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Conserved domains on  [gi|672059488|ref|XP_008763803|]
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leucine-rich repeat-containing protein 24 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
267-357 3.35e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 70.67  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPQaqvqleggAPGLGGHATRDTGSGMLFLTNITLA 346
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYK-----NGEPI--------SSGSTRSRSLSGSNSTLTISNVTRS 67
                          90
                  ....*....|.
gi 672059488  347 HAGKYECEATN 357
Cdd:pfam13927  68 DAGTYTCVASN 78
LRR_8 pfam13855
Leucine rich repeat;
84-142 8.07e-14

Leucine rich repeat;


:

Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 66.01  E-value: 8.07e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672059488   84 LRHLYLHNNTLRALESGAFRAQPRLLELALTGNRLRGLRGGAFVGLVQLRVLYLAGNQL 142
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-213 1.38e-12

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgALAPLAALRHLYLHNNTLRALeSGAFRAQPRLLELALTGNRLRGLrGGAFVGLVQLRVLYLAGN 140
Cdd:COG4886  162 KSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNN 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672059488 141 QLAKLLDFTflHLPRLQELHLQENsielledqalaglsslalldlsrnQLGTISKEAlqPLSSLQVLRLTENP 213
Cdd:COG4886  239 QLTDLPELG--NLTNLEELDLSNN------------------------QLTDLPPLA--NLTNLKTLDLSNNQ 283
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
188-259 1.03e-08

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: 58.17  E-value: 1.03e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672059488   188 NQLGTISKEALQPLSSLQVLRLTENPWRCDCALHWLGSWIKEGGRRLLssRDKKITCAEPPRLALQSLLEVS 259
Cdd:TIGR00864    5 NKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVR--QPEAALCAGPGALAGQPLLGIP 74
 
Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
267-357 3.35e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 70.67  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPQaqvqleggAPGLGGHATRDTGSGMLFLTNITLA 346
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYK-----NGEPI--------SSGSTRSRSLSGSNSTLTISNVTRS 67
                          90
                  ....*....|.
gi 672059488  347 HAGKYECEATN 357
Cdd:pfam13927  68 DAGTYTCVASN 78
LRR_8 pfam13855
Leucine rich repeat;
84-142 8.07e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 66.01  E-value: 8.07e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672059488   84 LRHLYLHNNTLRALESGAFRAQPRLLELALTGNRLRGLRGGAFVGLVQLRVLYLAGNQL 142
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-213 1.38e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgALAPLAALRHLYLHNNTLRALeSGAFRAQPRLLELALTGNRLRGLrGGAFVGLVQLRVLYLAGN 140
Cdd:COG4886  162 KSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNN 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672059488 141 QLAKLLDFTflHLPRLQELHLQENsielledqalaglsslalldlsrnQLGTISKEAlqPLSSLQVLRLTENP 213
Cdd:COG4886  239 QLTDLPELG--NLTNLEELDLSNN------------------------QLTDLPPLA--NLTNLKTLDLSNNQ 283
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
63-212 4.45e-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: 4.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  63 LFLQDNSIAHLEqgALAPLAALRHLYLHNNTLRALESgaFRAQPRLLELALTGNRLRGLRGgaFVGLVQLRVLYLAGNQL 142
Cdd:cd21340    7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672059488 143 AKL--LDftflHLPRLQELHLQENSI----ELLEDQALAGLSSLALLD--LSRNQLGTIskEALQPLSSLQVLRLTEN 212
Cdd:cd21340   81 SVVegLE----NLTNLEELHIENQRLppgeKLTFDPRSLAALSNSLRVlnISGNNIDSL--EPLAPLRNLEQLDASNN 152
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
274-370 6.90e-12

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: 61.37  E-value: 6.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488   274 PPELTANLGEDLQVACQASGYPQPLVVWRKmlqprdgkpQAQVQLeggAPGLGGHATRDTGSGMLFLTNITLAHAGKYEC 353
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYK---------QGGKLL---AESGRFSVSRSGSTSTLTISNVTPEDSGTYTC 68
                           90
                   ....*....|....*..
gi 672059488   354 EATNAGGKARVLFHLLV 370
Cdd:smart00410  69 AATNSSGSASSGTTLTV 85
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
267-360 8.59e-12

