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Conserved domains on  [gi|1907155919|ref|XP_036019990|]
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leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 411-500 6.49e-29

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 cd20969:

Pssm-ID: 472250  Cd Length: 92  Bit Score: 110.17  E-value: 6.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 411 KIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20969     3 AIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 82

                          90
                  ....*....|
gi 1907155919 491 NDTFTASLTV 500
Cdd:cd20969    83 NDSMPAHLHV 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-340 2.90e-20

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 93.46  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  48 LLAIPEGIPIETKILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLklvplgvFTG 127
Cdd:COG4886    39 LLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE-------LSN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 128 LSNLTKLDISENKIViLLDYMFQDLHNLKSLEVGDNDLVYIShRAFSGLLSLEQLTLEKCNLTAVPtEALSHLRSLIALH 207
Cdd:COG4886   112 LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 208 LKHLNINNMPvYAFKRLFHLKNLEIDYWPLLDLmpANSLYGL-NLTSLSITNTNLSTVPFLAfkHLVYLTHLNLSYNPIS 286
Cdd:COG4886   189 LSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL--PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLT 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907155919 287 TIEAgmFSDLIRLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENV 340
Cdd:COG4886   264 DLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 327-391 1.65e-05

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


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 48.15  E-value: 1.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919  327 NVSQNLLETLEENVFSSPRALEVLSINNNPLACDCRLLWLLQRQPNLQFGGQQP---MCAGPDTIRER 391
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQ 68
LRRNT smart00013
Leucine rich repeat N-terminal domain;
27-60 2.18e-04

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.84  E-value: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907155919   27 GCPARCECSAQnkSVSCHRRRLLAIPEGIPIETK 60
Cdd:smart00013   1 ACPAPCNCSGT--AVDCSGRGLTEVPLDLPPDTT 32
 
Name Accession Description Interval E-value
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 411-500 6.49e-29

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: 110.17  E-value: 6.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 411 KIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20969     3 AIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 82

                          90
                  ....*....|
gi 1907155919 491 NDTFTASLTV 500
Cdd:cd20969    83 NDSMPAHLHV 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-340 2.90e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 93.46  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  48 LLAIPEGIPIETKILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLklvplgvFTG 127
Cdd:COG4886    39 LLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE-------LSN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 128 LSNLTKLDISENKIViLLDYMFQDLHNLKSLEVGDNDLVYIShRAFSGLLSLEQLTLEKCNLTAVPtEALSHLRSLIALH 207
Cdd:COG4886   112 LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 208 LKHLNINNMPvYAFKRLFHLKNLEIDYWPLLDLmpANSLYGL-NLTSLSITNTNLSTVPFLAfkHLVYLTHLNLSYNPIS 286
Cdd:COG4886   189 LSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL--PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLT 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907155919 287 TIEAgmFSDLIRLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENV 340
Cdd:COG4886   264 DLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315
I-set pfam07679
Immunoglobulin I-set domain;
410-500 2.73e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.69  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIrEKKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRATvlgdgtLEIRFAQDQDSGMYVC 483
Cdd:pfam07679   1 PKF-TQKPKDVEVQEGESARFTCTVTGTPDPEVSWfkdgqpLRSSDRFKVTYEGGTYT------LTISNVQPDDSGKYTC 73

                          90
                  ....*....|....*..
gi 1907155919 484 IASNAAGNDTFTASLTV 500
Cdd:pfam07679  74 VATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 418-500 2.05e-16

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: 74.46  E-value: 2.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKsnGRATVLGDG---TLEIRFAQDQDSGMYVCIASNAAGNDTF 494
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES--GRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASS 79


                   ....*.
gi 1907155919  495 TASLTV 500
Cdd:smart00410  80 GTTLTV 85
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 176-373 5.99e-12

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 65.58  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 176 LLSLEQLTLEKCNLTAVptEALSHLRSLIALHLKhlniNNmpvyafkRLFHLKNLEidywplldlmpANSlyglNLTSLS 255
Cdd:cd21340     1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLY----DN-------KITKIENLE-----------FLT----NLTHLY 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 256 ITNTNLSTVPFLAfkHLVYLTHLNLSYNPISTIEAgmFSDLIRLQELHIVGAQLR-----TIEPHSFQGL-RFLRVLNVS 329
Cdd:cd21340    53 LQNNQIEKIENLE--NLVNLKKLYLGGNRISVVEG--LENLTNLEELHIENQRLPpgeklTFDPRSLAALsNSLRVLNIS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907155919 330 QNLLETLEEnvFSSPRALEVLSINNNPLACDCRLLWLLQRQPNL 373
Cdd:cd21340   129 GNNIDSLEP--LAPLRNLEQLDASNNQISDLEELLDLLSSWPSL 170
LRR_8 pfam13855
Leucine rich repeat;
106-165 7.59e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.92  E-value: 7.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 106 NLRSLRLKGNRLKLVPLGVFTGLSNLTKLDISENKIVILLDYMFQDLHNLKSLEVGDNDL 165
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
39-217 5.94e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 49.31  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  39 KSVSCHRRRLLAIPEGIPIETKILDLSKNRLKSInPEEFISypLLEEIDLSDNIIANVePGAFNNlfNLRSLRLKGNRLK 118
Cdd:PRK15370  223 KTLYANSNQLTSIPATLPDTIQEMELSINRITEL-PERLPS--ALQSLDLFHNKISCL-PENLPE--ELRYLSVYDNSIR 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 119 LVPLGVFTGlsnLTKLDISENKIVILLDYMFQdlhNLKSLEVGDNDLVYISHrafSGLLSLEQLTLEKCNLTAVPtEALS 198
Cdd:PRK15370  297 TLPAHLPSG---ITHLNVQSNSLTALPETLPP---GLKTLEAGENALTSLPA---SLPPELQVLDVSKNQITVLP-ETLP 366

                         170
                  ....*....|....*....
gi 1907155919 199 hlRSLIALHLKHLNINNMP 217
Cdd:PRK15370  367 --PTITTLDVSRNALTNLP 383
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 327-391 1.65e-05

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 48.15  E-value: 1.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919  327 NVSQNLLETLEENVFSSPRALEVLSINNNPLACDCRLLWLLQRQPNLQFGGQQP---MCAGPDTIRER 391
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQ 68
LRRCT smart00082
Leucine rich repeat C-terminal domain;
355-408 1.98e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.03  E-value: 1.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919  355 NPLACDCRLLWLL--QRQPNLQFGGQQPMCAGPDTIRERSFKDFHSTalsfyFTCK 408
Cdd:smart00082   1 NPFICDCELRWLLrwLQANEHLQDPVDLRCASPSSLRGPLLELLHSE-----FKCP 51
LRRNT smart00013
Leucine rich repeat N-terminal domain;
27-60 2.18e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.84  E-value: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907155919   27 GCPARCECSAQnkSVSCHRRRLLAIPEGIPIETK 60
Cdd:smart00013   1 ACPAPCNCSGT--AVDCSGRGLTEVPLDLPPDTT 32
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 27-56 5.27e-04

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


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 37.61  E-value: 5.27e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907155919  27 GCPARCECSAqnKSVSCHRRRLLAIPEGIP 56
Cdd:pfam01462   1 ACPVPCHCSA--TVVNCSDRGLTAVPRDLP 28
 
Name Accession Description Interval E-value
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 411-500 6.49e-29

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: 110.17  E-value: 6.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 411 KIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20969     3 AIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 82

                          90
                  ....*....|
gi 1907155919 491 NDTFTASLTV 500
Cdd:cd20969    83 NDSMPAHLHV 92
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 415-500 1.30e-20

