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Conserved domains on  [gi|1207193658|ref|XP_021329535|]
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leucine-rich repeat neuronal protein 3 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-276 3.06e-22

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.01  E-value: 3.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  56 NDLGLLTLPERLPSDTQVLLSQANSIAKidspldyLVNLTEVDLSRNNISSLSDiYIGHIPQLLSLHLEENWLSSLHDNf 135
Cdd:COG4886    84 LLLLGLTDLGDLTNLTELDLSGNEELSN-------LTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPEP- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 136 LAHFPNLQELYVNHNLLSLISAEaFQGLNKLLRLHLNSNQLRAIrSEWFQDLSQLEILMIGENPIARIqNMNFKPLINLR 215
Cdd:COG4886   155 LGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLE 231

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 216 SLVLTRMNLTEIPDsaLVGLDKLESVSFYDNMFPKVPqaALRQVRNLKFLDLNKNPIERIQ 276
Cdd:COG4886   232 TLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLP--PLANLTNLKTLDLSNNQLTDLK 288
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 421-513 3.77e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05764:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 88  Bit Score: 62.49  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 421 PLISPESlpDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGeKILPqmDSKKYHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:cd05764     1 PLITRHT--HELRVLEGQRATLRCKARGDPEPAIHWISPEG-KLIS--NSSRTLVYDNGTLDILITTVKDTGAFTCIASN 75

                          90
                  ....*....|...
gi 1207193658 501 LIGVDMRSVLVIV 513
Cdd:cd05764    76 PAGEATARVELHI 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 526-591 2.52e-06

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.34  E-value: 2.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 526 HIQVENTEPNSVSISWVPPK--GSLVSN--IKWSTNSQHHSLQFTSHVVsNVKKFNLTNLHSLTQYEVCV 591
Cdd:cd00063     6 NLRVTDVTSTSVTLSWTPPEddGGPITGyvVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRV 74
LRRCT smart00082
Leucine rich repeat C-terminal domain;
368-412 2.86e-05

Leucine rich repeat C-terminal domain;


:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.03  E-value: 2.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1207193658  368 NPIYCDCVIRWI-NMNNTRVRFMELDALLCAGPSEFEGRLVKQVHS 412
Cdd:smart00082   1 NPFICDCELRWLlRWLQANEHLQDPVDLRCASPSSLRGPLLELLHS 46
LRR_8 pfam13855
Leucine rich repeat;
309-370 8.43e-05

Leucine rich repeat;


:

Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 8.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193658 309 PELTKIEATNNpRLSYIHPNAFSQLPRLESLMLNSNALRALHHITVESLPNLQEVSIHSNPI 370
Cdd:pfam13855   1 PNLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-276 3.06e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.01  E-value: 3.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  56 NDLGLLTLPERLPSDTQVLLSQANSIAKidspldyLVNLTEVDLSRNNISSLSDiYIGHIPQLLSLHLEENWLSSLHDNf 135
Cdd:COG4886    84 LLLLGLTDLGDLTNLTELDLSGNEELSN-------LTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPEP- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 136 LAHFPNLQELYVNHNLLSLISAEaFQGLNKLLRLHLNSNQLRAIrSEWFQDLSQLEILMIGENPIARIqNMNFKPLINLR 215
Cdd:COG4886   155 LGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLE 231

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 216 SLVLTRMNLTEIPDsaLVGLDKLESVSFYDNMFPKVPqaALRQVRNLKFLDLNKNPIERIQ 276
Cdd:COG4886   232 TLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLP--PLANLTNLKTLDLSNNQLTDLK 288
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 421-513 3.77e-12

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 62.49  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 421 PLISPESlpDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGeKILPqmDSKKYHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:cd05764     1 PLITRHT--HELRVLEGQRATLRCKARGDPEPAIHWISPEG-KLIS--NSSRTLVYDNGTLDILITTVKDTGAFTCIASN 75

                          90
                  ....*....|...
gi 1207193658 501 LIGVDMRSVLVIV 513
Cdd:cd05764    76 PAGEATARVELHI 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 429-500 3.96e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.20  E-value: 3.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWvTPSGEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 429-513 1.20e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGVDMRS 508
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 1207193658  509 VLVIV 513
Cdd:smart00410  81 TTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
140-200 3.62e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.99  E-value: 3.62e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 140 PNLQELYVNHNLLSLISAEAFQGLNKLLRLHLNSNQLRAIRSEWFQDLSQLEILMIGENPI 200
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 72-277 1.08e-08