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: 61.56  E-value: 8.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKMLqprdgkpqaqvqleGGAPG-----LGGHATRDTGSGMLFLT 341
Cdd:cd20954    1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKAT--------------GSTPGeykdlLYDPNVRILPNGTLVFG 66
                         90
                 ....*....|....*....
gi 672059488 342 NITLAHAGKYECEATNAGG 360
Cdd:cd20954   67 HVQKENEGHYLCEAKNGIG 85
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
63-166 5.59e-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: 56.33  E-value: 5.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  63 LFLQDNSIAHLEQgaLAPLAALRHLYLHNNTLRALESgaFRAQPRLLEL------------------------------A 112
Cdd:cd21340   51 LYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVEG--LENLTNLEELhienqrlppgekltfdprslaalsnslrvlN 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672059488 113 LTGNRLRGLRGgaFVGLVQLRVLYLAGNQLAKLLDFTFL--HLPRLQELHLQENSI 166
Cdd:cd21340  127 ISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEELLDLlsSWPSLRELDLTGNPV 180
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
188-259 1.03e-08

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: 58.17  E-value: 1.03e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672059488   188 NQLGTISKEALQPLSSLQVLRLTENPWRCDCALHWLGSWIKEGGRRLLssRDKKITCAEPPRLALQSLLEVS 259
Cdd:TIGR00864    5 NKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVR--QPEAALCAGPGALAGQPLLGIP 74
LRRCT smart00082
Leucine rich repeat C-terminal domain;
212-265 1.06e-07

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 48.58  E-value: 1.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 672059488   212 NPWRCDCALHWLGSWIKEGGRRLLSSRdkkITCAEPPRLALQsLLEVSGGSLIC 265
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVD---LRCASPSSLRGP-LLELLHSEFKC 50
LRR_8 pfam13855
Leucine rich repeat;
131-213 6.72e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  131 QLRVLYLAGNQLAKLLDFTFLHLPRLQELHLqensielledqalaglsslalldlSRNQLGTISKEALQPLSSLQVLRLT 210
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDL------------------------SNNLLTTLSPGAFSGLPSLRYLDLS 57

                  ...
gi 672059488  211 ENP 213
Cdd:pfam13855  58 GNR 60
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-165 2.39e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgaLAPLAALRHLYLHNNTLRALESGAfrAQPRLLELALTGNRLRGLRGGAFVGLVQLRVLYLAGN 140
Cdd:COG4886  231 ETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306
                         90       100
                 ....*....|....*....|....*
gi 672059488 141 QLAKLLDFTFLHLPRLQELHLQENS 165
Cdd:COG4886  307 LLNLLELLILLLLLTTLLLLLLLLK 331
 
Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
267-357 3.35e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 70.67  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPQaqvqleggAPGLGGHATRDTGSGMLFLTNITLA 346
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYK-----NGEPI--------SSGSTRSRSLSGSNSTLTISNVTRS 67
                          90
                  ....*....|.
gi 672059488  347 HAGKYECEATN 357
Cdd:pfam13927  68 DAGTYTCVASN 78
LRR_8 pfam13855
Leucine rich repeat;
84-142 8.07e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 66.01  E-value: 8.07e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672059488   84 LRHLYLHNNTLRALESGAFRAQPRLLELALTGNRLRGLRGGAFVGLVQLRVLYLAGNQL 142
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-213 1.38e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgALAPLAALRHLYLHNNTLRALeSGAFRAQPRLLELALTGNRLRGLrGGAFVGLVQLRVLYLAGN 140
Cdd:COG4886  162 KSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNN 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672059488 141 QLAKLLDFTflHLPRLQELHLQENsielledqalaglsslalldlsrnQLGTISKEAlqPLSSLQVLRLTENP 213
Cdd:COG4886  239 QLTDLPELG--NLTNLEELDLSNN------------------------QLTDLPPLA--NLTNLKTLDLSNNQ 283
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
63-212 4.45e-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: 4.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  63 LFLQDNSIAHLEqgALAPLAALRHLYLHNNTLRALESgaFRAQPRLLELALTGNRLRGLRGgaFVGLVQLRVLYLAGNQL 142
Cdd:cd21340    7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672059488 143 AKL--LDftflHLPRLQELHLQENSI----ELLEDQALAGLSSLALLD--LSRNQLGTIskEALQPLSSLQVLRLTEN 212
Cdd:cd21340   81 SVVegLE----NLTNLEELHIENQRLppgeKLTFDPRSLAALSNSLRVlnISGNNIDSL--EPLAPLRNLEQLDASNN 152
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
274-370 6.90e-12