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: 86.38  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSngRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTF 494
Cdd:cd05764     5 RHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSS--RTLVYDNGTLDILITTVKDTGAFTCIASNPAGEATA 82


                  ....*.
gi 1907155919 495 TASLTV 500
Cdd:cd05764    83 RVELHI 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-340 2.90e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 93.46  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  48 LLAIPEGIPIETKILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLklvplgvFTG 127
Cdd:COG4886    39 LLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE-------LSN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 128 LSNLTKLDISENKIViLLDYMFQDLHNLKSLEVGDNDLVYIShRAFSGLLSLEQLTLEKCNLTAVPtEALSHLRSLIALH 207
Cdd:COG4886   112 LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 208 LKHLNINNMPvYAFKRLFHLKNLEIDYWPLLDLmpANSLYGL-NLTSLSITNTNLSTVPFLAfkHLVYLTHLNLSYNPIS 286
Cdd:COG4886   189 LSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL--PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLT 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907155919 287 TIEAgmFSDLIRLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENV 340
Cdd:COG4886   264 DLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-357 1.16e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.53  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  60 KILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLKLVPLGVFTGLSNLTKLDISEN 139
Cdd:COG4886    27 LLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 140 KivilldyMFQDLHNLKSLEVGDNDLVYISHrAFSGLLSLEQLTLEKCNLTAVPtEALSHLRSLIALHLKHLNINNMPVy 219
Cdd:COG4886   107 E-------ELSNLTNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPE- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 220 AFKRLFHLKNLEIDYWPLLDLmpANSLYGL-NLTSLSITNTNLSTVPfLAFKHLVYLTHLNLSYNPISTIEAgmFSDLIR 298
Cdd:COG4886   177 ELGNLTNLKELDLSNNQITDL--PEPLGNLtNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLPE--LGNLTN 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155919 299 LQELHIVGAQLRTIEPHSfqGLRFLRVLNVSQNLLETLEENVFSSPRALEVLSINNNPL 357
Cdd:COG4886   252 LEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
I-set pfam07679
Immunoglobulin I-set domain;
410-500 2.73e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 82.69  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIrEKKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRATvlgdgtLEIRFAQDQDSGMYVC 483
Cdd:pfam07679   1 PKF-TQKPKDVEVQEGESARFTCTVTGTPDPEVSWfkdgqpLRSSDRFKVTYEGGTYT------LTISNVQPDDSGKYTC 73

                          90
                  ....*....|....*..
gi 1907155919 484 IASNAAGNDTFTASLTV 500
Cdd:pfam07679  74 VATNSAGEAEASAELTV 90
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-356 1.40e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 85.37  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  60 KILDLSKNRLKSInPEEFISYPLLEEIDLSDNIIANVePGAFNNLFNLRSLRLKGNRLKLVPlGVFTGLSNLTKLDISEN 139
Cdd:COG4886   116 ESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 140 KIVILlDYMFQDLHNLKSLEVGDNDLVYIShRAFSGLLSLEQLTLEKCNLTAVPteALSHLRSLIALHLKHLNINNMPVy 219
Cdd:COG4886   193 QITDL-PEPLGNLTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPP- 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 220 afkrLFHLKNLEIdywplldlmpanslygLNLTSLSITNTNLSTVPFLAFKHLVYLTHLNLSYNPISTIEAGMFSDLIRL 299
Cdd:COG4886   268 ----LANLTNLKT----------------LDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLL 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 300 QELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENVFSSPRALEVLSINNNP 356
Cdd:COG4886   328 LLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLAL 384
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 409-487 1.50e-17

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 77.61  E-value: 1.50e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155919 409 KPKIREKKlQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASN 487
Cdd:pfam13927   1 KPVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 418-500 2.05e-16

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: 74.46  E-value: 2.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKsnGRATVLGDG---TLEIRFAQDQDSGMYVCIASNAAGNDTF 494
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES--GRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASS 79


                   ....*.
gi 1907155919  495 TASLTV 500
Cdd:smart00410  80 GTTLTV 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 418-500 4.18e-16

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: 73.68  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITtkSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd20952     7 QNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLG--KDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAV 84


                  ...
gi 1907155919 498 LTV 500
Cdd:cd20952    85 LDV 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 412-500 3.05e-15

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: 70.89  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 412 IREKKLQHLLVDegQTVQLECNADGDPQPVISWvtprRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGN 491
Cdd:cd05725     1 VKRPQNQVVLVD--DSAEFQCEVGGDPVPTVRW----RKEDGELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGK 74


                  ....*....
gi 1907155919 492 DTFTASLTV 500
Cdd:cd05725    75 IEASATLTV 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 428-490 6.93e-14

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: 66.58  E-value: 6.93e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907155919 428 VQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 410-500 1.71e-13

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: 66.26  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFitTKSNGRATVlGDGTLEIRFAQDQDSGMYVCIASNAA 489
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL--QGPMERATV-EDGTLTIINVQPEDTGYYGCVATNEI 77

                          90
                  ....*....|.
gi 1907155919 490 GNDTFTASLTV 500
Cdd:cd20978    78 GDIYTETLLHV 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
134-357 3.31e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.89  E-value: 3.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 134 LDISENKIVILLDYMFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEKCNLTAVPTEALSHLRSLIALHLKHLNI 213
Cdd:COG4886     2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 214 NNMPVYAFKRLFHLKNLEidywpLLDLMPANSLYGL-NLTSLSITNTNLSTVPFlAFKHLVYLTHLNLSYNPISTIEAGm 292
Cdd:COG4886    82 LSLLLLGLTDLGDLTNLT-----ELDLSGNEELSNLtNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPEP- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907155919 293 FSDLIRLQELHIVGAQLRTIePHSFQGLRFLRVLNVSQNLLETLEEnVFSSPRALEVLSINNNPL 357
Cdd:COG4886   155 LGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQL 217
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 422-490 1.58e-12

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: 63.68  E-value: 1.58e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 422 VDEGQTVQLECNADGDPQPVISWVTPRRRFITTksNGRATVLGDGT-LEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20970    14 AREGENATFMCRAEGSPEPEISWTRNGNLIIEF--NTRYIVRENGTtLTIRNIRRSDMGIYLCIASNGVP 81
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-285 3.08e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.81  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  60 KILDLSKNRLKSInPEEFISYPLLEEIDLSDNIIANVePGAFNNLFNLRSLRLKGNRLKLVPlgVFTGLSNLTKLDISEN 139
Cdd:COG4886   185 KELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNN 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 140 KIVILLDymFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEkcNLTAVPTEALSHLRSLIALHLKHLNINNMPVY 219
Cdd:COG4886   261 QLTDLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLL--LLLLNLLELLILLLLLTTLLLLLLLLKGLLVT 336

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919 220 AFKRLFHLKNLEIDYWPLLDLMPANSLYGLNLTSLSITNTNLSTVPFLAFKHLVYLTHLNLSYNPI 285
Cdd:COG4886   337 LTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 421-500 3.55e-12

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: 62.48  E-value: 3.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 421 LVDEGQTVQLECNADGDPQPVISWvtpRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLTV 500
Cdd:cd04969    13 LAAKGGDVIIECKPKASPKPTISW---SKGTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 176-373 5.99e-12

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 65.58  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 176 LLSLEQLTLEKCNLTAVptEALSHLRSLIALHLKhlniNNmpvyafkRLFHLKNLEidywplldlmpANSlyglNLTSLS 255
Cdd:cd21340     1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLY----DN-------KITKIENLE-----------FLT----NLTHLY 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 256 ITNTNLSTVPFLAfkHLVYLTHLNLSYNPISTIEAgmFSDLIRLQELHIVGAQLR-----TIEPHSFQGL-RFLRVLNVS 329
Cdd:cd21340    53 LQNNQIEKIENLE--NLVNLKKLYLGGNRISVVEG--LENLTNLEELHIENQRLPpgeklTFDPRSLAALsNSLRVLNIS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907155919 330 QNLLETLEEnvFSSPRALEVLSINNNPLACDCRLLWLLQRQPNL 373
Cdd:cd21340   129 GNNIDSLEP--LAPLRNLEQLDASNNQISDLEELLDLLSSWPSL 170
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 425-492 1.30e-11