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: 55.95  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  72 QVLLSQANSIAKIDSpLDYLVNLTEVDLSRNNISSLsdiyighipqllslhleENwlsslhdnfLAHFPNLQELYVNHNL 151
Cdd:cd21340    27 KVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKI-----------------EN---------LENLVNLKKLYLGGNR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 152 LSLIsaEAFQGLNKLLRLHLNSNQL----------RAIRSewfqdLSQ-LEILMIGENpiaRIQNMN-FKPLINLRSLVL 219
Cdd:cd21340    80 ISVV--EGLENLTNLEELHIENQRLppgekltfdpRSLAA-----LSNsLRVLNISGN---NIDSLEpLAPLRNLEQLDA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193658 220 TRMNLTEIpdsalvglDKLESVsfydnmfpkvpqaaLRQVRNLKFLDLNKNPIERIQR 277
Cdd:cd21340   150 SNNQISDL--------EELLDL--------------LSSWPSLRELDLTGNPVCKKPK 185
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
28-324 5.06e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.16  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  28 VCLKLCKCEIRPWFSPlsmyNEAPTVDCNDLGLLTLPERLPSDTQVLLSQANSIAKIDSPLDYLVNltEVDLSRNNISSL 107
Cdd:PRK15370  183 LRLKILGLTTIPACIP----EQITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQ--EMELSINRITEL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 108 SDiyigHIPQLL-SLHLEENWLSSLHDNflahFPN-LQELYVNHNLLSLISAEAFQGlnkLLRLHLNSNQLRAIRSEWFQ 185
Cdd:PRK15370  257 PE----RLPSALqSLDLFHNKISCLPEN----LPEeLRYLSVYDNSIRTLPAHLPSG---ITHLNVQSNSLTALPETLPP 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 186 DlsqLEILMIGENPIARIQNmNFKPliNLRSLVLTRMNLTEIPDSALVGLDKLE-SVSFYDNMFPKVPQAalrqvrnLKF 264
Cdd:PRK15370  326 G---LKTLEAGENALTSLPA-SLPP--ELQVLDVSKNQITVLPETLPPTITTLDvSRNALTNLPENLPAA-------LQI 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207193658 265 LDLNKNPIERIQRgdfvDMIHLKELGINSMPELVSIDSFA---LHNLPELTKIEATNNPRLSY 324
Cdd:PRK15370  393 MQASRNNLVRLPE----SLPHFRGEGPQPTRIIVEYNPFSertIQNMQRLMSSVGYQGPRVLF 451
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 526-591 2.52e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.34  E-value: 2.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 526 HIQVENTEPNSVSISWVPPK--GSLVSN--IKWSTNSQHHSLQFTSHVVsNVKKFNLTNLHSLTQYEVCV 591
Cdd:cd00063     6 NLRVTDVTSTSVTLSWTPPEddGGPITGyvVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRV 74
LRRCT smart00082
Leucine rich repeat C-terminal domain;
368-412 2.86e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.03  E-value: 2.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1207193658  368 NPIYCDCVIRWI-NMNNTRVRFMELDALLCAGPSEFEGRLVKQVHS 412
Cdd:smart00082   1 NPFICDCELRWLlRWLQANEHLQDPVDLRCASPSSLRGPLLELLHS 46
fn3 pfam00041
Fibronectin type III domain;
527-591 5.80e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 5.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 527 IQVENTEPNSVSISWVPPK--GSLVSN---IKWSTNSQHHSLQFTshVVSNVKKFNLTNLHSLTQYEVCV 591
Cdd:pfam00041   6 LTVTDVTSTSLTVSWTPPPdgNGPITGyevEYRPKNSGEPWNEIT--VPGTTTSVTLTGLKPGTEYEVRV 73
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 526-591 6.45e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 6.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658  526 HIQVENTEPNSVSISWVPPKGSLVSNIK---WSTNSQHHSLQFTSHVVSNVKKFNLTNLHSLTQYEVCV 591
Cdd:smart00060   6 NLRVTDVTSTSVTLSWEPPPDDGITGYIvgyRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRV 74
LRR_8 pfam13855
Leucine rich repeat;
309-370 8.43e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 8.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193658 309 PELTKIEATNNpRLSYIHPNAFSQLPRLESLMLNSNALRALHHITVESLPNLQEVSIHSNPI 370
Cdd:pfam13855   1 PNLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 341-405 1.61e-04

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: 45.46  E-value: 1.61e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658  341 LNSNALRALHHITVESLPNLQEVSIHSNPIYCDC----VIRWINMNNTRVRFMEldALLCAGPSEFEGR 405
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCglarLPRWAEEKGVKVRQPE--AALCAGPGALAGQ 68
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-276 3.06e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.01  E-value: 3.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  56 NDLGLLTLPERLPSDTQVLLSQANSIAKidspldyLVNLTEVDLSRNNISSLSDiYIGHIPQLLSLHLEENWLSSLHDNf 135
Cdd:COG4886    84 LLLLGLTDLGDLTNLTELDLSGNEELSN-------LTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPEP- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 136 LAHFPNLQELYVNHNLLSLISAEaFQGLNKLLRLHLNSNQLRAIrSEWFQDLSQLEILMIGENPIARIqNMNFKPLINLR 215
Cdd:COG4886   155 LGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLE 231

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 216 SLVLTRMNLTEIPDsaLVGLDKLESVSFYDNMFPKVPqaALRQVRNLKFLDLNKNPIERIQ 276
Cdd:COG4886   232 TLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLP--PLANLTNLKTLDLSNNQLTDLK 288
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
52-246 6.19e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.83  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  52 TVDCNDLGLLTLPERLPSDT--QVLLSQANSIAKIDSPLDYLVNLTEVDLSRNNISSLSDIyIGHIPQLLSLHLEENWLS 129
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLTnlKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQIT 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 130 SLHDNfLAHFPNLQELYVNHNLLSLISAEaFQGLNKLLRLHLNSNQLRAIrsEWFQDLSQLEILMIGENPIARIQnmNFK 209
Cdd:COG4886   196 DLPEP-LGNLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLTDL--PELGNLTNLEELDLSNNQLTDLP--PLA 269