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: 61.37  E-value: 6.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488   274 PPELTANLGEDLQVACQASGYPQPLVVWRKmlqprdgkpQAQVQLeggAPGLGGHATRDTGSGMLFLTNITLAHAGKYEC 353
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYK---------QGGKLL---AESGRFSVSRSGSTSTLTISNVTPEDSGTYTC 68
                           90
                   ....*....|....*..
gi 672059488   354 EATNAGGKARVLFHLLV 370
Cdd:smart00410  69 AATNSSGSASSGTTLTV 85
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
267-360 8.59e-12

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: 61.56  E-value: 8.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKMLqprdgkpqaqvqleGGAPG-----LGGHATRDTGSGMLFLT 341
Cdd:cd20954    1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKAT--------------GSTPGeykdlLYDPNVRILPNGTLVFG 66
                         90
                 ....*....|....*....
gi 672059488 342 NITLAHAGKYECEATNAGG 360
Cdd:cd20954   67 HVQKENEGHYLCEAKNGIG 85
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-212 2.74e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.34  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgALAPLAALRHLYLHNNTLRALeSGAFRAQPRLLELALTGNRLRGLRggAFVGLVQLRVLYLAGN 140
Cdd:COG4886  185 KELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNN 260
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672059488 141 QLAKLldFTFLHLPRLQELHLQENSIELLEDQALAGLSSLALLDLSRNQLGTISKEALQPLSSLQVLRLTEN 212
Cdd:COG4886  261 QLTDL--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLL 330
LRR_8 pfam13855
Leucine rich repeat;
106-166 1.18e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.15  E-value: 1.18e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059488  106 PRLLELALTGNRLRGLRGGAFVGLVQLRVLYLAGNQLAKLLDFTFLHLPRLQELHLQENSI 166
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
I-set pfam07679
Immunoglobulin I-set domain;
268-370 2.81e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.88  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  268 PSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPQAqvqleggaPGLGGHATRDTGSGMLFLTNITLAH 347
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK-----DGQPLR--------SSDRFKVTYEGGTYTLTISNVQPDD 67
                          90       100
                  ....*....|....*....|...
gi 672059488  348 AGKYECEATNAGGKARVLFHLLV 370
Cdd:pfam07679  68 SGKYTCVATNSAGEAEASAELTV 90
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
267-372 5.96e-10

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 56.09  E-value: 5.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 267 PPSVNAEPPEL--TANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPQAQvqleggapGLGGHATRDTGSGMLFLtNIT 344
Cdd:cd05730    1 PPTIRARQSEVnaTANLGQSVTLACDADGFPEPTMTWTK-----DGEPIES--------GEEKYSFNEDGSEMTIL-DVD 66
                         90       100
                 ....*....|....*....|....*...
gi 672059488 345 LAHAGKYECEATNAGGKARVLFHLLVNA 372
Cdd:cd05730   67 KLDEAEYTCIAENKAGEQEAEIHLKVFA 94
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
77-212 2.27e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  77 ALAPLAALRHLYLHNNTLRALESgAFRAQPRLLELALTGNRLRGLrGGAFVGLVQLRVLYLAGNQLAKlLDFTFLHLPRL 156
Cdd:COG4886  108 ELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNL 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672059488 157 QELHLQENSIE---------------LLEDqalaglsslalldlsrNQLGTISkEALQPLSSLQVLRLTEN 212
Cdd:COG4886  185 KELDLSNNQITdlpeplgnltnleelDLSG----------------NQLTDLP-EPLANLTNLETLDLSNN 238
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
63-166 5.59e-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: 56.33  E-value: 5.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  63 LFLQDNSIAHLEQgaLAPLAALRHLYLHNNTLRALESgaFRAQPRLLEL------------------------------A 112
Cdd:cd21340   51 LYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVEG--LENLTNLEELhienqrlppgekltfdprslaalsnslrvlN 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672059488 113 LTGNRLRGLRGgaFVGLVQLRVLYLAGNQLAKLLDFTFL--HLPRLQELHLQENSI 166
Cdd:cd21340  127 ISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEELLDLlsSWPSLRELDLTGNPV 180
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
61-213 6.49e-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: 56.33  E-value: 6.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgaLAPLAALRHLYLHNNTLRALESgaFRAQPRLLELALTGNRLR---GLRGgafvgLVQLRVLYL 137
Cdd:cd21340   27 KVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISvveGLEN-----LTNLEELHI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 138 AGNQLAKLLDFTF------LHLPRLQELHLQENSIELLEDqaLAGLSSLALLDLSRNQLGTIS--KEALQPLSSLQVLRL 209
Cdd:cd21340   98 ENQRLPPGEKLTFdprslaALSNSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEelLDLLSSWPSLRELDL 175

