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Conserved domains on  [gi|306482659|ref|NP_001182360|]
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immunoglobulin superfamily containing leucine-rich repeat protein precursor [Mus musculus]

Protein Classification

LRR and Ig domain-containing protein( domain architecture ID 11469616)

LRR and Ig domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-182 4.69e-21

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 4.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  51 NVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRSVAiGALAPLSHLKSLDLSHNLLSEFAwSDLHNLSALQLLKMD 130
Cdd:COG4886  137 NLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLS 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 306482659 131 SNELAFIPrDAFSSLSALRSLQLNHNRLHALAEgtFAPLTALSHLQINDNPF 182
Cdd:COG4886  214 GNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQL 262
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 153-227 5.30e-09

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


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 58.56  E-value: 5.30e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306482659   153 LNHNRLHALAEGTFAPLTALSHLQINDNPFDCTCGIVWFKTWALASAVSIPEQDNIACTTPHVLKGIPLGRLPPL 227
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLL 76
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 239-343 3.66e-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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  239 QPSQDgAELRPGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALpgalatSGQPRFQAFANG---SLLIP 315
Cdd:pfam07679   5 QKPKD-VEVQEGESARFTCTVTGTPDPEVSWF----------------KDGQPL------RSSDRFKVTYEGgtyTLTIS 61

                          90       100
                  ....*....|....*....|....*...
gi 306482659  316 DFGKLEEGTYSCLATNELGSAESSVNVA 343
Cdd:pfam07679  62 NVQPDDSGKYTCVATNSAGEAEASAELT 89
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-182 4.69e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 4.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  51 NVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRSVAiGALAPLSHLKSLDLSHNLLSEFAwSDLHNLSALQLLKMD 130
Cdd:COG4886  137 NLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLS 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 306482659 131 SNELAFIPrDAFSSLSALRSLQLNHNRLHALAEgtFAPLTALSHLQINDNPF 182
Cdd:COG4886  214 GNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQL 262
LRR_8 pfam13855
Leucine rich repeat;
98-158 3.08e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.39  E-value: 3.08e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 306482659   98 SHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNELAFIPRDAFSSLSALRSLQLNHNRL 158
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-180 1.72e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 63.33  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  52 VTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIrsvaIGALAPLS---HLKSLDLSHNLLSEFAWSDLHNLSALQLLK 128
Cdd:PLN00113 430 VYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDSFgskRLENLDLSRNQFSGAVPRKLGSLSELMQLK 505

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 306482659 129 MDSNELAFIPRDAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDN 180
Cdd:PLN00113 506 LSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQN 557
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 74-183 1.01e-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: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  74 PLLQSLWLAHNEIRSvaIGALAPLSHLKSLDLSHNLLSEFawSDLHNLSALQLLKMD------SNELAFIPRDAFSSLSA 147
Cdd:cd21340   46 TNLTHLYLQNNQIEK--IENLENLVNLKKLYLGGNRISVV--EGLENLTNLEELHIEnqrlppGEKLTFDPRSLAALSNS 121

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 306482659 148 LRSLQLNHNRLHALAEgtFAPLTALSHLQINDNPFD 183
Cdd:cd21340  122 LRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQIS 155
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 153-227 5.30e-09

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: 58.56  E-value: 5.30e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306482659   153 LNHNRLHALAEGTFAPLTALSHLQINDNPFDCTCGIVWFKTWALASAVSIPEQDNIACTTPHVLKGIPLGRLPPL 227
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLL 76
I-set pfam07679
Immunoglobulin I-set domain;
239-343 3.66e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  239 QPSQDgAELRPGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALpgalatSGQPRFQAFANG---SLLIP 315
Cdd:pfam07679   5 QKPKD-VEVQEGESARFTCTVTGTPDPEVSWF----------------KDGQPL------RSSDRFKVTYEGgtyTLTIS 61

                          90       100
                  ....*....|....*....|....*...
gi 306482659  316 DFGKLEEGTYSCLATNELGSAESSVNVA 343
Cdd:pfam07679  62 NVQPDDSGKYTCVATNSAGEAEASAELT 89
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 253-342 1.04e-07