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 61.35  E-value: 1.30e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907155919 425 GQTVQLECNADGDPQPVISWVTPRRRFI-----TTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGND 492
Cdd:cd05734    16 GKAVVLNCSADGYPPPTIVWKHSKGSGVpqfqhIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCKVSNDVGAD 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 425-501 1.58e-11

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: 60.50  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 425 GQTVQLECNADGDPQPVISWV-----TPRRRFITTKSNGratvlgdgTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLT 499
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIklggeLPKGRTKFENFNK--------TLKIENVSEADSGEYQCTASNTMGSARHTISVT 81


                  ..
gi 1907155919 500 VK 501
Cdd:cd05731    82 VE 83
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 410-500 2.42e-11

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: 60.25  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHLLVDEGQTVQLECNADGDPQPVISWV----TPRRRFITTKSNGratvlgdgTLEIRFAQDQDSGMYVCIA 485
Cdd:cd04968     1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRkvdgSPSSQWEITTSEP--------VLEIPNVQFEDEGTYECEA 72

                          90
                  ....*....|....*
gi 1907155919 486 SNAAGNDTFTASLTV 500
Cdd:cd04968    73 ENSRGKDTVQGRIIV 87
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 425-490 3.72e-11

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 59.43  E-value: 3.72e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907155919 425 GQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRatvlgdGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWrlnwghVPDSARVSITSEGGY------GTLTIRDVKESDQGAYTCEAINTRG 66
LRR_8 pfam13855
Leucine rich repeat;
106-165 7.59e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.92  E-value: 7.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 106 NLRSLRLKGNRLKLVPLGVFTGLSNLTKLDISENKIVILLDYMFQDLHNLKSLEVGDNDL 165
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 424-500 7.74e-11

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: 58.41  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 424 EGQTVQLECNADGDPQPVISWvtprrrfitTKSNG------RATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAW---------TKGGSqlsvdrRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQ 71


                  ...
gi 1907155919 498 LTV 500
Cdd:cd05745    72 LTV 74
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 418-490 2.75e-10

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


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 57.33  E-value: 2.75e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907155919 418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05738     7 QLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTATSNGRIKQLRSGALQIENSEESDQGKYECVATNSAG 79
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 409-500 3.15e-10

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: 57.30  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 409 KPKIR--EKKLQHLLVDEgqtVQLECNADGDPQPVISWVTPRRRFITTKS--NGRATVLGD---GTLEIRFAQDQDSGMY 481
Cdd:cd05869     2 KPKITyvENQTAMELEEQ---ITLTCEASGDPIPSITWRTSTRNISSEEKtlDGHIVVRSHarvSSLTLKYIQYTDAGEY 78

                          90
                  ....*....|....*....
gi 1907155919 482 VCIASNAAGNDTFTASLTV 500
Cdd:cd05869    79 LCTASNTIGQDSQSMYLEV 97
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 409-492 4.06e-10

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: 56.76  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 409 KPKIreKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKS--NGRATVLGD---GTLEIRFAQDQDSGMYVC 483
Cdd:cd05732     2 QPKI--TYLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEGdlDGRIVVRGHarvSSLTLKDVQLTDAGRYDC 79


                  ....*....
gi 1907155919 484 IASNAAGND 492
Cdd:cd05732    80 EASNRIGGD 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 417-500 5.09e-10

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 56.49  E-value: 5.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 417 LQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFitTKSNGRATV-LGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFT 495
Cdd:cd20976     8 PKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL--QYAADRSTCeAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85


                  ....*
gi 1907155919 496 ASLTV 500
Cdd:cd20976    86 AWVTV 90
LRR_8 pfam13855
Leucine rich repeat;
81-141 1.36e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.07  E-value: 1.36e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907155919  81 PLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLKLVPLGVFTGLSNLTKLDISENKI 141
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 425-500 1.51e-09

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 55.10  E-value: 1.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155919 425 GQTVQLECNAD-GDPQPVISWvtpRRRFITTK-SNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG-NDTFTASLTV 500
Cdd:cd05724    12 GEMAVLECSPPrGHPEPTVSW---RKDGQPLNlDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGeRESRAARLSV 87
LRR_8 pfam13855
Leucine rich repeat;
250-309 2.07e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.68  E-value: 2.07e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 250 NLTSLSITNTNLSTVPFLAFKHLVYLTHLNLSYNPISTIEAGMFSDLIRLQELHIVGAQL 309
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 419-490 2.71e-09

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: 54.48  E-value: 2.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 419 HLLVDEGQTVQLECNADGDPQPVISW---VTPRRRFITTKSNGRATVL--GDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05765     9 HQTVKVGETASFHCDVTGRPQPEITWekqVPGKENLIMRPNHVRGNVVvtNIGQLVIYNAQPQDAGLYTCTARNSGG 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 416-499 3.09e-09

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


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 416 KLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFT 495
Cdd:cd05747     9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQ 88


                  ....
gi 1907155919 496 ASLT 499
Cdd:cd05747    89 FTLT 92
LRR_8 pfam13855
Leucine rich repeat;
298-357 3.28e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.30  E-value: 3.28e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 298 RLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENVFSSPRALEVLSINNNPL 357
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 62-288 5.82e-09

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 5.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  62 LDLSKNRLKSInpEEFISYPLLEEIDLSDNIIANVEpgAFNNLFNLRSLRLKGNRL-KLVPLGvftGLSNLTKLDISENK 140
Cdd:cd21340     7 LYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQIeKIENLE---NLVNLKKLYLGGNR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 141 IVILldymfQDLHNLKSLEvgdnDLvYISH-RAFSGllslEQLTLEKCNLTAvptealshlrslIALHLKHLNI--NNMP 217
Cdd:cd21340    80 ISVV-----EGLENLTNLE----EL-HIENqRLPPG----EKLTFDPRSLAA------------LSNSLRVLNIsgNNID 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907155919 218 VYAFkrLFHLKNLEIdywplldlmpanslygLNLTSLSITN-TNLSTVpflaFKHLVYLTHLNLSYNPISTI 288
Cdd:cd21340   134 SLEP--LAPLRNLEQ----------------LDASNNQISDlEELLDL----LSSWPSLRELDLTGNPVCKK 183
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 416-501 5.87e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first 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: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.51  E-value: 5.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 416 KLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGT--LEIRFAQDQDSGMYVCIASNAAGNDT 493
Cdd:cd20974     6 PLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRakLSIPAVTKANSGRYSLTATNGSGQAT 85


                  ....*...
gi 1907155919 494 FTASLTVK 501
Cdd:cd20974    86 STAELLVL 93
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 416-502 6.24e-09

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: 53.42  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 416 KLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFI-----TTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05726     5 KPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLlfpyqPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAG 84

                          90
                  ....*....|..
gi 1907155919 491 NDTFTASLTVKG 502
Cdd:cd05726    85 SILAKAQLEVTD 96
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 428-499 6.25e-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: 52.57  E-value: 6.25e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907155919 428 VQLECNADGDPQPVISWVtprRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLT 499
Cdd:cd05746     1 VQIPCSAQGDPEPTITWN---KDGVQVTESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
LRR_8 pfam13855
Leucine rich repeat;
275-333 6.44e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.14  E-value: 6.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155919 275 LTHLNLSYNPISTIEAGMFSDLIRLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLL 333
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 415-500 7.62e-09