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207193658 210 PLINLRSLVLTRMNLTEIPDSALVGLDKLESVSFYDN 246
Cdd:COG4886   270 NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-360 6.41e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.44  E-value: 6.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  60 LLTLPERLPSDTQVLLSQANSIAKIDSPLDYLVNLTEVDLSRNNISSLSDIYIGHIPQLLSLHLEENwlsslhdNFLAHF 139
Cdd:COG4886    40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 140 PNLQELYVNHNLLSLISAEaFQGLNKLLRLHLNSNQLRAIrSEWFQDLSQLEILMIGENPIARIQNmNFKPLINLRSLVL 219
Cdd:COG4886   113 TNLESLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 220 TRMNLTEIPDSaLVGLDKLESVSFYDNMFPKVPqAALRQVRNLKFLDLNKNPIERIqrgdfvdmihlkelginsmPElvs 299
Cdd:COG4886   190 SNNQITDLPEP-LGNLTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDL-------------------PE--- 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 300 idsfaLHNLPELTKIEATNNpRLSYIHPNAfsQLPRLESLMLNSNALRALHHITVESLPNL 360
Cdd:COG4886   246 -----LGNLTNLEELDLSNN-QLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGL 298
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
55-370 3.09e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 81.52  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  55 CNDLGLLTLPERLPSDTQVLLSQANSIAKIDSPLDYLVNLTEVDLSRNNISSLSDIYIGHIPQLLSLHLEENWLSSLHDN 134
Cdd:COG4886     5 LLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 135 FLAHFPNLQELyVNHNLLSLISAEAFQGLNKLLRLHLNSNQLRAIrSEWFQDLSQLEILMIGENPIARIQNmNFKPLINL 214
Cdd:COG4886    85 LLLGLTDLGDL-TNLTELDLSGNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 215 RSLVLTRMNLTEIPDSaLVGLDKLESVSFYDNMFPKVPqAALRQVRNLKFLDLNKNPIERIqrgdfvdmihlkelginsm 294
Cdd:COG4886   162 KSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL------------------- 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193658 295 pelvsidSFALHNLPELTKIEATNNpRLSYIhpNAFSQLPRLESLMLNSNALRALHHITveSLPNLQEVSIHSNPI 370
Cdd:COG4886   221 -------PEPLANLTNLETLDLSNN-QLTDL--PELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQL 284
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 421-513 3.77e-12

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 62.49  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 421 PLISPESlpDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGeKILPqmDSKKYHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:cd05764     1 PLITRHT--HELRVLEGQRATLRCKARGDPEPAIHWISPEG-KLIS--NSSRTLVYDNGTLDILITTVKDTGAFTCIASN 75

                          90
                  ....*....|...
gi 1207193658 501 LIGVDMRSVLVIV 513
Cdd:cd05764    76 PAGEATARVELHI 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 429-500 3.96e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.20  E-value: 3.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWvTPSGEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPPTITW-YKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
93-370 5.77e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.04  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  93 NLTEVDLSRNNISSLSDIYIGHIPQLLSLHLEENWLSSLHDNFLAHFPNLQELYVNHNLLSLISAEAFQGLNKLLRLHLN 172
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 173 SNQLRAIRSEWFQDLSQLEILMIGENPiariqnmNFKPLINLRSLVLTRMNLTEIPDSaLVGLDKLESVSFYDNMFPKVP 252
Cdd:COG4886    81 LLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 253 qAALRQVRNLKFLDLNKNPIERIqrgdfvdmihlkelginsmpelvsidSFALHNLPELTKIEATNNpRLSYIhPNAFSQ 332
Cdd:COG4886   153 -EPLGNLTNLKSLDLSNNQLTDL--------------------------PEELGNLTNLKELDLSNN-QITDL-PEPLGN 203

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1207193658 333 LPRLESLMLNSNALRALhHITVESLPNLQEVSIHSNPI 370
Cdd:COG4886   204 LTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQL 240
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 429-513 1.20e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGVDMRS 508
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 1207193658  509 VLVIV 513
Cdd:smart00410  81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
429-513 1.60e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.04  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPsGEKILPqmdSKKYHLHPEG---TFDIYGITENEAGQYTCVAHNLIGVD 505
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRS---SDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATNSAGEA 82


                  ....*...
gi 1207193658 506 MRSVLVIV 513
Cdd:pfam07679  83 EASAELTV 90
LRR_8 pfam13855
Leucine rich repeat;
140-200 3.62e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.99  E-value: 3.62e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 140 PNLQELYVNHNLLSLISAEAFQGLNKLLRLHLNSNQLRAIRSEWFQDLSQLEILMIGENPI 200
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 440-503 4.68e-10

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: 56.18  E-value: 4.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207193658 440 VSLHCRAFADPEPEIYWVTPsGEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIG 503
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKN-GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
LRR_8 pfam13855
Leucine rich repeat;
116-176 5.20e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.61  E-value: 5.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193658 116 PQLLSLHLEENWLSSLHDNFLAHFPNLQELYVNHNLLSLISAEAFQGLNKLLRLHLNSNQL 176
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 428-513 3.24e-09

