMPNLTPLVGLEELEMSG-NHFPEIrPGSFHGLSSLKKLwVMNSQVSLIERNAFD 262
Cdd:PLN03210  625 KLWDGVHS-LTGLRNIDLrGSKNLKEIPDLSMATNLETLKLSDcSSLVEL-PSSIQYLNKLEDL-DMSRCENLEILPTGI 701

                         170
                  ....*....|
gi 124339785  263 GLASLVELNL 272
Cdd:PLN03210  702 NLKSLYRLNL 711
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 123-165 8.22e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.53  E-value: 8.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 124339785  123 SLNTLELFDNWLTVIPsgAFEYLSKLRELWL-RNNPIESIPSYA 165
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLsGNNKITDLSDLA 43
 
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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