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: 52.97  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRF-----ITTKSNGratvlGDGTLEIRFAQDQDSGMYVCIASNAA 489
Cdd:cd20972     6 QKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELqnspdIQIHQEG-----DLHSLIIAEAFEEDTGRYSCLATNSV 80

                          90
                  ....*....|.
gi 1907155919 490 GNDTFTASLTV 500
Cdd:cd20972    81 GSDTTSAEIFV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 415-500 7.70e-09

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: 53.27  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGratvlGDGTLEIRFAQDQDSGMYVCIASNA 488
Cdd:cd05744     5 QAPGDLEVQEGRLCRFDCKVSGLPTPDLFWqlngkpVRPDSAHKMLVREN-----GRHSLIIEPVTKRDAGIYTCIARNR 79

                          90
                  ....*....|..
gi 1907155919 489 AGNDTFTASLTV 500
Cdd:cd05744    80 AGENSFNAELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 415-500 1.43e-08

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 52.19  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSngratvlGDG--TLEIRFAQDQDSGMYVCIAS 486
Cdd:cd20973     2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWmkddnpIVESRRFQIDQD-------EDGlcSLIISDVCGDDSGKYTCKAV 74

                          90
                  ....*....|....
gi 1907155919 487 NAAGNDTFTASLTV 500
Cdd:cd20973    75 NSLGEATCSAELTV 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 425-501 1.72e-08

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: 52.26  E-value: 1.72e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919 425 GQTVQLECNADGDPQPVISWVTpRRRFITTKSNGRATVLGDGT-LEIRFAQDQDSGMYVCIASNAAGNDTFTASLTVK 501
Cdd:cd05736    15 GVEASLRCHAEGIPLPRVQWLK-NGMDINPKLSKQLTLIANGSeLHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVE 91
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 414-500 1.83e-08

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 51.83  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 414 EKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFittKSNGRATVLGdGTLEIRFAQDQDSGMYVCIASNAAGNDT 493
Cdd:cd05728     3 LKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPL---ASENRIEVEA-GDLRITKLSLSDSGMYQCVAENKHGTIY 78


                  ....*..
gi 1907155919 494 FTASLTV 500
Cdd:cd05728    79 ASAELAV 85
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 410-500 2.18e-08

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: 52.17  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKlQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRA--TVLGDGTLeiRFAQ-------DQDSGM 480
Cdd:cd07693     1 PRIVEHP-SDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRShrIVLPSGSL--FFLRvvhgrkgRSDEGV 77

                          90       100
                  ....*....|....*....|.
gi 1907155919 481 YVCIASNAAGNDT-FTASLTV 500
Cdd:cd07693    78 YVCVAHNSLGEAVsRNASLEV 98
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 410-500 2.29e-08

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 51.74  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHllVDEGQTVQLECNADGD-PQPVISWVT-----PRRRFITTK-SNGRatvlGDGTLEIRFAQDQDSGMYV 482
Cdd:cd05750     1 PKLKEMKSQT--VQEGSKLVLKCEATSEnPSPRYRWFKdgkelNRKRPKNIKiRNKK----KNSELQINKAKLEDSGEYT 74

                          90
                  ....*....|....*...
gi 1907155919 483 CIASNAAGNDTFTASLTV 500
Cdd:cd05750    75 CVVENILGKDTVTGNVTV 92
IgI_2_Dscam cd20953
Second immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 410-500 3.14e-08

Second 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 second immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. 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: 409545  Cd Length: 95  Bit Score: 51.39  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIR-EKKLQHLLVDEGQTVQLECNADGDPQPVISWVtprrRFITTKSNGRATVLGD------GTLEIRFAQDQDSGMYV 482
Cdd:cd20953     2 PKIPgLSKSQPLTVSSASSIALLCPAQGYPAPSFRWY----KFIEGTTRKQAVVLNDrvkqvsGTLIIKDAVVEDSGKYL 77

                          90
                  ....*....|....*...
gi 1907155919 483 CIASNAAGNDTFTASLTV 500
Cdd:cd20953    78 CVVNNSVGGESVETVLTV 95
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 419-501 3.69e-08

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 51.07  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 419 HLLVDEGQTVQLECNADGDPQPVISWvtprRRFITTKSNGRATVLG-DGTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd05876     4 SLVALRGQSLVLECIAEGLPTPTVKW----LRPSGPLPPDRVKYQNhNKTLQLLNVGESDDGEYVCLAENSLGSARHAYY 79


                  ....
gi 1907155919 498 LTVK 501
Cdd:cd05876    80 VTVE 83
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 415-500 5.28e-08

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: 50.70  E-value: 5.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISWV--------TPRRRFITTKSNgratvlgDGTLEIRFAQDQDSGMYVCIAS 486
Cdd:cd05763     4 KTPHDITIRAGSTARLECAATGHPTPQIAWQkdggtdfpAARERRMHVMPE-------DDVFFIVDVKIEDTGVYSCTAQ 76

                          90
                  ....*....|....
gi 1907155919 487 NAAGNDTFTASLTV 500
Cdd:cd05763    77 NSAGSISANATLTV 90
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 424-490 5.37e-08

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 50.70  E-value: 5.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 424 EGQTVQLECNADGDPQPVISWVtprRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20968    13 EGLKAVLPCTTMGNPKPSVSWI---KGDDLIKENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLG 76
LRR_8 pfam13855
Leucine rich repeat;
129-189 6.56e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.45  E-value: 6.56e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907155919 129 SNLTKLDISENKIVILLDYMFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEKCNL 189
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
60-117 6.89e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.45  E-value: 6.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919  60 KILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRL 117
Cdd:pfam13855   4 RSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 414-490 9.95e-08

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 49.75  E-value: 9.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 414 EKKLQHLLVDEGQTVQLECNADGDPQPVISWVTpRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd04978     3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRL-NGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 411-494 1.36e-07

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 49.47  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 411 KIREKKLQHLLvdeGQTVQLECNADGDPQPVISWVTPRRRfITTKSNGRATvLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05856     8 KMRRRVIARPV---GSSVRLKCVASGNPRPDITWLKDNKP-LTPPEIGENK-KKKWTLSLKNLKPEDSGKYTCHVSNRAG 82


                  ....*.
gi 1907155919 491 --NDTF 494
Cdd:cd05856    83 eiNATY 88
IgI_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig ...
 410-490 2.15e-07

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. 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 lacks a C" strand.


Pssm-ID: 409459  Cd Length: 95  Bit Score: 49.20  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHLLVDEGQTVQLECNADGDPQPVISWvTPRRRFITTKSNGRATVLG-DGTLEIRFA----QDQDSGMYVCI 484
Cdd:cd05875     1 PTITKQSAKDYIVDPRDNILIECEAKGNPVPTFHW-TRNGKFFNVAKDPRVSMRRrSGTLVIDFRgggrPEDYEGEYQCF 79


                  ....*.
gi 1907155919 485 ASNAAG 490
Cdd:cd05875    80 ARNKFG 85
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 420-500 3.05e-07

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


Pssm-ID: 409582  Cd Length: 91  Bit Score: 48.56  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 420 LLVDEGQTVQLECNADGDPQPVISWVTPRRRfITTKSNGRATVLGDG--TLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd20990    10 LTVQEGKLCRMDCKVSGLPTPDLSWQLDGKP-IRPDSAHKMLVRENGvhSLIIEPVTSRDAGIYTCIATNRAGQNSFNLE 88


                  ...
gi 1907155919 498 LTV 500
Cdd:cd20990    89 LVV 91
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 425-501 3.49e-07