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


Pssm-ID: 409561  Cd Length: 92  Bit Score: 54.32  E-value: 3.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 428 LPDQVNVGTGHLVSLHCRAFADPEPEIYWVTPsGEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGVDMR 507
Cdd:cd20969     8 KAQQVFVDEGHTVQFVCRADGDPPPAILWLSP-RKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSM 86


                  ....*.
gi 1207193658 508 SVLVIV 513
Cdd:cd20969    87 PAHLHV 92
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 440-506 4.52e-09

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: 53.34  E-value: 4.52e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 440 VSLHCRAFADPEPEIYWvTPSGEKIlpqMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIG---VDM 506
Cdd:cd05746     1 VQIPCSAQGDPEPTITW-NKDGVQV---TESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGyasVSM 66
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 72-277 1.08e-08

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: 55.95  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  72 QVLLSQANSIAKIDSpLDYLVNLTEVDLSRNNISSLsdiyighipqllslhleENwlsslhdnfLAHFPNLQELYVNHNL 151
Cdd:cd21340    27 KVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKI-----------------EN---------LENLVNLKKLYLGGNR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 152 LSLIsaEAFQGLNKLLRLHLNSNQL----------RAIRSewfqdLSQ-LEILMIGENpiaRIQNMN-FKPLINLRSLVL 219
Cdd:cd21340    80 ISVV--EGLENLTNLEELHIENQRLppgekltfdpRSLAA-----LSNsLRVLNISGN---NIDSLEpLAPLRNLEQLDA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193658 220 TRMNLTEIpdsalvglDKLESVsfydnmfpkvpqaaLRQVRNLKFLDLNKNPIERIQR 277
Cdd:cd21340   150 SNNQISDL--------EELLDL--------------LSSWPSLRELDLTGNPVCKKPK 185
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 429-506 1.54e-08

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: 52.16  E-value: 1.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWvtpsgEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGVDM 506
Cdd:cd04968     8 PADTYALKGQTVTLECFALGNPVPQIKW-----RKVDGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKDT 80
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 421-510 3.93e-08

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. 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: 409363  Cd Length: 102  Bit Score: 51.65  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 421 PLISPESLPDQ-VNVGTGhlVSLHCRAFADPEPEIYWV-------TPSGEKILPQMDS-KKYHLHPEG---TFDIYGITE 488
Cdd:cd04974     1 PILQAGLPANQtVVLGSD--VEFHCKVYSDAQPHIQWLkhvevngSKYGPDGLPYVTVlKVAGVNTTGeenTLTISNVTF 78

                          90       100
                  ....*....|....*....|..
gi 1207193658 489 NEAGQYTCVAHNLIGVDMRSVL 510
Cdd:cd04974    79 DDAGEYICLAGNSIGLSFHSAW 100
LRR_8 pfam13855
Leucine rich repeat;
93-152 4.17e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.22  E-value: 4.17e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  93 NLTEVDLSRNNISSLSDIYIGHIPQLLSLHLEENWLSSLHDNFLAHFPNLQELYVNHNLL 152
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 429-512 4.75e-08

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: 50.86  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEkilpqMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIG-VDMR 507
Cdd:cd05725     4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGE-----LPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGkIEAS 78


                  ....*
gi 1207193658 508 SVLVI 512
Cdd:cd05725    79 ATLTV 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 426-513 1.06e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.08  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 426 ESLPDQVNVGTGHLVSLHCRAFADPEPEIYWvTPSGEKIlpQMDSKKYHLHpEGTFDIYGITENEAGQYTCVAHNLIGVD 505
Cdd:cd20978     5 QKPEKNVVVKGGQDVTLPCQVTGVPQPKITW-LHNGKPL--QGPMERATVE-DGTLTIINVQPEDTGYYGCVATNEIGDI 80


                  ....*...
gi 1207193658 506 MRSVLVIV 513
Cdd:cd20978    81 YTETLLHV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 421-500 2.88e-07

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 48.66  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 421 PLISPESLPDQVNVGTGHLVSLHCRAFADPEPEIYWVTpsgEKILPQMDSKKYHLHPEGT-FDIYGITENEAGQYTCVAH 499
Cdd:cd20970     1 PVISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTR---NGNLIIEFNTRYIVRENGTtLTIRNIRRSDMGIYLCIAS 77


                  .
gi 1207193658 500 N 500
Cdd:cd20970    78 N 78
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 429-512 2.98e-07

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 48.79  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEpEIYWVTPSGEKILPQMDSKKYHLHPE--GTFDIYGITENEAGQYTCVAHNLIGVDM 506
Cdd:cd04977     7 PSYAEISVGESKFFLCKVSGDAK-NINWVSPNGEKVLTKHGNLKVVNHGSvlSSLTIYNANINDAGIYKCVATNGKGTES 85