                 ....
gi 672059488 210 TENP 213
Cdd:cd21340  176 TGNP 179
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
279-370 8.58e-09

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. 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 structures of the titin-A168169 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: 409563  Cd Length: 93  Bit Score: 52.86  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 279 ANLGEDLQVACQASGYPQPLVVWRKMLQPrdgkpqaqvqleggAPGLGGHATRDT--GSGMLFLTNITL-AHAGKYECEA 355
Cdd:cd20971   13 VRYQSNATLVCKVTGHPKPIVKWYRQGKE--------------IIADGLKYRIQEfkGGYHQLIIASVTdDDATVYQVRA 78
                         90
                 ....*....|....*
gi 672059488 356 TNAGGKARVLFHLLV 370
Cdd:cd20971   79 TNQGGSVSGTASLEV 93
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
268-367 9.92e-09

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 52.55  E-value: 9.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 268 PSVNAE-PPELTANLGEDLQVACQASGYPQPLVVWRKMlqprDGKPQAQvqleggapglgghATRDTGSGMLFLTNITLA 346
Cdd:cd04968    1 PSIKVRfPADTYALKGQTVTLECFALGNPVPQIKWRKV----DGSPSSQ-------------WEITTSEPVLEIPNVQFE 63
                         90       100
                 ....*....|....*....|....*
gi 672059488 347 HAGKYECEATNAGGK----ARVLFH 367
Cdd:cd04968   64 DEGTYECEAENSRGKdtvqGRIIVQ 88
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
188-259 1.03e-08

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: 58.17  E-value: 1.03e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672059488   188 NQLGTISKEALQPLSSLQVLRLTENPWRCDCALHWLGSWIKEGGRRLLssRDKKITCAEPPRLALQSLLEVS 259
Cdd:TIGR00864    5 NKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVR--QPEAALCAGPGALAGQPLLGIP 74
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
273-372 1.32e-08

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: 52.07  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 273 EPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPqaqVQLEGGAPGLGGHatRDTgsgmLFLTNITLAHAGKYE 352
Cdd:cd04978    5 EPPSLVLSPGETGELICEAEGNPQPTITWRL-----NGVP---IEPAPEDMRRTVD--GRT----LIFSNLQPNDTAVYQ 70
                         90       100
                 ....*....|....*....|
gi 672059488 353 CEATNAGGkarvlfHLLVNA 372
Cdd:cd04978   71 CNASNVHG------YLLANA 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
289-363 1.76e-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: 51.18  E-value: 1.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672059488 289 CQASGYPQPLVVWRKmlqprDGKPQAQVQLEGGapglgghaTRDTGSGMLFLTNITLAHAGKYECEATNAGGKAR 363
Cdd:cd00096    5 CSASGNPPPTITWYK-----NGKPLPPSSRDSR--------RSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
267-361 9.39e-08

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


Pssm-ID: 143259  Cd Length: 88  Bit Score: 49.63  E-value: 9.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKMLQPRDGkpQAQVQLEGgapglgghatrdtgsGMLFLTNITLA 346
Cdd:cd05851    1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPA--TAEISMSG---------------AVLKIFNIQPE 63
                         90
                 ....*....|....*
gi 672059488 347 HAGKYECEATNAGGK 361
Cdd:cd05851   64 DEGTYECEAENIKGK 78
LRRCT smart00082
Leucine rich repeat C-terminal domain;
212-265 1.06e-07

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 48.58  E-value: 1.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 672059488   212 NPWRCDCALHWLGSWIKEGGRRLLSSRdkkITCAEPPRLALQsLLEVSGGSLIC 265
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVD---LRCASPSSLRGP-LLELLHSEFKC 50
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
268-361 5.12e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.39  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  268 PSVNAEPPELTAnlGEDLQVACQASGYPQPLVVWRKmlqprdgkpqaqvqleggapglGGHATRDTGSgmLFLTNITLAH 347
Cdd:pfam13895   2 PVLTPSPTVVTE--GEPVTLTCSAPGNPPPSYTWYK----------------------DGSAISSSPN--FFTLSVSAED 55
                          90
                  ....*....|....
gi 672059488  348 AGKYECEATNAGGK 361
Cdd:pfam13895  56 SGTYTCVARNGRGG 69
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
282-370 1.23e-06