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: 48.48  E-value: 3.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 425 GQTVQLECNADGDPQPVISWvtprRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLTVK 501
Cdd:cd05851    16 GQNVTLECFALGNPVPVIRW----RKILEPMPATAEISMSGAVLKIFNIQPEDEGTYECEAENIKGKDKHQARVYVQ 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 418-501 3.85e-07

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


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 48.30  E-value: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFIttkSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAgnDTFTAS 497
Cdd:cd20957     9 PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLG---HSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDG--DSAQAT 83


                  ....
gi 1907155919 498 LTVK 501
Cdd:cd20957    84 AELK 87
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 416-500 4.92e-07

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: 47.84  E-value: 4.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 416 KLQHLLVDEGQTVQLECNADGDPQPVISWvtPRRRFITTKSNGRATVLGDGT----LEIRFAQDQDSGMYVCIASNAAGN 491
Cdd:cd05892     6 KPQNKKVLEGDPVRLECQISAIPPPQIFW--KKNNEMLQYNTDRISLYQDNCgricLLIQNANKKDAGWYTVSAVNEAGV 83


                  ....*....
gi 1907155919 492 DTFTASLTV 500
Cdd:cd05892    84 VSCNARLDV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 423-500 5.07e-07

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: 48.00  E-value: 5.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155919 423 DEGQTVQLECNADGDPQPVISWvTPRRRFITTKSNgRATVLGDGT-LEIRFAQDQDSGMYVCIASNAAGNDTFTASLTV 500
Cdd:cd05730    16 NLGQSVTLACDADGFPEPTMTW-TKDGEPIESGEE-KYSFNEDGSeMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 422-490 6.32e-07

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: 47.69  E-value: 6.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919 422 VDEGQTVQLECNADGDPQPVISWvtpRRRFITT-------KSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20954    13 VAAGQDVMLHCQADGFPTPTVTW---KKATGSTpgeykdlLYDPNVRILPNGTLVFGHVQKENEGHYLCEAKNGIG 85
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 404-500 7.37e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 47.60  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 404 YFTckKPKIREKKLQHLLVdeGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDG-TLEIRFAQDQDSGMYV 482
Cdd:cd05729     2 RFT--DTEKMEEREHALPA--ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYT 77

                          90
                  ....*....|....*...
gi 1907155919 483 CIASNAAGNDTFTASLTV 500
Cdd:cd05729    78 CIVENEYGSINHTYDVDV 95
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 420-498 8.53e-07

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.19  E-value: 8.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 420 LLVDEGQTVQLECNA-DGDPQPVISWVTPRRRFIT-TKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:pfam00047   6 VTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIEsLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTS 85


                  .
gi 1907155919 498 L 498
Cdd:pfam00047  86 L 86
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 415-501 9.10e-07

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: 47.42  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISW----------VTPRRRFITTKSngratvlGDGTLEIRFAQDQDSGMYVCI 484
Cdd:cd20951     5 IRLQSHTVWEKSDAKLRVEVQGKPDPEVKWykngvpidpsSIPGKYKIESEY-------GVHVLHIRRVTVEDSAVYSAV 77

                          90
                  ....*....|....*..
gi 1907155919 485 ASNAAGNDTFTASLTVK 501
Cdd:cd20951    78 AKNIHGEASSSASVVVE 94
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 402-500 1.33e-06

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


Pssm-ID: 409438  Cd Length: 89  Bit Score: 46.53  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 402 SFYFTCKKPKIrekklqhlLVDEGQTVQLECNADGDPQPVISWVTPRRRFIttkSNGRATVLGDGTLEIRFAQDQDSGMY 481
Cdd:cd05852     2 TFEFNPMKKKI--------LAAKGGRVIIECKPKAAPKPKFSWSKGTELLV---NNSRISIWDDGSLEILNITKLDEGSY 70

                          90
                  ....*....|....*....
gi 1907155919 482 VCIASNAAGNDTFTASLTV 500
Cdd:cd05852    71 TCFAENNRGKANSTGVLSV 89
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 410-500 1.45e-06

Sixth 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 sixth 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: 409551  Cd Length: 94  Bit Score: 46.72  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHLLVDEGQTVQLECN-ADGDPQPVISWVTPRRRFI------TTKSNGRATVLGDGTLEIRFAqdqdsGMYV 482
Cdd:cd20959     2 PRIIPFAFGEGAAQVGMRAQLHCGvPGGDLPLNIRWTLDGQPISddlgitVSRLGRRSSILSIDSLEASHA-----GNYT 76

                          90
                  ....*....|....*...
gi 1907155919 483 CIASNAAGNDTFTASLTV 500
Cdd:cd20959    77 CHARNSAGSASYTAPLTV 94
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 418-495 1.56e-06

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 46.94  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 418 QHLLVDEGQTVQLECNADG-DPQPVISW--------------VTPRRRFITTKSNGRATVLGDG----TLEIRFAQDQDS 478
Cdd:cd00099     6 RSLSVQEGESVTLSCEVSSsFSSTYIYWyrqkpgqgpefliyLSSSKGKTKGGVPGRFSGSRDGtssfSLTISNLQPEDS 85

                          90
                  ....*....|....*..
gi 1907155919 479 GMYVCIASNAAGNDTFT 495
Cdd:cd00099    86 GTYYCAVSESGGTDKLT 102
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 64-302 2.59e-06

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 49.66  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  64 LSKNRLKSInPEEFISYPLLEEIDLSDNIIANVEPGAfnnlfnlrslrlkgnrlkLVPLGVFTGLSNLTKLDISENKIVI 143
Cdd:cd00116    35 LGEEAAKAL-ASALRPQPSLKELCLSLNETGRIPRGL------------------QSLLQGLTKGCGLQELDLSDNALGP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 144 LLDYMFQDLHNLKSLEVGD--NDLVYISHRAFS--GLLS----LEQLTLEKCNLTAVPTEALSH-LRSLIALHLKHLNIN 214
Cdd:cd00116    96 DGCGVLESLLRSSSLQELKlnNNGLGDRGLRLLakGLKDlppaLEKLVLGRNRLEGASCEALAKaLRANRDLKELNLANN 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 215 NMPVYAFKRLFHLknleidywplldlMPANS-LYGLNLTSLSITNTNLStvpFLA--FKHLVYLTHLNLSYNPI-----S 286
Cdd:cd00116   176 GIGDAGIRALAEG-------------LKANCnLEVLDLNNNGLTDEGAS---ALAetLASLKSLEVLNLGDNNLtdagaA 239

                         250
                  ....*....|....*.
gi 1907155919 287 TIEAGMFSDLIRLQEL 302
Cdd:cd00116   240 ALASALLSPNISLLTL 255
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 422-498 2.71e-06

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 45.63  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 422 VDEGQTVQLECNA-DGDPQPVISWvtprrrfitTKSNG----RATVLGdGTLEIRFAQDQDSGMYVCIASNAAGNDTFTA 496
Cdd:cd05754    13 VRPGADVSFICRAkSKSPAYTLVW---------TRVNGtlpsRAMDFN-GILTIRNVQLSDAGTYVCTGSNMLDTDEATA 82


                  ..
gi 1907155919 497 SL 498
Cdd:cd05754    83 TL 84
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 422-500 3.52e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). 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 human APEG-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: 409567  Cd Length: 91  Bit Score: 45.54  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 422 VDEGQTVQLECNADGDPQPVISWVTPR-------RRFITTKSNGRAtvlgdgTLEIRFAQDQDSGMYVCIASNAAGNDTF 494
Cdd:cd20975    12 VREGQDVIMSIRVQGEPKPVVSWLRNRqpvrpdqRRFAEEAEGGLC------RLRILAAERGDAGFYTCKAVNEYGARQC 85