                  ....*.
gi 1207193658 507 RSVLVI 512
Cdd:cd04977    86 EATVKL 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 429-503 3.33e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 48.65  E-value: 3.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWvTPSGEKILPQmdSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIG 503
Cdd:cd20952     6 PQNQTVAVGGTVVLNCQATGEPVPTISW-LKDGVPLLGK--DERITTLENGSLQIKGAEKSDTGEYTCVALNLSG 77
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
28-324 5.06e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.16  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  28 VCLKLCKCEIRPWFSPlsmyNEAPTVDCNDLGLLTLPERLPSDTQVLLSQANSIAKIDSPLDYLVNltEVDLSRNNISSL 107
Cdd:PRK15370  183 LRLKILGLTTIPACIP----EQITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQ--EMELSINRITEL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 108 SDiyigHIPQLL-SLHLEENWLSSLHDNflahFPN-LQELYVNHNLLSLISAEAFQGlnkLLRLHLNSNQLRAIRSEWFQ 185
Cdd:PRK15370  257 PE----RLPSALqSLDLFHNKISCLPEN----LPEeLRYLSVYDNSIRTLPAHLPSG---ITHLNVQSNSLTALPETLPP 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 186 DlsqLEILMIGENPIARIQNmNFKPliNLRSLVLTRMNLTEIPDSALVGLDKLE-SVSFYDNMFPKVPQAalrqvrnLKF 264
Cdd:PRK15370  326 G---LKTLEAGENALTSLPA-SLPP--ELQVLDVSKNQITVLPETLPPTITTLDvSRNALTNLPENLPAA-------LQI 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207193658 265 LDLNKNPIERIQRgdfvDMIHLKELGINSMPELVSIDSFA---LHNLPELTKIEATNNPRLSY 324
Cdd:PRK15370  393 MQASRNNLVRLPE----SLPHFRGEGPQPTRIIVEYNPFSertIQNMQRLMSSVGYQGPRVLF 451
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 428-513 6.61e-07

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: 48.03  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 428 LPDQVNVGTGHLVSLHCRAFADPEPEIYW---VTPSGEKILPqmDSKKYH--LHPEG--TFD-------IYGITENEAGQ 493
Cdd:cd05858     7 LPANTSVVVGTDAEFVCKVYSDAQPHIQWlkhVEKNGSKYGP--DGLPYVevLKTAGvnTTDkeievlyLRNVTFEDAGE 84

                          90       100
                  ....*....|....*....|
gi 1207193658 494 YTCVAHNLIGVDMRSVLVIV 513
Cdd:cd05858    85 YTCLAGNSIGISHHSAWLTV 104
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 428-513 9.14e-07

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 47.60  E-value: 9.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 428 LPDQVNVGTGHLVSLHCRAFADPEPEIYW------VTPSgEKILPQMDSKKYhlhpeGTFDIYGITENEAGQYTCVAHNL 501
Cdd:cd05891     7 LPDVVTIMEGKTLNLTCTVFGNPDPEVIWfkndqdIELS-EHYSVKLEQGKY-----ASLTIKGVTSEDSGKYSINVKNK 80

                          90
                  ....*....|..
gi 1207193658 502 IGVDMRSVLVIV 513
Cdd:cd05891    81 YGGETVDVTVSV 92
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 163-376 2.03e-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: 49.40  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 163 LNKLLRLHLNSNQLRAIrsewfQDLSQ---LEILMIGENPIARIQNMNFkpLINLRSLVLTRMNLTEIPdsalvGLDKLe 239
Cdd:cd21340     1 LKRITHLYLNDKNITKI-----DNLSLcknLKVLYLYDNKITKIENLEF--LTNLTHLYLQNNQIEKIE-----NLENL- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 240 svsfydnmfpkvpqaalrqvRNLKFLDLNKNPIERIQrgDFVDMIHLKELGINS----MPELVSIDSFALHNL-PELTKI 314
Cdd:cd21340    68 --------------------VNLKKLYLGGNRISVVE--GLENLTNLEELHIENqrlpPGEKLTFDPRSLAALsNSLRVL 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658 315 EATNNpRLSYIHPnaFSQLPRLESLMLNSNALRALHHI--TVESLPNLQEVSIHSNPI-----YCDCVI 376
Cdd:cd21340   126 NISGN-NIDSLEP--LAPLRNLEQLDASNNQISDLEELldLLSSWPSLRELDLTGNPVckkpkYRDKII 191
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 526-591 2.52e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.34  E-value: 2.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 526 HIQVENTEPNSVSISWVPPK--GSLVSN--IKWSTNSQHHSLQFTSHVVsNVKKFNLTNLHSLTQYEVCV 591
Cdd:cd00063     6 NLRVTDVTSTSVTLSWTPPEddGGPITGyvVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRV 74
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 428-513 2.72e-06

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 46.04  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 428 LPDQVNVGTGHLVSLHCRAFADPEPEIYWVtpSGEKILPQMD--SKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGVD 505
Cdd:cd05737     7 LPDVVTIMEGKTLNLTCNVWGDPPPEVSWL--KNDQALAFLDhcNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSE 84


                  ....*...
gi 1207193658 506 MRSVLVIV 513
Cdd:cd05737    85 TSDVTVSV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 440-503 3.05e-06

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.91  E-value: 3.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207193658 440 VSLHCRAFADPEPEIYWvtPSGEKILPQmdSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIG 503
Cdd:cd04969    20 VIIECKPKASPKPTISW--SKGTELLTN--SSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFG 79
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 437-503 5.00e-06