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: 46.08  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 282 GEDLQVACQASGYPQPLVVWRKmlqprdgkpqaqvqleGGAPGLGGHATRDTGSGMLFLTNITLAHAGKYECEATNAGGK 361
Cdd:cd05745    2 GQTVDFLCEAQGYPQPVIAWTK----------------GGSQLSVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGS 65

                 ....*....
gi 672059488 362 ARVLFHLLV 370
Cdd:cd05745   66 QRTVAQLTV 74
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
267-362 1.39e-06

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: 46.47  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRkmlqpRDGKPqaqVQLEggapglGGHATRDTGSGMLFLTNITLA 346
Cdd:cd20976    1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWI-----RNAQP---LQYA------ADRSTCEAGVGELHIQDVLPE 66
                         90
                 ....*....|....*.
gi 672059488 347 HAGKYECEATNAGGKA 362
Cdd:cd20976   67 DHGTYTCLAKNAAGQV 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
273-362 1.47e-06

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.42  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  273 EPPELTANLGEDLQVACQAS-GYPQPLVVWRKMLQprdgkpqaqvQLEGGApgLGGHATRDTGSGMLFLTNITLAHAGKY 351
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGG----------TLIESL--KVKHDNGRTTQSSLLISNVTKEDAGTY 69
                          90
                  ....*....|.
gi 672059488  352 ECEATNAGGKA 362
Cdd:pfam00047  70 TCVVNNPGGSA 80
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
269-362 1.64e-06

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 269 SVNAEPPELTANLGEDLQVACQASGYPQPLVVWRkmlqpRDGK-PQAQVQleggapglgGHATRDTGSgMLFLTNITLAH 347
Cdd:cd20970    4 STPQPSFTVTAREGENATFMCRAEGSPEPEISWT-----RNGNlIIEFNT---------RYIVRENGT-TLTIRNIRRSD 68
                         90
                 ....*....|....*.
gi 672059488 348 AGKYECEATN-AGGKA 362
Cdd:cd20970   69 MGIYLCIASNgVPGSV 84
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
81-170 2.05e-06

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: 48.63  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  81 LAALRHLYLHNNTLRALEsgAFRAQPRLLELALTGNRLRGLRGgaFVGLVQLRVLYLAGNQLAKLLDFTflHLPRLQELH 160
Cdd:cd21340    1 LKRITHLYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIENLE--NLVNLKKLY 74
                         90
                 ....*....|
gi 672059488 161 LQENSIELLE 170
Cdd:cd21340   75 LGGNRISVVE 84
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
289-360 2.63e-06

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


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 45.77  E-value: 2.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672059488 289 CQASGYPQPLVVWRKMLQPRDgkpqaqvqleggaPGLGGHATRDTGSGMLFLTNITLAHAGKYECEATNAGG 360
Cdd:cd05738   21 CAASGNPDPEISWFKDFLPVD-------------TATSNGRIKQLRSGALQIENSEESDQGKYECVATNSAG 79
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
268-370 4.95e-06

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


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 45.23  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 268 PSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKMLQPRDGKPQAQVQLEGGapglgghaTRDTGSGMLFLTNITLAH 347
Cdd:cd05765    1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQVPGKENLIMRPNHVRGN--------VVVTNIGQLVIYNAQPQD 72
                         90       100
                 ....*....|....*....|...
gi 672059488 348 AGKYECEATNAGGKARVLFHLLV 370
Cdd:cd05765   73 AGLYTCTARNSGGLLRANFPLSV 95
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
282-370 5.47e-06

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 282 GEDLQVACQASGYPQPLVVWRKMlqprdgkpqaqvqlegGAPGLGGHATRDTGSGMLFLTNITLAHAGKYECEATNAGGK 361
Cdd:cd05731   10 GGVLLLECIAEGLPTPDIRWIKL----------------GGELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGS 73

                 ....*....
gi 672059488 362 ARVLFHLLV 370
Cdd:cd05731   74 ARHTISVTV 82
LRR_8 pfam13855
Leucine rich repeat;
131-213 6.72e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  131 QLRVLYLAGNQLAKLLDFTFLHLPRLQELHLqensielledqalaglsslalldlSRNQLGTISKEALQPLSSLQVLRLT 210
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDL------------------------SNNLLTTLSPGAFSGLPSLRYLDLS 57