                  ....*.
gi 1907155919 495 TASLTV 500
Cdd:cd20975    86 EARLEV 91
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 425-501 5.70e-06

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: 44.94  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 425 GQTVQLECNADGDPQPvISWVTPRRRFITTKSNGRATVLGDG---TLEIRFAQDQDSGMYVCIASNAAGNdtfTASLTVK 501
Cdd:cd04977    15 GESKFFLCKVSGDAKN-INWVSPNGEKVLTKHGNLKVVNHGSvlsSLTIYNANINDAGIYKCVATNGKGT---ESEATVK 90
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
39-217 5.94e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 49.31  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  39 KSVSCHRRRLLAIPEGIPIETKILDLSKNRLKSInPEEFISypLLEEIDLSDNIIANVePGAFNNlfNLRSLRLKGNRLK 118
Cdd:PRK15370  223 KTLYANSNQLTSIPATLPDTIQEMELSINRITEL-PERLPS--ALQSLDLFHNKISCL-PENLPE--ELRYLSVYDNSIR 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 119 LVPLGVFTGlsnLTKLDISENKIVILLDYMFQdlhNLKSLEVGDNDLVYISHrafSGLLSLEQLTLEKCNLTAVPtEALS 198
Cdd:PRK15370  297 TLPAHLPSG---ITHLNVQSNSLTALPETLPP---GLKTLEAGENALTSLPA---SLPPELQVLDVSKNQITVLP-ETLP 366

                         170
                  ....*....|....*....
gi 1907155919 199 hlRSLIALHLKHLNINNMP 217
Cdd:PRK15370  367 --PTITTLDVSRNALTNLP 383
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 425-500 5.95e-06

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 425 GQTVQLECNADGDPQPVISWV--------TPRRR---FITtkSNGRATvlgdGTLEIRFAQDQDSGMYVCIASNAAGNDT 493
Cdd:cd20956    16 GPSVSLKCVASGNPLPQITWTldgfpipeSPRFRvgdYVT--SDGDVV----SYVNISSVRVEDGGEYTCTATNDVGSVS 89


                  ....*..
gi 1907155919 494 FTASLTV 500
Cdd:cd20956    90 HSARINV 96
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 242-343 8.11e-06

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


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 45.61  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 242 PANSLYGLNLTSLSITNtNLSTVPFLAFKHLVYLTHLNLSYNpISTIEAGMFSDlIRLQELHIvGAQLRTIEPHSFQGLR 321
Cdd:pfam13306   4 GSYAFYNCSLTSITIPS-SLTSIGEYAFSNCTSLKSITLPSS-LTSIGSYAFYN-CSLTSITI-PSSLTSIGEYAFSNCS 79

                          90       100
                  ....*....|....*....|..
gi 1907155919 322 FLRVLNVSQNlLETLEENVFSS 343
Cdd:pfam13306  80 NLKSITLPSN-LTSIGSYAFSN 100
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 427-498 8.61e-06

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


Pssm-ID: 409417  Cd Length: 95  Bit Score: 44.53  E-value: 8.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155919 427 TVQLECNADGDPQPVISWVtprrRFITTKSNGRATVL---GDGTLEIRFAQDQDSGMYVCIASNAAG----NDTFTASL 498
Cdd:cd05760    18 RVTLRCHIDGHPRPTYQWF----RDGTPLSDGQGNYSvssKERTLTLRSAGPDDSGLYYCCAHNAFGsvcsSQNFTLSI 92
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 425-500 9.30e-06

First 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 first 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 all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 44.50  E-value: 9.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919 425 GQTVQLECNADGDPQpVISWVtprRRFITTKSNGRATVLGDgTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLTV 500
Cdd:cd04973    24 GDLLQLRCRLRDDVQ-SINWT---KDGVQLGENNRTRITGE-EVQIKDAVPRDSGLYACVTSSPSGSDTTYFSVNV 94
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 410-500 1.39e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 44.07  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLqhLLVDEGQTVQLECNADGDPQPVISWVTPRRRFittKSNGRAtvlgdGTLEIRFAQDQ---------DSGM 480
Cdd:cd05857     6 PEKMEKKL--HAVPAANTVKFRCPAAGNPTPTMRWLKNGKEF---KQEHRI-----GGYKVRNQHWSlimesvvpsDKGN 75

                          90       100
                  ....*....|....*....|
gi 1907155919 481 YVCIASNAAGNDTFTASLTV 500
Cdd:cd05857    76 YTCVVENEYGSINHTYHLDV 95
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 327-391 1.65e-05

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 48.15  E-value: 1.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919  327 NVSQNLLETLEENVFSSPRALEVLSINNNPLACDCRLLWLLQRQPNLQFGGQQP---MCAGPDTIRER 391
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQ 68
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 418-501 1.68e-05

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 44.18  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 418 QHLLVDEGQTVQLECNADGDPQPVISW-----------VTPRRRFITTKSNGRATV-----LGDGTLEIRFAQDQDSGMY 481
Cdd:cd04983     6 QSLSVQEGENVTLNCNYSTSTFYYLFWyrqypgqgpqfLIYISSDSGNKKKGRFSAtldksRKSSSLHISAAQLSDSAVY 85

                          90       100
                  ....*....|....*....|....
gi 1907155919 482 VCIASNAAGND--TFTA--SLTVK 501
Cdd:cd04983    86 FCALSESGGTGklTFGKgtRLTVE 109
LRRCT smart00082
Leucine rich repeat C-terminal domain;
355-408 1.98e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 42.03  E-value: 1.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919  355 NPLACDCRLLWLL--QRQPNLQFGGQQPMCAGPDTIRERSFKDFHSTalsfyFTCK 408
Cdd:smart00082   1 NPFICDCELRWLLrwLQANEHLQDPVDLRCASPSSLRGPLLELLHSE-----FKCP 51
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 410-490 2.42e-05

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. 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 lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 43.16  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHLLVDEGQTVQLECNADGDPQPVISWvTPRRRFITTKSNGRATVLGD-GTLEIRFAQ---DQDSGMYVCIA 485
Cdd:cd05733     1 PTITEQSPKDYIVDPRDNITIKCEAKGNPQPTFRW-TKDGKFFDPAKDPRVSMRRRsGTLVIDNHNggpEDYQGEYQCYA 79


                  ....*
gi 1907155919 486 SNAAG 490
Cdd:cd05733    80 SNELG 84
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
 421-501 2.74e-05

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


Pssm-ID: 409398  Cd Length: 101  Bit Score: 43.25  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 421 LVDEGQTVQLECNADGDPQPVISW------VTPR---RRFITTKSNGRATVlgdGTLEIRFAQDQDSGMYVCIASNAAGN 491
Cdd:cd05735    14 LATKGQKKEMSCTAHGEKPIIVRWekedtiINPSemsRYLVTTKEVGDEVI---STLQILPTVREDSGFFSCHAINSYGE 90

                          90
                  ....*....|
gi 1907155919 492 DTFTASLTVK 501
Cdd:cd05735    91 DRGIIQLTVQ 100
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 62-177 3.02e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.15  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  62 LDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLK-LVPLGvFTGLSNLTKLDISENK 140
Cdd:PLN00113  480 LDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSgQIPAS-FSEMPVLSQLDLSQNQ 558

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907155919 141 iviLLDYMFQDLHNLKSLEvgdndLVYISHRAFSGLL 177
Cdd:PLN00113  559 ---LSGEIPKNLGNVESLV-----QVNISHNHLHGSL 587
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 418-490 3.71e-05