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 44.90  E-value: 5.00e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWVTPSGeKILPQMDSKKYHlhpEGTFDIYGITENEAGQYTCVAHNLIG 503
Cdd:cd05876    10 GQSLVLECIAEGLPTPTVKWLRPSG-PLPPDRVKYQNH---NKTLQLLNVGESDDGEYVCLAENSLG 72
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 429-503 6.03e-06

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


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.92  E-value: 6.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEKiLPQMDSKKYHLHPE-GTFDIYGITENEAGQYTCVAHNLIG 503
Cdd:cd05763     6 PHDITIRAGSTARLECAATGHPTPQIAWQKDGGTD-FPAARERRMHVMPEdDVFFIVDVKIEDTGVYSCTAQNSAG 80
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 430-503 6.79e-06

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


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 44.95  E-value: 6.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193658 430 DQVnVGTGHLVSLHCRAFADPEPEIYWVTPSGEKIL----PQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIG 503
Cdd:cd05726     8 DQV-VALGRTVTFQCETKGNPQPAIFWQKEGSQNLLfpyqPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAG 84
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 441-505 7.93e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 44.94  E-value: 7.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193658 441 SLHCRAFADPEPEIYWVTpSGEKILPQMdSKKYHLHPEGT-FDIYGITENEAGQYTCVAHNLIGVD 505
Cdd:cd05736    19 SLRCHAEGIPLPRVQWLK-NGMDINPKL-SKQLTLIANGSeLHISNVRYEDTGAYTCIAKNEGGVD 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 434-513 8.13e-06

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 44.72  E-value: 8.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 434 VGTGHLVSLHCRAFADPEPEIYWVTpSGEKILPQMDSKKYHLHPEG---TFDIYGITENEAGQYTCVAHNLIGVDMRSVL 510
Cdd:cd20951    12 VWEKSDAKLRVEVQGKPDPEVKWYK-NGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAKNIHGEASSSAS 90


                  ...
gi 1207193658 511 VIV 513
Cdd:cd20951    91 VVV 93
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
 436-500 1.80e-05

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.


Pssm-ID: 409534  Cd Length: 116  Bit Score: 44.57  E-value: 1.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193658 436 TGHLVSLHCRAFADPEPEIYWVTPSGE--KILPQM-DSKK---------YHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:cd20940    14 VGDSVELHCEAVGSPIPEIQWWFEGQEpnEICSQLwDGARldrvhinatYHQHATSTISIDNLTEEDTGTYECRASN 90
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 429-504 2.15e-05

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: 43.69  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEKILPQMDSKKYH-LHPEGTFDIYGI-----TENEAGQYTCVAHNLI 502
Cdd:cd07693     7 PSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRiVLPSGSLFFLRVvhgrkGRSDEGVYVCVAHNSL 86


                  ..
gi 1207193658 503 GV 504
Cdd:cd07693    87 GE 88
LRRCT smart00082
Leucine rich repeat C-terminal domain;
368-412 2.86e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.03  E-value: 2.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1207193658  368 NPIYCDCVIRWI-NMNNTRVRFMELDALLCAGPSEFEGRLVKQVHS 412
Cdd:smart00082   1 NPFICDCELRWLlRWLQANEHLQDPVDLRCASPSSLRGPLLELLHS 46
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 420-503 3.87e-05

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: 43.00  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 420 LPLISPESLPDQVNVGTGHLVSLHCRAFADPEPEIYWvTPSGEKIlpQMDSKKYHLHPEGT-FDIYGITENEAGQYTCVA 498
Cdd:cd05730     1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTW-TKDGEPI--ESGEEKYSFNEDGSeMTILDVDKLDEAEYTCIA 77


                  ....*
gi 1207193658 499 HNLIG 503
Cdd:cd05730    78 ENKAG 82
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 437-513 4.19e-05

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 42.23  E-value: 4.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWvTPSGEkilpQMDSKKYHL-HPEGTFDIYGITENEAGQYTCVAHNLIGVDMRSVLVIV 513
Cdd:cd05745     2 GQTVDFLCEAQGYPQPVIAW-TKGGS----QLSVDRRHLvLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
fn3 pfam00041
Fibronectin type III domain;
527-591 5.80e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 5.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 527 IQVENTEPNSVSISWVPPK--GSLVSN---IKWSTNSQHHSLQFTshVVSNVKKFNLTNLHSLTQYEVCV 591
Cdd:pfam00041   6 LTVTDVTSTSLTVSWTPPPdgNGPITGyevEYRPKNSGEPWNEIT--VPGTTTSVTLTGLKPGTEYEVRV 73
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 429-512 5.81e-05

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: 42.30  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEKILPQMDSKK---YHLHPEGTFDIYGITENEAGQYTCVAHNLIGVD 505
Cdd:cd20954     8 PVDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPGEYKDLLYdpnVRILPNGTLVFGHVQKENEGHYLCEAKNGIGSG 87


                  ....*..
gi 1207193658 506 MRSVLVI 512
Cdd:cd20954    88 LSKVIFL 94
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 526-591 6.45e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 6.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658  526 HIQVENTEPNSVSISWVPPKGSLVSNIK---WSTNSQHHSLQFTSHVVSNVKKFNLTNLHSLTQYEVCV 591
Cdd:smart00060   6 NLRVTDVTSTSVTLSWEPPPDDGITGYIvgyRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRV 74
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 440-509 8.15e-05