                  ...
gi 672059488  211 ENP 213
Cdd:pfam13855  58 GNR 60
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
279-360 7.82e-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: 44.13  E-value: 7.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 279 ANLGEDLQVACQASGYPQPLVVWRkmlqpRDGKP---QAQVQLEGGApglgghatrdtgsgmLFLTNITLAHAGKYECEA 355
Cdd:cd05728   11 ADIGSSLRWECKASGNPRPAYRWL-----KNGQPlasENRIEVEAGD---------------LRITKLSLSDSGMYQCVA 70

                 ....*
gi 672059488 356 TNAGG 360
Cdd:cd05728   71 ENKHG 75
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
268-370 1.10e-05

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: 43.92  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 268 PSVNAEPPELT-ANLGEDLQVACQASGYPQPLVVWRkmlqpRDGKPqaqvqLEGGAPglgghaTRDTGSGMLFLTNITLA 346
Cdd:cd20978    1 PKFIQKPEKNVvVKGGQDVTLPCQVTGVPQPKITWL-----HNGKP-----LQGPME------RATVEDGTLTIINVQPE 64
                         90       100
                 ....*....|....*....|....
gi 672059488 347 HAGKYECEATNAGGKARVLFHLLV 370
Cdd:cd20978   65 DTGYYGCVATNEIGDIYTETLLHV 88
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
282-360 2.33e-05

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 42.48  E-value: 2.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672059488 282 GEDLQVACQASGYPQPLVVWRKMLQPRDGKPQAQVQLEGgapglgghatrdtGSGMLFLTNITLAHAGKYECEATNAGG 360
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEG-------------GYGTLTIRDVKESDQGAYTCEAINTRG 66
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
282-362 2.70e-05

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.83  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 282 GEDLQVACQASGYPQPLVVWRKmlqprdgkpqaqvqleggapglGGHATRDTG------SGMLFLTNITLAHAGKYECEA 355
Cdd:cd04969   17 GGDVIIECKPKASPKPTISWSK----------------------GTELLTNSSricilpDGSLKIKNVTKSDEGKYTCFA 74

                 ....*..
gi 672059488 356 TNAGGKA 362
Cdd:cd04969   75 VNFFGKA 81
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
273-364 4.09e-05

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: 42.10  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 273 EPPELTANLGEDLQVACQASGYPQPLVVWRKMLQPRDGKPQAQVQLEGGApglgghatrdtgsgmLFLTNITLAHAGKYE 352
Cdd:cd20952    5 GPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGS---------------LQIKGAEKSDTGEYT 69
                         90
                 ....*....|..
gi 672059488 353 CEATNAGGKARV 364
Cdd:cd20952   70 CVALNLSGEATW 81
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
273-362 5.00e-05

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: 42.00  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 273 EPPELTANLGEDLQVACQASGYPQPLVVWRKmlqpRDGK-PQAQVQLeggapglgghatRDTGSgmLFLTNITLAHAGKY 351
Cdd:cd05725    3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRK----EDGElPKGRYEI------------LDDHS--LKIRKVTAGDMGSY 64
                         90
                 ....*....|.
gi 672059488 352 ECEATNAGGKA 362
Cdd:cd05725   65 TCVAENMVGKI 75
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
266-370 7.00e-05

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: 41.41  E-value: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 266 IPPSVNAEPPEltanlGEDLQVACQASGYPQPLVVWRKMLQPRdgKPQAQVQLEGGAPGLGGhatrdtgsgmLFLTNITL 345
Cdd:cd20973    1 IQTLRDKEVVE-----GSAARFDCKVEGYPDPEVKWMKDDNPI--VESRRFQIDQDEDGLCS----------LIISDVCG 63
                         90       100
                 ....*....|....*....|....*
gi 672059488 346 AHAGKYECEATNAGGKARVLFHLLV 370
Cdd:cd20973   64 DDSGKYTCKAVNSLGEATCSAELTV 88
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
274-360 1.15e-04