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 49.49  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 253 LALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALPgalatsgQPRFQ-AFANGSLLIPD-FGKLEEGTYSCLAT 330
Cdd:cd20958   18 LRLHCPVAGYPISSITWE----------------KDGRRLP-------LNHRQrVFPNGTLVIENvQRSSDEGEYTCTAR 74

                         90
                 ....*....|...
gi 306482659 331 NELG-SAESSVNV 342
Cdd:cd20958   75 NQQGqSASRSVFV 87
LRRCT smart00082
Leucine rich repeat C-terminal domain;
180-228 1.34e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.11  E-value: 1.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 306482659   180 NPFDCTCGIVWFKTWALASaVSIPEQDNIACTTPHVLKGiPLGRLPPLP 228
Cdd:smart00082   1 NPFICDCELRWLLRWLQAN-EHLQDPVDLRCASPSSLRG-PLLELLHSE 47
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 248-342 9.48e-05

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: 40.95  E-value: 9.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659   248 RPGFVLALHCDVDGQPVPQLHWHIhtpGGTVEIASPnvgtdgralpgalatsgqPRFQAFANG---SLLIPDFGKLEEGT 324
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYK---QGGKLLAES------------------GRFSVSRSGstsTLTISNVTPEDSGT 65

                           90
                   ....*....|....*...
gi 306482659   325 YSCLATNELGSAESSVNV 342
Cdd:smart00410  66 YTCAATNSSGSASSGTTL 83
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-182 4.69e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 4.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  51 NVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRSVAiGALAPLSHLKSLDLSHNLLSEFAwSDLHNLSALQLLKMD 130
Cdd:COG4886  137 NLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLS 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 306482659 131 SNELAFIPrDAFSSLSALRSLQLNHNRLHALAEgtFAPLTALSHLQINDNPF 182
Cdd:COG4886  214 GNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-180 1.01e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 81.52  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  50 ANVTTLSLSANRlpglpegAFREVPLLQSLWLAHNEIRSVAIgALAPLSHLKSLDLSHNLLSEFAwSDLHNLSALQLLKM 129
Cdd:COG4886   96 TNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDL 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 306482659 130 DSNELAFIPrDAFSSLSALRSLQLNHNRLHALAEgTFAPLTALSHLQINDN 180
Cdd:COG4886  167 SNNQLTDLP-EELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGN 215
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-182 1.69e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 80.75  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  51 NVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRSVAiGALAPLSHLKSLDLSHNLLSEFAWsdLHNLSALQLLKMD 130
Cdd:COG4886  183 NLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLS 258

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 306482659 131 SNELAFIPrdAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDNPF 182
Cdd:COG4886  259 NNQLTDLP--PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
LRR_8 pfam13855
Leucine rich repeat;
98-158 3.08e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.39  E-value: 3.08e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 306482659   98 SHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNELAFIPRDAFSSLSALRSLQLNHNRL 158
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
51-110 1.70e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.08  E-value: 1.70e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659   51 NVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLL 110
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
74-134 1.15e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 1.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 306482659   74 PLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNEL 134
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
124-182 1.62e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.38  E-value: 1.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 306482659  124 LQLLKMDSNELAFIPRDAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDNPF 182
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-180 1.72e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 63.33  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  52 VTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIrsvaIGALAPLS---HLKSLDLSHNLLSEFAWSDLHNLSALQLLK 128
Cdd:PLN00113 430 VYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDSFgskRLENLDLSRNQFSGAVPRKLGSLSELMQLK 505

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 306482659 129 MDSNELAFIPRDAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDN 180
Cdd:PLN00113 506 LSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQN 557
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 74-183 1.01e-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: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  74 PLLQSLWLAHNEIRSvaIGALAPLSHLKSLDLSHNLLSEFawSDLHNLSALQLLKMD------SNELAFIPRDAFSSLSA 147
Cdd:cd21340   46 TNLTHLYLQNNQIEK--IENLENLVNLKKLYLGGNRISVV--EGLENLTNLEELHIEnqrlppGEKLTFDPRSLAALSNS 121