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(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. 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: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.89  E-value: 8.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207193658 440 VSLHCRAFADPEPEIYWVT-----PSGEKILPQMDSKKYHLHPEgTFDIYGITENEAGQYTCVAHNLIGVDMRSV 509
Cdd:cd05869    20 ITLTCEASGDPIPSITWRTstrniSSEEKTLDGHIVVRSHARVS-SLTLKYIQYTDAGEYLCTASNTIGQDSQSM 93
LRR_8 pfam13855
Leucine rich repeat;
309-370 8.43e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 8.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193658 309 PELTKIEATNNpRLSYIHPNAFSQLPRLESLMLNSNALRALHHITVESLPNLQEVSIHSNPI 370
Cdd:pfam13855   1 PNLRSLDLSNN-RLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_9 pfam14580
Leucine-rich repeat;
171-288 9.04e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 43.60  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 171 LNSNQLRAIrsEWFQDLSQLEILMIGENPIARIQNMNFKPLINLRSLVLTRMNLTEIPD-SALVGLDKLESVSFYDNMFP 249
Cdd:pfam14580  49 FSDNEIRKL--DGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDlDPLASLKKLTFLSLLRNPVT 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207193658 250 KVPQAALR---QVRNLKFLDLNKnpIERIQRGDFVDMIHLKE 288
Cdd:pfam14580 127 NKPHYRLYviyKVPQLRLLDFRK--VKQKERQAAEKMFRSKQ 166
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 437-500 9.57e-05

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


Pssm-ID: 409438  Cd Length: 89  Bit Score: 41.52  E-value: 9.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWvtPSGEKILpqMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHN 500
Cdd:cd05852    17 GGRVIIECKPKAAPKPKFSW--SKGTELL--VNNSRISIWDDGSLEILNITKLDEGSYTCFAEN 76
LRR_8 pfam13855
Leucine rich repeat;
213-272 1.04e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 213 NLRSLVLTRMNLTEIPDSALVGLDKLESVSFYDNMFPKVPQAALRQVRNLKFLDLNKNPI 272
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 341-405 1.61e-04

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: 45.46  E-value: 1.61e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658  341 LNSNALRALHHITVESLPNLQEVSIHSNPIYCDC----VIRWINMNNTRVRFMEldALLCAGPSEFEGR 405
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCglarLPRWAEEKGVKVRQPE--AALCAGPGALAGQ 68
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 56-272 2.12e-04

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: 43.88  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  56 NDLGLLTLPERL---PSDTQVLLSqANSIAKID----SPLDYL---VNLTEVDLSRNNIS-SLSDIYIG--HIPQLLSLH 122
Cdd:cd00116    36 GEEAAKALASALrpqPSLKELCLS-LNETGRIPrglqSLLQGLtkgCGLQELDLSDNALGpDGCGVLESllRSSSLQELK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 123 LEENWLSSLHDNFLA-----HFPNLQELYVNHNLLSLISAEAFqglnkllrlhlnSNQLRAIRSewfqdlsqLEILMIGE 197
Cdd:cd00116   115 LNNNGLGDRGLRLLAkglkdLPPALEKLVLGRNRLEGASCEAL------------AKALRANRD--------LKELNLAN 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658 198 NPI----ARIQNMNFKPLINLRSLVLTRMNLTEIPDSALVGldklesvsfydnmfpkvpqaALRQVRNLKFLDLNKNPI 272
Cdd:cd00116   175 NGIgdagIRALAEGLKANCNLEVLDLNNNGLTDEGASALAE--------------------TLASLKSLEVLNLGDNNL 233
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 429-504 2.14e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.78  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVTPSGEKILPQMDSKKYHLHPEGTFdIYGITENEAGQYTCVAHNLIGV 504
Cdd:cd20949     6 AYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLL-INKVTQDDTGEYTCRAYQVNSI 80
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 429-504 2.79e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 40.52  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWvtpSGEKILPQMDSKKYHLHPEGT----FDIYGITENEAGQYTCVAHNLIGV 504
Cdd:cd05892     7 PQNKKVLEGDPVRLECQISAIPPPQIFW---KKNNEMLQYNTDRISLYQDNCgricLLIQNANKKDAGWYTVSAVNEAGV 83
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 429-504 4.49e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 39.53  E-value: 4.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWVtpSGEKILPQmdSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGV 504
Cdd:cd20968     6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWI--KGDDLIKE--NNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGI 77
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 440-508 6.15e-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: 39.43  E-value: 6.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207193658 440 VSLHCRAFADPEPEIYWVT-----PSGEKILPQMDSKKYHlHPEGTFDIYGITENEAGQYTCVAHNLIGVDMRS 508
Cdd:cd05732    19 ITLTCEAEGDPIPEITWRRatrgiSFEEGDLDGRIVVRGH-ARVSSLTLKDVQLTDAGRYDCEASNRIGGDQQS 91
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 437-513 6.70e-04