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


Pssm-ID: 409454  Cd Length: 89  Bit Score: 42.66  E-value: 3.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907155919 418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDgTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05868     7 TNLVLSPGEDGTLICRANGNPKPSISWLTNGVPIEIAPTDPSRKVDGD-TIIFSKVQERSSAVYQCNASNEYG 78
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
33-289 4.13e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 46.61  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  33 ECSAQNKSVSCHRR-RLLAIPEGIPIETKILDLSKNRLKSInPEEFisYPLLEEIDLSDNIIANVePGAFNNlfNLRSLR 111
Cdd:PRK15370  174 DCLKNNKTELRLKIlGLTTIPACIPEQITTLILDNNELKSL-PENL--QGNIKTLYANSNQLTSI-PATLPD--TIQEME 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 112 LKGNRLKLVPLGVftgLSNLTKLDISENKIVILLDYMFQDlhnLKSLEVGDNDLVYISHRAFSGLLsleQLTLEKCNLTA 191
Cdd:PRK15370  248 LSINRITELPERL---PSALQSLDLFHNKISCLPENLPEE---LRYLSVYDNSIRTLPAHLPSGIT---HLNVQSNSLTA 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 192 VPT-------------EALSHLRSLIALHLKHLNINNMPVYAFKRLF--HLKNLEIDYWPLLDLmPANSLYGLNLtsLSI 256
Cdd:PRK15370  319 LPEtlppglktleageNALTSLPASLPPELQVLDVSKNQITVLPETLppTITTLDVSRNALTNL-PENLPAALQI--MQA 395

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907155919 257 TNTNLSTVPfLAFKHLV----YLTHLNLSYNPIS--TIE 289
Cdd:PRK15370  396 SRNNLVRLP-ESLPHFRgegpQPTRIIVEYNPFSerTIQ 433
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 421-502 4.28e-05

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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: 409359  Cd Length: 102  Bit Score: 42.92  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 421 LVDEGQTVQLECNADGDPQPVISWVTPRRRFIT--TKSNG---RATVLGD-GTLEIRFAQDQDSGMYVCIASNAAGNDTF 494
Cdd:cd04970    13 DITVGENATLQCHASHDPTLDLTFTWSFNGVPIdlEKIEGhyrRRYGKDSnGDLEIVNAQLKHAGRYTCTAQTVVDSDSA 92


                  ....*...
gi 1907155919 495 TASLTVKG 502
Cdd:cd04970    93 SATLVVRG 100
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 415-500 4.52e-05

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


Pssm-ID: 409388  Cd Length: 84  Bit Score: 42.18  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISWVtprrrfittkSNGRATV-------LGDGTLEIRFAQDQDSGMYVCIASN 487
Cdd:cd05723     2 KKPSNIYAHESMDIVFECEVTGKPTPTVKWV----------KNGDVVIpsdyfkiVKEHNLQVLGLVKSDEGFYQCIAEN 71

                          90
                  ....*....|...
gi 1907155919 488 AAGNDTFTASLTV 500
Cdd:cd05723    72 DVGNAQASAQLII 84
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 61-268 4.92e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.38  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  61 ILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLKLVPLGVFTGLSNLTKLDISENK 140
Cdd:PLN00113  360 VLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNN 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 141 IVILLDYMFQDLHNLKSLEVGDNDL---------------VYISHRAFSG--------LLSLEQLTLEKCNLTAVPTEAL 197
Cdd:PLN00113  440 LQGRINSRKWDMPSLQMLSLARNKFfgglpdsfgskrlenLDLSRNQFSGavprklgsLSELMQLKLSENKLSGEIPDEL 519

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919 198 SHLRSLIALHLKHLNINNMPVYAFKRLFHLKNLEIDYWPLLDLMPAN-----SLYGLNLTSLSITNTNLSTVPFLA 268
Cdd:PLN00113  520 SSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKNlgnveSLVQVNISHNHLHGSLPSTGAFLA 595
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
 410-500 6.85e-05

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.90  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQHllVDEGQTVQLECNADGD-PQPVISW------VTPRRRFITTKSNGRAtvlGDGTLEIRFAQDQDSGMYV 482
Cdd:cd05895     1 PKLKEMKSQE--VAAGSKLVLRCETSSEyPSLRFKWfkngkeINRKNKPENIKIQKKK---KKSELRINKASLADSGEYM 75

                          90
                  ....*....|....*...
gi 1907155919 483 CIASNAAGNDTFTASLTV 500
Cdd:cd05895    76 CKVSSKLGNDSASANVTI 93
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 425-487 7.14e-05

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


Pssm-ID: 409387  Cd Length: 97  Bit Score: 42.08  E-value: 7.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907155919 425 GQTVQLECNADGDPQPVISWvtprRR---FITTKSNGRATVLGDGTLEIRFAQDQ-----DSGMYVCIASN 487
Cdd:cd05722    16 GGPVVLNCSAESDPPPKIEW----KKdgvLLNLVSDERRQQLPNGSLLITSVVHSkhnkpDEGFYQCVAQN 82
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 425-500 8.49e-05

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 41.69  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 425 GQTVQLECNADGDPQPVISW---VTP---RRRFITTKSNGRATVLGDGTLEIrfaqDQDSGMYVCIASNAAGNDTFTASL 498
Cdd:cd20971    16 QSNATLVCKVTGHPKPIVKWyrqGKEiiaDGLKYRIQEFKGGYHQLIIASVT----DDDATVYQVRATNQGGSVSGTASL 91


                  ..
gi 1907155919 499 TV 500
Cdd:cd20971    92 EV 93
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 60-115 1.02e-04

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.01  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919  60 KILDLSKNRLKSINPEEFISYplLEEIDLSDNIIANVEP--GAFNNLFNLRSLRLKGN 115
Cdd:cd21340   123 RVLNISGNNIDSLEPLAPLRN--LEQLDASNNQISDLEEllDLLSSWPSLRELDLTGN 178
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-355 1.05e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  51 IPEGIPIETKILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNR-------------- 116
Cdd:PLN00113  134 IPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQlvgqiprelgqmks 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 117 LKLVPLGV----------FTGLSNLTKLDISENKIVILLDYMFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEK 186
Cdd:PLN00113  214 LKWIYLGYnnlsgeipyeIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 187 CNLTAVPTEALSHLRSLIALHLKHLNINNMPVYAFKRLFHLKNLEIDYWPLLDLMPANSLYGLNLTSLSITNTNLS-TVP 265
Cdd:PLN00113  294 NSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEIP 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 266 --FLAFKHLVYLTHLNLSYNPISTIEAGMFSDL--IRLQELHIVGAQlrtiePHSFQGLRFLRVLNVSQN-LLETLEENV 340
Cdd:PLN00113  374 egLCSSGNLFKLILFSNSLEGEIPKSLGACRSLrrVRLQDNSFSGEL-----PSEFTKLPLVYFLDISNNnLQGRINSRK 448

                         330
                  ....*....|....*
gi 1907155919 341 FSSPrALEVLSINNN 355
Cdd:PLN00113  449 WDMP-SLQMLSLARN 462
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 422-500 1.08e-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: 41.16  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 422 VDEGQTVQLECNADGDPQPVISWVTPRRRF-ITTKSNGRATVLGDGTLEIRFAQDqDSGMYVCIASNAAGNDTFTASLTV 500
Cdd:cd20949    11 VKEGQSATILCEVKGEPQPNVTWHFNGQPIsASVADMSKYRILADGLLINKVTQD-DTGEYTCRAYQVNSIASDMQERTV 89
IgI_1_hemolin-like cd20979
First immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 410-490 1.30e-04

First 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 first 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 first 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 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, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM).