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


Pssm-ID: 409444  Cd Length: 105  Bit Score: 41.48  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 274 PPELTANLGEDLQVACQASGYPQPLVVWRKMLQPR------DGKPQAQVQLEGGApglgghATRDTGSGMLFLTNITLAH 347
Cdd:cd05858    8 PANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNgskygpDGLPYVEVLKTAGV------NTTDKEIEVLYLRNVTFED 81
                         90
                 ....*....|...
gi 672059488 348 AGKYECEATNAGG 360
Cdd:cd05858   82 AGEYTCLAGNSIG 94
LRR_8 pfam13855
Leucine rich repeat;
48-92 1.21e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 1.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 672059488   48 RLRVVPPGI---PPGTQTLFLQDNSIAHLEQGALAPLAALRHLYLHNN 92
Cdd:pfam13855  12 RLTSLDDGAfkgLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
282-372 1.24e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 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.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 41.03  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 282 GEDLQVACQASGYPQPLVVWRKmlqprDGKPQAqvqleggapGLGGHATRDTGSGMLFLTNITLAHAGKYECEATNAGGk 361
Cdd:cd05867   14 GETARLDCQVEGIPTPNITWSI-----NGAPIE---------GTDPDPRRHVSSGALILTDVQPSDTAVYQCEARNRHG- 78
                         90
                 ....*....|.
gi 672059488 362 arvlfHLLVNA 372
Cdd:cd05867   79 -----NLLANA 84
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
278-360 1.52e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 40.97  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 278 TANLGEDLQVACQASGYPQPLVVWR---KMLQPRDGKPQAQVQLEGgapglgghatrDTGSGMLFLTNITLAHAGKYECE 354
Cdd:cd05732   12 TAVELEQITLTCEAEGDPIPEITWRratRGISFEEGDLDGRIVVRG-----------HARVSSLTLKDVQLTDAGRYDCE 80

                 ....*.
gi 672059488 355 ATNAGG 360
Cdd:cd05732   81 ASNRIG 86
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
268-363 1.85e-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: 40.61  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 268 PSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKPqaqvqLEGGAPGLGGHATRDTGSGMLFLTNI---- 343
Cdd:cd07693    1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLK-----NGQP-----LETDKDDPRSHRIVLPSGSLFFLRVVhgrk 70
                         90       100
                 ....*....|....*....|
gi 672059488 344 TLAHAGKYECEATNAGGKAR 363
Cdd:cd07693   71 GRSDEGVYVCVAHNSLGEAV 90
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
275-362 2.20e-04

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: 40.24  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 275 PELTANLGEDLQVACQASGYPQPLVVWRkmlqpRDGKPQAqvqlEGGAPGLGGHATRDtGSGMLFL--TNITLAHAGKYE 352
Cdd:cd20956    9 SEQTLQPGPSVSLKCVASGNPLPQITWT-----LDGFPIP----ESPRFRVGDYVTSD-GDVVSYVniSSVRVEDGGEYT 78
                         90
                 ....*....|
gi 672059488 353 CEATNAGGKA 362
Cdd:cd20956   79 CTATNDVGSV 88
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
285-364 2.40e-04

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 39.47  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 285 LQVACQASGYPQPLVVWRKmlqprDGkpqaqVQL-EGGApglgGHATRDtgsGMLFLTNITLAHAGKYECEATNAGGKAR 363
Cdd:cd05746    1 VQIPCSAQGDPEPTITWNK-----DG-----VQVtESGK----FHISPE---GYLAIRDVGVADQGRYECVARNTIGYAS 63

                 .
gi 672059488 364 V 364
Cdd:cd05746   64 V 64
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
268-370 3.20e-04

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


Pssm-ID: 409582  Cd Length: 91  Bit Score: 39.70  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 268 PSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRkmlqpRDGKPqaqVQLEGGAPGLgghaTRDTGSGMLFLTNITLAH 347
Cdd:cd20990    1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQ-----LDGKP---IRPDSAHKML----VRENGVHSLIIEPVTSRD 68
                         90       100
                 ....*....|....*....|...
gi 672059488 348 AGKYECEATNAGGKARVLFHLLV 370
Cdd:cd20990   69 AGIYTCIATNRAGQNSFNLELVV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
273-360 3.95e-04

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 39.31  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 273 EPPELTANLGEDLQVACQAS-GYPQPLVVWRKmlqprDGKPQAqvqleggapgLGGHATRDTGSGMLFLTNITLAHAGKY 351
Cdd:cd05724    3 EPSDTQVAVGEMAVLECSPPrGHPEPTVSWRK-----DGQPLN----------LDNERVRIVDDGNLLIAEARKSDEGTY 67