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


Pssm-ID: 143259  Cd Length: 88  Bit Score: 39.23  E-value: 6.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWvtpsgEKILPQMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGVDMRSVLVIV 513
Cdd:cd05851    16 GQNVTLECFALGNPVPVIRW-----RKILEPMPATAEISMSGAVLKIFNIQPEDEGTYECEAENIKGKDKHQARVYV 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 429-504 9.39e-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: 39.02  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYW------VTPSGEKILPQMDSKKYHLHpegtfdIYGITENEAGQYTCVAHNLI 502
Cdd:cd05744     7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWqlngkpVRPDSAHKMLVRENGRHSLI------IEPVTKRDAGIYTCIARNRA 80


                  ..
gi 1207193658 503 GV 504
Cdd:cd05744    81 GE 82
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 428-505 9.86e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 38.87  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 428 LPDQVNVGTGHLVSLHCRAFADPE-PEIYWVTPSGEKILP--QMDSKKYHLHPEGTFDIYGITENEAGQYTCVAHNLIGV 504
Cdd:cd05865     6 VPSQGEISVGESKFFLCQVAGEAKdKDISWFSPNGEKLTPnqQRISVVRNDDYSSTLTIYNANIDDAGIYKCVVSNEDEG 85


                  .
gi 1207193658 505 D 505
Cdd:cd05865    86 E 86
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 437-500 1.51e-03

First 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: 409474  Cd Length: 92  Bit Score: 38.15  E-value: 1.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWVTpSGEKILPQMDSKKYHLHPEGTFDIY--GITENEAGQYTCVAHN 500
Cdd:cd05893    15 GMPVTFTCRVAGNPKPKIYWFK-DGKQISPKSDHYTIQRDLDGTCSLHttASTLDDDGNYTIMAAN 79
LRR_8 pfam13855
Leucine rich repeat;
260-346 1.63e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 260 RNLKFLDLNKNPIERIQRGDFVDMIHLKELGINsmpelvsidsfalHNLpeltkieatnnprLSYIHPNAFSQLPRLESL 339
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLS-------------NNL-------------LTTLSPGAFSGLPSLRYL 54


                  ....*..
gi 1207193658 340 MLNSNAL 346
Cdd:pfam13855  55 DLSGNRL 61
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 434-513 1.80e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 37.95  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 434 VGTGHLVSLHCRAFADPEPEIYWVTPSGEkilpQMDSKKYHLHPEGtfDIYGIT-----ENEAGQYTCVAHNLIGVDMRS 508
Cdd:cd20972    13 VAEGSKVRLECRVTGNPTPVVRWFCEGKE----LQNSPDIQIHQEG--DLHSLIiaeafEEDTGRYSCLATNSVGSDTTS 86


                  ....*
gi 1207193658 509 VLVIV 513
Cdd:cd20972    87 AEIFV 91
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 437-513 2.27e-03

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 37.39  E-value: 2.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWVTPSGEkiLPQMDSKKYHLHPegTFDIYGITENEAGQYTCVAHNLIGVDMRSVLVIV 513
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIKLGGE--LPKGRTKFENFNK--TLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 86-145 3.19e-03

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 39.77  E-value: 3.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207193658  86 SPLDYLVNLTEVDLSRNNISSLSDI--YIGHIPQLLSLHLEENWLSSLH---DNFLAHFPNLQEL 145
Cdd:cd21340   136 EPLAPLRNLEQLDASNNQISDLEELldLLSSWPSLRELDLTGNPVCKKPkyrDKIILASKSLEVL 200
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 429-504 4.54e-03

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: 37.14  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 429 PDQVNVGTGHLVSLHCRAFADPEPEIYWvtpsgEKILPqmDSKKYHLHPE-----------GTFDIYGITENEAGQYTCV 497
Cdd:cd05765     7 PTHQTVKVGETASFHCDVTGRPQPEITW-----EKQVP--GKENLIMRPNhvrgnvvvtniGQLVIYNAQPQDAGLYTCT 79


                  ....*..
gi 1207193658 498 AHNLIGV 504
Cdd:cd05765    80 ARNSGGL 86
LRR_9 pfam14580
Leucine-rich repeat;
305-370 5.61e-03

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 38.21  E-value: 5.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193658 305 LHNLPELTKIEA--TNNPRLSYIHPNAFSQLPRLESLMLNSNALRALHHIT-VESLPNLQEVSIHSNPI 370
Cdd:pfam14580  57 LDGFPLLRRLKTllLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDpLASLKKLTFLSLLRNPV 125
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 437-513 7.15e-03

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 36.39  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658 437 GHLVSLHCRAFADPEPEIYWvtpsgEK---ILPqmDSKKYHLHPEGTFDIYGITENE-AGQYTCVAHNLIGV-DMRSVLV 511
Cdd:cd20958    15 GQTLRLHCPVAGYPISSITW-----EKdgrRLP--LNHRQRVFPNGTLVIENVQRSSdEGEYTCTARNQQGQsASRSVFV 87


                  ..
gi 1207193658 512 IV 513
Cdd:cd20958    88 KV 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 93-176 7.54e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.83  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193658  93 NLTEVDLSRNNISSLSDIYIGHIPQLLSLHLEENWLSSLHDNFLAHFPNLQELYVNHNLLSLISAEAFQGLNKLLRLHLN 172
Cdd:PLN00113  476 RLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLS 555


                  ....
gi 1207193658 173 SNQL 176
Cdd:PLN00113  556 QNQL 559
 
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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