Pssm-ID: 409571  Cd Length: 91  Bit Score: 41.02  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 410 PKIREKKLQhLLVDEGQTVQLECNADGDPQPV-ISWVTPRRRFITTKSNgRATVLGDGTLEIRFAQDQDSGMYVCIASNA 488
Cdd:cd20979     1 PVLKEQPAE-VLFREGQPTVLECVTEGGDQGVkYSWLKDGKSFNWQEHN-VAQRKDEGSLVFLKPQASDEGQYQCFAETP 78


                  ..
gi 1907155919 489 AG 490
Cdd:cd20979    79 AG 80
LRR_8 pfam13855
Leucine rich repeat;
154-210 1.38e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 154 NLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEKCNLTAVPTEALSHLRSLIALHLKH 210
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSG 58
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 414-500 1.65e-04

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: 40.85  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 414 EKKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNgratVLGDGTLEIRFAQDQDSGMYVCIASN 487
Cdd:cd05893     4 EMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWfkdgkqISPKSDHYTIQRD----LDGTCSLHTTASTLDDDGNYTIMAAN 79

                          90
                  ....*....|...
gi 1907155919 488 AAGNDTFTASLTV 500
Cdd:cd05893    80 PQGRISCTGRLMV 92
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 83-180 1.66e-04

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


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 41.76  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919  83 LEEIDLSDNIIaNVEPGAFNNlFNLRSLRLkGNRLKLVPLGVFTGLSNLTKLDISENkIVILLDYMFQDLhNLKSLEVGD 162
Cdd:pfam13306  36 LKSITLPSSLT-SIGSYAFYN-CSLTSITI-PSSLTSIGEYAFSNCSNLKSITLPSN-LTSIGSYAFSNC-SLKSITIPS 110

                          90
                  ....*....|....*...
gi 1907155919 163 NdLVYISHRAFSGLLSLE 180
Cdd:pfam13306 111 S-VTTIGSYAFSNCSNLK 127
LRRNT smart00013
Leucine rich repeat N-terminal domain;
27-60 2.18e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.84  E-value: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907155919   27 GCPARCECSAQnkSVSCHRRRLLAIPEGIPIETK 60
Cdd:smart00013   1 ACPAPCNCSGT--AVDCSGRGLTEVPLDLPPDTT 32
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 154-276 2.26e-04

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


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 41.38  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 154 NLKSLEVGDNdLVYISHRAFSGLLSLEQLTLEKcNLTAVPTEALSHlrsliaLHLKHLNINN----MPVYAFKRLFHLKN 229
Cdd:pfam13306  12 SLTSITIPSS-LTSIGEYAFSNCTSLKSITLPS-SLTSIGSYAFYN------CSLTSITIPSsltsIGEYAFSNCSNLKS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907155919 230 LEIdyWPLLDLMPANSLYGLNLTSLSITNtNLSTVPFLAFKHLVYLT 276
Cdd:pfam13306  84 ITL--PSNLTSIGSYAFSNCSLKSITIPS-SVTTIGSYAFSNCSNLK 127
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 420-501 3.06e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 39.82  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 420 LLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGD-GTLEIRFAQDQDSGMYVCIASNAAGNDtfTASL 498
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDlSSFVIEGAEREDEGVYTITVTNPVGED--HASL 82


                  ...
gi 1907155919 499 TVK 501
Cdd:cd05894    83 FVK 85
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 425-500 4.48e-04

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


Pssm-ID: 409444  Cd Length: 105  Bit Score: 39.94  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 425 GQTVQLECNADGDPQPVISWV--------------TPRRRFIttKSNGRATVlgDGTLEIRFAQD---QDSGMYVCIASN 487
Cdd:cd05858    16 GTDAEFVCKVYSDAQPHIQWLkhvekngskygpdgLPYVEVL--KTAGVNTT--DKEIEVLYLRNvtfEDAGEYTCLAGN 91

                          90
                  ....*....|...
gi 1907155919 488 AAGNDTFTASLTV 500
Cdd:cd05858    92 SIGISHHSAWLTV 104
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 424-490 5.09e-04

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 39.54  E-value: 5.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919 424 EGQTVQLECNADGDPQPVISWVTPRRRfITTKSNGRATVLgDGTLEIRFAQD-QDSGMYVCIASNAAG 490
Cdd:cd05848    18 DEKKVILNCEARGNPVPTYRWLRNGTE-IDTESDYRYSLI-DGNLIISNPSEvKDSGRYQCLATNSIG 83
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 425-501 5.19e-04

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 39.47  E-value: 5.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919 425 GQTVQLECNADGDPQPVISWvtpRRRFITTKSNGRATVLGDGTLEIRFAQ-DQDSGMYVCIASNAAGNdTFTASLTVK 501
Cdd:cd20958    15 GQTLRLHCPVAGYPISSITW---EKDGRRLPLNHRQRVFPNGTLVIENVQrSSDEGEYTCTARNQQGQ-SASRSVFVK 88
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 27-56 5.27e-04

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


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 37.61  E-value: 5.27e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907155919  27 GCPARCECSAqnKSVSCHRRRLLAIPEGIP 56
Cdd:pfam01462   1 ACPVPCHCSA--TVVNCSDRGLTAVPRDLP 28
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 415-491 5.30e-04

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


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 39.49  E-value: 5.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155919 415 KKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGdGTLEIRFAQDQDSGMYVCIASNAAGN 491
Cdd:cd05867     4 RRPQSHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSS-GALILTDVQPSDTAVYQCEARNRHGN 79
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 436-501 5.64e-04

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 39.11  E-value: 5.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907155919 436 GDPQPVISW--------VTPRRRFITTKSNgratvlgdGTLEIRFAQDQDSGMYVCIASNAAGNDtfTASLTVK 501
Cdd:cd05748    18 GRPTPTVTWskdgqplkETGRVQIETTASS--------TSLVIKNAKRSDSGKYTLTLKNSAGEK--SATINVK 81
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 432-503 8.24e-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: 8.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907155919 432 CNADGDPQPV-ISWVTPRRRFITTKSNGRATVLGD---GTLEIRFAQDQDSGMYVCIASNAAGNDTfTASLTVKGF 503
Cdd:cd05865    22 CQVAGEAKDKdISWFSPNGEKLTPNQQRISVVRNDdysSTLTIYNANIDDAGIYKCVVSNEDEGES-EATVNVKIF 96
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 425-499 1.21e-03

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: 38.56  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 425 GQTVQLECNADGDPQPVISWV-------TPRRRFITT-----KSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGND 492
Cdd:cd04974    16 GSDVEFHCKVYSDAQPHIQWLkhvevngSKYGPDGLPyvtvlKVAGVNTTGEENTLTISNVTFDDAGEYICLAGNSIGLS 95


                  ....*..
gi 1907155919 493 TFTASLT 499
Cdd:cd04974    96 FHSAWLT 102
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 424-500 1.78e-03

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: 37.97  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 424 EGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRATvlgdgTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd05891    15 EGKTLNLTCTVFGNPDPEVIWfkndqdIELSEHYSVKLEQGKYA-----SLTIKGVTSEDSGKYSINVKNKYGGETVDVT 89


                  ...
gi 1907155919 498 LTV 500
Cdd:cd05891    90 VSV 92
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
 416-490 3.65e-03

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


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 37.26  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155919 416 KLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITT---KS-NGRATV---LGDGTLEIRFAQDQDSGMYVCIASNA 488
Cdd:cd05870     7 QLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSegdKSpDGRIEVkgqHGESSLHIKDVKLSDSGRYDCEAASR 86


                  ..
gi 1907155919 489 AG 490
Cdd:cd05870    87 IG 88
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 424-500 4.36e-03

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: 36.80  E-value: 4.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907155919 424 EGQTVQLECNADGDPQPVISWVTPRRRF-ITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLTV 500
Cdd:cd05737    15 EGKTLNLTCNVWGDPPPEVSWLKNDQALaFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
 
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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