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 306482659 148 LRSLQLNHNRLHALAEgtFAPLTALSHLQINDNPFD 183
Cdd:cd21340  122 LRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQIS 155
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 153-227 5.30e-09

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: 58.56  E-value: 5.30e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306482659   153 LNHNRLHALAEGTFAPLTALSHLQINDNPFDCTCGIVWFKTWALASAVSIPEQDNIACTTPHVLKGIPLGRLPPL 227
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLL 76
I-set pfam07679
Immunoglobulin I-set domain;
239-343 3.66e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  239 QPSQDgAELRPGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALpgalatSGQPRFQAFANG---SLLIP 315
Cdd:pfam07679   5 QKPKD-VEVQEGESARFTCTVTGTPDPEVSWF----------------KDGQPL------RSSDRFKVTYEGgtyTLTIS 61

                          90       100
                  ....*....|....*....|....*...
gi 306482659  316 DFGKLEEGTYSCLATNELGSAESSVNVA 343
Cdd:pfam07679  62 NVQPDDSGKYTCVATNSAGEAEASAELT 89
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 253-342 1.04e-07

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 49.49  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 253 LALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALPgalatsgQPRFQ-AFANGSLLIPD-FGKLEEGTYSCLAT 330
Cdd:cd20958   18 LRLHCPVAGYPISSITWE----------------KDGRRLP-------LNHRQrVFPNGTLVIENvQRSSDEGEYTCTAR 74

                         90
                 ....*....|...
gi 306482659 331 NELG-SAESSVNV 342
Cdd:cd20958   75 NQQGqSASRSVFV 87
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 253-340 1.19e-06

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


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 46.54  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 253 LALHCDVDGQPVPQLHW---HIHTPGGTVEIASpnvgtdgralpgalatsgQPRFQAFANGSLLIPDFGKLEEGTYSCLA 329
Cdd:cd20954   19 VMLHCQADGFPTPTVTWkkaTGSTPGEYKDLLY------------------DPNVRILPNGTLVFGHVQKENEGHYLCEA 80

                         90
                 ....*....|.
gi 306482659 330 TNELGSAESSV 340
Cdd:cd20954   81 KNGIGSGLSKV 91
LRRCT smart00082
Leucine rich repeat C-terminal domain;
180-228 1.34e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.11  E-value: 1.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 306482659   180 NPFDCTCGIVWFKTWALASaVSIPEQDNIACTTPHVLKGiPLGRLPPLP 228
Cdd:smart00082   1 NPFICDCELRWLLRWLQAN-EHLQDPVDLRCASPSSLRG-PLLELLHSE 47
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 239-335 1.43e-06

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


Pssm-ID: 409387  Cd Length: 97  Bit Score: 46.32  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 239 QPSqDGAELRpGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGralpGALATSGQPRFQAFANGSLLIPDF- 317
Cdd:cd05722    7 EPS-DIVAMR-GGPVVLNCSAESDPPPKIEWK----------------KDG----VLLNLVSDERRQQLPNGSLLITSVv 64

                         90       100
                 ....*....|....*....|...
gi 306482659 318 ----GKLEEGTYSCLATNE-LGS 335
Cdd:cd05722   65 hskhNKPDEGFYQCVAQNEsLGS 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 255-339 1.45e-06

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: 45.40  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 255 LHCDVDGQPVPQLHWHIhtpggtveiaspnvgtDGRALPGalaTSGQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELG 334
Cdd:cd00096    3 LTCSASGNPPPTITWYK----------------NGKPLPP---SSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63


                 ....*
gi 306482659 335 SAESS 339
Cdd:cd00096   64 GSASA 68
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 43-159 3.45e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.46  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  43 GVPPGFPA-NVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNL 121
Cdd:PLN00113 467 GLPDSFGSkRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEM 546