                 ....*....
gi 672059488 352 ECEATNAGG 360
Cdd:cd05724   68 KCVATNMVG 76
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
278-366 6.03e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 39.19  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 278 TANLGEDLQVACQASGYPQPLVVWRKM-----LQPRDGKPQAQVQLEGgapglgghatrDTGSGMLFLTNITLAHAGKYE 352
Cdd:cd05870   12 TTVENGAATLSCKAEGEPIPEITWKRAsdghtFSEGDKSPDGRIEVKG-----------QHGESSLHIKDVKLSDSGRYD 80
                         90
                 ....*....|....*
gi 672059488 353 CEA-TNAGGKARVLF 366
Cdd:cd05870   81 CEAaSRIGGHQKSMY 95
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
274-362 7.73e-04

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: 38.63  E-value: 7.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 274 PPELTANLGEDLQVACQASGYPQPLVVWR---KMLQPRDGKPQAQvqleggapglgghatRDTGSGMLFLTNITLAHAGK 350
Cdd:cd05744    7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQlngKPVRPDSAHKMLV---------------RENGRHSLIIEPVTKRDAGI 71
                         90
                 ....*....|..
gi 672059488 351 YECEATNAGGKA 362
Cdd:cd05744   72 YTCIARNRAGEN 83
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
281-361 7.75e-04

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 38.69  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 281 LGEDLQVACQASGYPQPLVVWRKmlqprDGKPQaqvqleggAPGLGGHATRDTGSgmLFLTNITLAHAGKYECEATNAGG 360
Cdd:cd05856   18 VGSSVRLKCVASGNPRPDITWLK-----DNKPL--------TPPEIGENKKKKWT--LSLKNLKPEDSGKYTCHVSNRAG 82

                 .
gi 672059488 361 K 361
Cdd:cd05856   83 E 83
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
267-312 1.18e-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: 38.28  E-value: 1.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 672059488 267 PPSVNAEPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGKP 312
Cdd:cd20957    1 PLSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMK-----DGKP 41
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
57-166 1.34e-03

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 40.80  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  57 PPGTQTLFLQDN------SIAHLEQGALAPLAALRHLYLHNNTLRALESGAFRA---QPRLLELALTGNRLrGLRGGAFV 127
Cdd:cd00116   50 QPSLKELCLSLNetgripRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESllrSSSLQELKLNNNGL-GDRGLRLL 128
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 672059488 128 GLV------QLRVLYLAGNQL----AKLLDFTFLHLPRLQELHLQENSI 166
Cdd:cd00116  129 AKGlkdlppALEKLVLGRNRLegasCEALAKALRANRDLKELNLANNGI 177
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
273-360 1.41e-03

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: 38.01  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488 273 EPPELTANLGEDLQVACQASGYPQPLVVWRKmlqprDGkpqAQVQLEGGAPGLGGHATRDTGSGMLFLTNITLAHAGKYE 352
Cdd:cd05726    5 KPRDQVVALGRTVTFQCETKGNPQPAIFWQK-----EG---SQNLLFPYQPPQPSSRFSVSPTGDLTITNVQRSDVGYYI 76

                 ....*...
gi 672059488 353 CEATNAGG 360
Cdd:cd05726   77 CQALNVAG 84
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-165 2.39e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  61 QTLFLQDNSIAHLEQgaLAPLAALRHLYLHNNTLRALESGAfrAQPRLLELALTGNRLRGLRGGAFVGLVQLRVLYLAGN 140
Cdd:COG4886  231 ETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306
                         90       100
                 ....*....|....*....|....*
gi 672059488 141 QLAKLLDFTFLHLPRLQELHLQENS 165
Cdd:COG4886  307 LLNLLELLILLLLLTTLLLLLLLLK 331
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
89-213 3.35e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.92  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672059488  89 LHNNTLRALESGAFRAQPRLLELALTGNRlrglrggAFVGLVQLRVLYLAGNQLAKlLDFTFLHLPRLQELHLQENSI-- 166
Cdd:COG4886   79 LLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTD-LPEELANLTNLKELDLSNNQLtd 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 672059488 167 -----------ELLEdqalaglsslalldLSRNQLGTISKEaLQPLSSLQVLRLTENP 213
Cdd:COG4886  151 lpeplgnltnlKSLD--------------LSNNQLTDLPEE-LGNLTNLKELDLSNNQ 193
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
131-164 5.77e-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: 34.91  E-value: 5.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 672059488  131 QLRVLYLAGNQLAKLldFTFLHLPRLQELHLQEN 164
Cdd:pfam12799   2 NLEVLDLSNNQITDI--PPLAKLPNLETLDLSGN 33
 
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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