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 306482659 122 SALQLLKMDSNELAF-IPRDaFSSLSALRSLQLNHNRLH 159
Cdd:PLN00113 547 PVLSQLDLSQNQLSGeIPKN-LGNVESLVQVNISHNHLH 584
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 242-343 4.46e-06

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: 44.79  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 242 QDGAE--LRPGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALPGAlatsgQPRFQAFANGSLLIPDFGK 319
Cdd:cd20952    4 QGPQNqtVAVGGTVVLNCQATGEPVPTISWL----------------KDGVPLLGK-----DERITTLENGSLQIKGAEK 62

                         90       100
                 ....*....|....*....|....
gi 306482659 320 LEEGTYSCLATNELGSAESSVNVA 343
Cdd:cd20952   63 SDTGEYTCVALNLSGEATWSAVLD 86
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 239-335 4.98e-06

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 44.79  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 239 QPS-QDGAElrpGFVLALHCDVDGQPVPQLHWHiHTPGGTVEIASPNVGTDGRAlpgalatsgqprfQAFANGSLLIPDF 317
Cdd:cd05734    7 QPNdQDGIY---GKAVVLNCSADGYPPPTIVWK-HSKGSGVPQFQHIVPLNGRI-------------QLLSNGSLLIKHV 69

                         90
                 ....*....|....*...
gi 306482659 318 GKLEEGTYSCLATNELGS 335
Cdd:cd05734   70 LEEDSGYYLCKVSNDVGA 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 246-342 6.07e-06

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: 44.50  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 246 ELRPGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALpgalatSGQPRFQAFANG---SLLIPDFGKLEE 322
Cdd:cd20972   12 EVAEGSKVRLECRVTGNPTPVVRWF----------------CEGKEL------QNSPDIQIHQEGdlhSLIIAEAFEEDT 69

                         90       100
                 ....*....|....*....|
gi 306482659 323 GTYSCLATNELGSAESSVNV 342
Cdd:cd20972   70 GRYSCLATNSVGSDTTSAEI 89
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 50-181 8.58e-06

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 47.35  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  50 ANVTTLSLSANRL-PGLPEG--AFREVPLLQSLWLAHNEI-----RSVAIGALAPLSHLKSLDLSHNLL---SEFAWSD- 117
Cdd:cd00116   81 CGLQELDLSDNALgPDGCGVleSLLRSSSLQELKLNNNGLgdrglRLLAKGLKDLPPALEKLVLGRNRLegaSCEALAKa 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306482659 118 LHNLSALQLLKMDSNEL--AFIPR--DAFSSLSALRSLQLNHNRLH-----ALAEgTFAPLTALSHLQINDNP 181
Cdd:cd00116  161 LRANRDLKELNLANNGIgdAGIRAlaEGLKANCNLEVLDLNNNGLTdegasALAE-TLASLKSLEVLNLGDNN 232
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-177 1.33e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.54  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  55 LSLSANRLPG-LPEGAfreVPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNE 133
Cdd:PLN00113 123 LNLSNNNFTGsIPRGS---IPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQ 199

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 306482659 134 L-AFIPRDafssLSALRSLQ---LNHNRLHALAEGTFAPLTALSHLQI 177
Cdd:PLN00113 200 LvGQIPRE----LGQMKSLKwiyLGYNNLSGEIPYEIGGLTSLNHLDL 243
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 255-331 6.21e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 6.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 306482659  255 LHCDVDGQPVPQLHWHIhtpggtveiaspnvgtDGRALPGalaTSGQPRFQAFANGSLLIPDFGKLEEGTYSCLATN 331
Cdd:pfam13927  21 LTCEATGSPPPTITWYK----------------NGEPISS---GSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 74-108 6.93e-05

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 39.92  E-value: 6.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 306482659   74 PLLQSLWLAHNEIRSvaIGALAPLSHLKSLDLSHN 108
Cdd:pfam12799   1 PNLEVLDLSNNQITD--IPPLAKLPNLETLDLSGN 33
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 248-342 9.48e-05

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: 40.95  E-value: 9.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659   248 RPGFVLALHCDVDGQPVPQLHWHIhtpGGTVEIASPnvgtdgralpgalatsgqPRFQAFANG---SLLIPDFGKLEEGT 324
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYK---QGGKLLAES------------------GRFSVSRSGstsTLTISNVTPEDSGT 65

                           90
                   ....*....|....*...
gi 306482659   325 YSCLATNELGSAESSVNV 342
Cdd:smart00410  66 YTCAATNSSGSASSGTTL 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 302-339 1.00e-04

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: 40.91  E-value: 1.00e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 306482659 302 PRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSAESS 339
Cdd:cd04969   47 SRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANST 84
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 22-182 1.38e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.45  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  22 PCDCGEKYGFQIADCAYRDLEGVPPGFPANVTTL---SLSANRLPGlpeGAFREVPLLQSL---WLAHNEIRS---VAIG 92
Cdd:PLN00113 157 PNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLeflTLASNQLVG---QIPRELGQMKSLkwiYLGYNNLSGeipYEIG 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  93 ALAPLSHLkslDLSHNLLSEFAWSDLHNLSALQLLKMDSNELAF-IPRDAFsSLSALRSLQLNHNRLHALAEGTFAPLTA 171
Cdd:PLN00113 234 GLTSLNHL---DLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGpIPPSIF-SLQKLISLDLSDNSLSGEIPELVIQLQN 309

                        170
                 ....*....|.
gi 306482659 172 LSHLQINDNPF 182
Cdd:PLN00113 310 LEILHLFSNNF 320
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 76-156 1.47e-04

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: 42.85  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  76 LQSLWLAHNEIRSvaIGALAPLSHLKSLDLSHNLLSEFawsdlhnlsalqllkmdsNELAfiprDAFSSLSALRSLQLNH 155
Cdd:cd21340  122 LRVLNISGNNIDS--LEPLAPLRNLEQLDASNNQISDL------------------EELL----DLLSSWPSLRELDLTG 177


                 .
gi 306482659 156 N 156
Cdd:cd21340  178 N 178
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-182 2.43e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.68  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  55 LSLSANRLPG-LPEgAFREvPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNE 133
Cdd:PLN00113 457 LSLARNKFFGgLPD-SFGS-KRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQ 534

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 306482659 134 LA-FIPrDAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDNPF 182
Cdd:PLN00113 535 LSgQIP-ASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHL 583
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 254-342 4.54e-04

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: 39.00  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 254 ALHCDVDGQPVPQLHWhihtpggtveiaspnVGTDGRALPGAlatsgqPRFQAFANGSLLIPDFGKLEEGTYSCLATNEL 333
Cdd:cd05764   19 TLRCKARGDPEPAIHW---------------ISPEGKLISNS------SRTLVYDNGTLDILITTVKDTGAFTCIASNPA 77


                 ....*....
gi 306482659 334 GSAESSVNV 342
Cdd:cd05764   78 GEATARVEL 86
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 246-342 4.91e-04

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 38.93  E-value: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 246 ELRpGFVLALHCDVDGQPVPQLHWhihtpggtveiaspnvgtdgRALPGALAtSGQPRFQAFaNGSLLIPDFGKLEEGTY 325
Cdd:cd05731    7 VLR-GGVLLLECIAEGLPTPDIRW--------------------IKLGGELP-KGRTKFENF-NKTLKIENVSEADSGEY 63

                         90
                 ....*....|....*..
gi 306482659 326 SCLATNELGSAESSVNV 342
Cdd:cd05731   64 QCTASNTMGSARHTISV 80
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 255-342 5.15e-04

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: 38.91  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 255 LHCDVDGQPVPQLHWhIHtpggtveiaspnvgtDGRALpgalaTSGQPRFQaFANGSLLIPDFGKLEEGTYSCLATNELG 334
Cdd:cd20978   21 LPCQVTGVPQPKITW-LH---------------NGKPL-----QGPMERAT-VEDGTLTIINVQPEDTGYYGCVATNEIG 78


                 ....*...
gi 306482659 335 SAESSVNV 342
Cdd:cd20978   79 DIYTETLL 86
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 254-342 5.54e-04

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 38.77  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 254 ALHCDVDGQPVPQLHWHIhtpggtveiaspnvgtDGRALPGALAtsgqpRFQAFAN-GSLLIPDFGKLEEGTYSCLATNE 332
Cdd:cd20976   20 VAQCSARGKPVPRITWIR----------------NAQPLQYAAD-----RSTCEAGvGELHIQDVLPEDHGTYTCLAKNA 78

                         90
                 ....*....|
gi 306482659 333 LGSAESSVNV 342
Cdd:cd20976   79 AGQVSCSAWV 88
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 250-334 1.23e-03

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 37.91  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 250 GFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvGTDGRALPGALATSgqprfqafANGSLLIPDFGKLEEGTYSCLA 329
Cdd:cd04968   16 GQTVTLECFALGNPVPQIKWR---------------KVDGSPSSQWEITT--------SEPVLEIPNVQFEDEGTYECEA 72


                 ....*
gi 306482659 330 TNELG 334
Cdd:cd04968   73 ENSRG 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-182 1.37e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  48 FPANVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNLSALQLL 127
Cdd:COG4886   22 TTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTEL 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 306482659 128 KMDSNElafiprdAFSSLSALRSLQLNHNRLHALAEgTFAPLTALSHLQINDNPF 182
Cdd:COG4886  102 DLSGNE-------ELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQL 148
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 98-182 1.66e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.99  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  98 SHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNELAF-IPRDAFSSLSALRSLQLNHNRLHALAEGTFAPLtaLSHLQ 176
Cdd:PLN00113  69 SRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGpIPDDIFTTSSSLRYLNLSNNNFTGSIPRGSIPN--LETLD 146


                 ....*.
gi 306482659 177 INDNPF 182
Cdd:PLN00113 147 LSNNML 152
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 301-340 1.69e-03

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 37.38  E-value: 1.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 306482659 301 QPRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSAESSV 340
Cdd:cd05724   43 NERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESRA 82
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 245-349 1.76e-03

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 37.60  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 245 AELRPGFVLALHCDVDGQPVPQLHWHihtpggtveiaspnvgTDGRALP---GALATSGQPRfqafangSLLIPDFGKLE 321
Cdd:cd05760   11 AEIQPSSRVTLRCHIDGHPRPTYQWF----------------RDGTPLSdgqGNYSVSSKER-------TLTLRSAGPDD 67

                         90       100
                 ....*....|....*....|....*...
gi 306482659 322 EGTYSCLATNELGSAESSVNVALATPGE 349
Cdd:cd05760   68 SGLYYCCAHNAFGSVCSSQNFTLSIIDE 95
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 38-158 2.56e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  38 YRDLEGVPP---GFPANVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFA 114
Cdd:PLN00113 221 YNNLSGEIPyeiGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEI 300

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 306482659 115 WSDLHNLSALQLLKMDSNEL-AFIPRdAFSSLSALRSLQLNHNRL 158
Cdd:PLN00113 301 PELVIQLQNLEILHLFSNNFtGKIPV-ALTSLPRLQVLQLWSNKF 344
PLN03150 PLN03150
hypothetical protein; Provisional
 76-135 4.02e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 39.41  E-value: 4.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659  76 LQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNELA 135
Cdd:PLN03150 444 LQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLS 503
PLN03150 PLN03150
hypothetical protein; Provisional
 103-180 5.00e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 39.03  E-value: 5.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306482659 103 LDLSHNLLSEFAWSDLHNLSALQLLKMDSNELAFIPRDAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDN 180
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGN 500
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 257-339 8.27e-03

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


Pssm-ID: 409388  Cd Length: 84  Bit Score: 35.25  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306482659 257 CDVDGQPVPQLHWhihTPGGTVEIASPnvgtdgralpgalatsgqpRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSA 336
Cdd:cd05723   19 CEVTGKPTPTVKW---VKNGDVVIPSD-------------------YFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNA 76


                 ...
gi 306482659 337 ESS 339
Cdd:cd05723   77 QAS 79
 
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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